https://teaching.ncl.ac.uk/bms/wiki//index.php?action=history&feed=atom&title=Monoamine_oxidaseMonoamine oxidase - Revision history2026-04-13T10:20:09ZRevision history for this page on the wikiMediaWiki 1.44.0https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13260&oldid=prevNnjm2 at 06:11, 19 October 20152015-10-19T06:11:50Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 06:11, 19 October 2015</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel ''et al.'', 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. and Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong ''et al.'', 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. and Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow and Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel ''et al.'', 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. and Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong ''et al.'', 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. and Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow and Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<del style="font-weight: bold; text-decoration: none;"><br> </del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]] </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in [[Vesicles|vesicles]] are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human [[Brain|brain]] (Shih, Chen &amp; Ridd, 1999; Siegel ''et al.'', 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. and Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. and Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in [[Vesicles|vesicles]] are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human [[Brain|brain]] (Shih, Chen &amp; Ridd, 1999; Siegel ''et al.'', 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. and Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. and Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"><br> </del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent [[Genes|genes]] that are located on the [[X chromosome|X-chromosome]] and they have 70% [[Homology|homology]] (Wu ''et al.'', 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. and Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different [[Polypeptides|polypeptides]] (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. and Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div> </div></td><td colspan="2" class="diff-side-added"></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent [[Genes|genes]] that are located on the [[X chromosome|X-chromosome]] and they have 70% [[Homology|homology]] (Wu ''et al.'', 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. and Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different [[Polypeptides|polypeptides]] (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. and Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td colspan="2" class="diff-side-added"></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>=== References ===</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>=== References ===</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
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</table>Nnjm2https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13228&oldid=prev150015927 at 15:18, 18 October 20152015-10-18T15:18:41Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 15:18, 18 October 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel ''et al.'', 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. <del style="font-weight: bold; text-decoration: none;">&amp;amp;amp;amp;amp;amp;amp; </del>Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong ''et al.'', 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. <del style="font-weight: bold; text-decoration: none;">&amp;amp;amp;amp;amp; </del>Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow <del style="font-weight: bold; text-decoration: none;">&amp;amp;amp;amp;amp; </del>Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel ''et al.'', 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. <ins style="font-weight: bold; text-decoration: none;">and </ins>Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong ''et al.'', 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. <ins style="font-weight: bold; text-decoration: none;">and </ins>Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow <ins style="font-weight: bold; text-decoration: none;">and </ins>Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in [[Vesicles|vesicles]] are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human [[Brain|brain]] (Shih, Chen &amp; Ridd, 1999; Siegel ''et al.'', 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. <del style="font-weight: bold; text-decoration: none;">&amp;amp;amp;amp;amp;amp; </del>Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. <del style="font-weight: bold; text-decoration: none;">&amp;amp;amp;amp;amp;amp;amp; </del>Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in [[Vesicles|vesicles]] are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human [[Brain|brain]] (Shih, Chen &amp; Ridd, 1999; Siegel ''et al.'', 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. <ins style="font-weight: bold; text-decoration: none;">and </ins>Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. <ins style="font-weight: bold; text-decoration: none;">and </ins>Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent [[Genes|genes]] that are located on the [[X chromosome|X-chromosome]] and they have 70% [[Homology|homology]] (Wu ''et al.'', 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. <del style="font-weight: bold; text-decoration: none;">&amp;amp;amp;amp;amp; </del>Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different [[Polypeptides|polypeptides]] (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. <del style="font-weight: bold; text-decoration: none;">&amp;amp;amp;amp;amp;amp; </del>Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent [[Genes|genes]] that are located on the [[X chromosome|X-chromosome]] and they have 70% [[Homology|homology]] (Wu ''et al.'', 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. <ins style="font-weight: bold; text-decoration: none;">and </ins>Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different [[Polypeptides|polypeptides]] (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. <ins style="font-weight: bold; text-decoration: none;">and </ins>Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13225&oldid=prev150015927 at 14:59, 18 October 20152015-10-18T14:59:50Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:59, 18 October 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel ''et al.'', 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong ''et al.'', 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp;amp;amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp;amp;amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel ''et al.'', 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong ''et al.'', 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in [[Vesicles|vesicles]] are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human [[Brain|brain]] (Shih, Chen &amp; Ridd, 1999; Siegel ''et al.'', 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in [[Vesicles|vesicles]] are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human [[Brain|brain]] (Shih, Chen &amp; Ridd, 1999; Siegel ''et al.'', 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent [[Genes|genes]] that are located on the [[<del style="font-weight: bold; text-decoration: none;">X_chromosome</del>|X-chromosome]] and they have 70% homology (Wu ''et al.'', 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp;amp;amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent [[Genes|genes]] that are located on the [[<ins style="font-weight: bold; text-decoration: none;">X chromosome</ins>|X-chromosome]] and they have 70% <ins style="font-weight: bold; text-decoration: none;">[[Homology|</ins>homology<ins style="font-weight: bold; text-decoration: none;">]] </ins>(Wu ''et al.'', 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different <ins style="font-weight: bold; text-decoration: none;">[[Polypeptides|</ins>polypeptides<ins style="font-weight: bold; text-decoration: none;">]] </ins>(Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13224&oldid=prev150015927 at 14:55, 18 October 20152015-10-18T14:55:35Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:55, 18 October 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong et al., 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp;amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp;amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel <ins style="font-weight: bold; text-decoration: none;">''</ins>et al.<ins style="font-weight: bold; text-decoration: none;">''</ins>, 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine [[Neurotransmitter|neurotransmitters]] including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[Enzyme Inhibitors|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong <ins style="font-weight: bold; text-decoration: none;">''</ins>et al.<ins style="font-weight: bold; text-decoration: none;">''</ins>, 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas [[Catecholamines|catecholamines]] are metabolised by MAO<sub>B</sub>. However, 5-HT and [[Catecholamines|catecholamines]] that are stored in <ins style="font-weight: bold; text-decoration: none;">[[Vesicles|</ins>vesicles<ins style="font-weight: bold; text-decoration: none;">]] </ins>are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human <ins style="font-weight: bold; text-decoration: none;">[[Brain|</ins>brain<ins style="font-weight: bold; text-decoration: none;">]] </ins>(Shih, Chen &amp; Ridd, 1999; Siegel <ins style="font-weight: bold; text-decoration: none;">''</ins>et al.<ins style="font-weight: bold; text-decoration: none;">''</ins>, 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp;amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent <ins style="font-weight: bold; text-decoration: none;">[[Genes|</ins>genes<ins style="font-weight: bold; text-decoration: none;">]] </ins>that are located on the <ins style="font-weight: bold; text-decoration: none;">[[X_chromosome|</ins>X-chromosome<ins style="font-weight: bold; text-decoration: none;">]] </ins>and they have 70% homology (Wu <ins style="font-weight: bold; text-decoration: none;">''</ins>et al.<ins style="font-weight: bold; text-decoration: none;">''</ins>, 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13222&oldid=prev150015927 at 14:51, 18 October 20152015-10-18T14:51:14Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:51, 18 October 2015</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[<del style="font-weight: bold; text-decoration: none;">Enzyme_Inhibitors</del>|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong et al., 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in [[Neuron|neurones]], glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine <ins style="font-weight: bold; text-decoration: none;">[[Neurotransmitter|</ins>neurotransmitters<ins style="font-weight: bold; text-decoration: none;">]] </ins>including [[Serotonin|serotonin]] (5-HT) as well as [[Catecholamines|catecholamines]] such as [[Noradrenaline|noradrenaline]] (NA) and [[Dopamine|dopamine]] (DA). Two [[Isoenzyme|isoenzymes]] of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different [[Substrate|substrate]] preference, [[<ins style="font-weight: bold; text-decoration: none;">Enzyme Inhibitors</ins>|inhibitor]] sensitivity and distribution in tissue and [[Brain|brain]] (Tong et al., 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas <ins style="font-weight: bold; text-decoration: none;">[[Catecholamines|</ins>catecholamines<ins style="font-weight: bold; text-decoration: none;">]] </ins>are metabolised by MAO<sub>B</sub>. However, 5-HT and <ins style="font-weight: bold; text-decoration: none;">[[Catecholamines|</ins>catecholamines<ins style="font-weight: bold; text-decoration: none;">]] </ins>that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13207&oldid=prev150015927 at 14:05, 18 October 20152015-10-18T14:05:38Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:05, 18 October 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in <del style="font-weight: bold; text-decoration: none;">neurons</del>, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of [[Mitochondria|mitochondria]] in <ins style="font-weight: bold; text-decoration: none;">[[Neuron|neurones]]</ins>, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including <ins style="font-weight: bold; text-decoration: none;">[[Serotonin|</ins>serotonin<ins style="font-weight: bold; text-decoration: none;">]] </ins>(5-HT) as well as <ins style="font-weight: bold; text-decoration: none;">[[Catecholamines|</ins>catecholamines<ins style="font-weight: bold; text-decoration: none;">]] </ins>such as <ins style="font-weight: bold; text-decoration: none;">[[Noradrenaline|</ins>noradrenaline<ins style="font-weight: bold; text-decoration: none;">]] </ins>(NA) and <ins style="font-weight: bold; text-decoration: none;">[[Dopamine|</ins>dopamine<ins style="font-weight: bold; text-decoration: none;">]] </ins>(DA). Two <ins style="font-weight: bold; text-decoration: none;">[[Isoenzyme|</ins>isoenzymes<ins style="font-weight: bold; text-decoration: none;">]] </ins>of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different <ins style="font-weight: bold; text-decoration: none;">[[Substrate|</ins>substrate<ins style="font-weight: bold; text-decoration: none;">]] </ins>preference, <ins style="font-weight: bold; text-decoration: none;">[[Enzyme_Inhibitors|</ins>inhibitor<ins style="font-weight: bold; text-decoration: none;">]] </ins>sensitivity and distribution in tissue and <ins style="font-weight: bold; text-decoration: none;">[[Brain|</ins>brain<ins style="font-weight: bold; text-decoration: none;">]] </ins>(Tong et al., 2015)<ref name="Tong et al., 2015">Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref name="Wu et al., 2009">Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13206&oldid=prev150015927 at 13:59, 18 October 20152015-10-18T13:59:42Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 13:59, 18 October 2015</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of mitochondria in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<del style="font-weight: bold; text-decoration: none;">amp;amp;</del>amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<del style="font-weight: bold; text-decoration: none;">amp;amp;</del>amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial [[Flavoprotein|flavoprotein]], can be found anchored to the outer membrane of <ins style="font-weight: bold; text-decoration: none;">[[Mitochondria|</ins>mitochondria<ins style="font-weight: bold; text-decoration: none;">]] </ins>in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref <ins style="font-weight: bold; text-decoration: none;">name="Tong et al., 2015"</ins>>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<del style="font-weight: bold; text-decoration: none;">amp;amp;</del>amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref <ins style="font-weight: bold; text-decoration: none;">name="Wu et al., 2009"</ins>>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref name="Shih, Chen & Ridd, 1999">Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13204&oldid=prev150015927 at 13:56, 18 October 20152015-10-18T13:56:44Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 13:56, 18 October 2015</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial flavoprotein, can be found anchored to the outer membrane of mitochondria in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial <ins style="font-weight: bold; text-decoration: none;">[[Flavoprotein|</ins>flavoprotein<ins style="font-weight: bold; text-decoration: none;">]]</ins>, can be found anchored to the outer membrane of mitochondria in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref>Shih, J. C., Chen, K. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref <ins style="font-weight: bold; text-decoration: none;">name="Shih, Chen & Ridd, 1999"</ins>>Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref name="Siegel et al., 2015">Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref>Shih, J. C., Chen, K. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp;amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref <ins style="font-weight: bold; text-decoration: none;">name="Shih, Chen & Ridd, 1999"</ins>>Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13203&oldid=prev150015927 at 13:54, 18 October 20152015-10-18T13:54:41Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 13:54, 18 October 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial flavoprotein, can be found anchored to the outer membrane of mitochondria in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial flavoprotein, can be found anchored to the outer membrane of mitochondria in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref <ins style="font-weight: bold; text-decoration: none;">name="Siegel et al., 2015"</ins>>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref>Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref>Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref <ins style="font-weight: bold; text-decoration: none;">name="Siegel et al., 2015"</ins>>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref>Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref>Shih, J. C., Chen, K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
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</table>150015927https://teaching.ncl.ac.uk/bms/wiki//index.php?title=Monoamine_oxidase&diff=13201&oldid=prev150015927 at 13:43, 18 October 20152015-10-18T13:43:11Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 13:43, 18 October 2015</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial flavoprotein, can be found anchored to the outer membrane of mitochondria in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref <del style="font-weight: bold; text-decoration: none;">name="1"</del>>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref <del style="font-weight: bold; text-decoration: none;">name="2"</del>>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Monoamine oxidase (MAO), an integral mitochondrial flavoprotein, can be found anchored to the outer membrane of mitochondria in neurons, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)<ref>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<ins style="font-weight: bold; text-decoration: none;">amp;</ins>amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>. It plays an important role in metabolising and thus inactivating monoamine neurotransmitters including serotonin (5-HT) as well as catecholamines such as noradrenaline (NA) and dopamine (DA). Two isoenzymes of MAO – MAO<sub>A</sub> and MAO<sub>B</sub> – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)<ref>Tong, J., Meyer, J.H., Furukawa, Y., Boileau, I., Chang, L. J., Wilson, A. A., Houle, S. &amp; Kish, S. J. (2013) Distribution of monoamine oxidase proteins in human brain: implications for brain imaging studies. Journal of Cerebral Blood Flow &amp; Metabolism. [Online] 33(6). p. 863-871. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677103/ [Accessed 18/10/2015]</ref>. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref <del style="font-weight: bold; text-decoration: none;">name="3"</del>>Shih, J. C., Chen, K. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref <del style="font-weight: bold; text-decoration: none;">name="1"</del>>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>5-HT is preferably metabolised by MAO<sub>A</sub> whereas catecholamines are metabolised by MAO<sub>B</sub>. However, 5-HT and catecholamines that are stored in vesicles are be protected from action of MAO. Analyses and assays have also showed that more MAO<sub>B</sub> than MAO<sub>A</sub> are observed in human brain (Shih, Chen &amp; Ridd, 1999; Siegel et al., 2015)<ref>Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref><ref>Siegel, G. J., Agranoff, B. W., Albers, R. W., Fisher, S. K. &amp; Uhler, M. D. (1999) Basic Neurochemistry. [Online] Philadelphia: Lippincott-Raven. Available from: http://www.ncbi.nlm.nih.gov/books/NBK20385/ [Accessed 18/10/2015]</ref>.<br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref <del style="font-weight: bold; text-decoration: none;">name="4"</del>>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref <del style="font-weight: bold; text-decoration: none;">name="3"</del>>Shih, J. C., Chen, K. &<del style="font-weight: bold; text-decoration: none;">amp;</del>amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>MAO<sub>A</sub> and MAO<sub>B</sub> are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)<ref>Wu, J. B., Chen, K., Li, Y., Lau, Y. F. C. &amp; Shih, J. C. (2009) Regulation of monoamine oxidase A by the SRY gene on the Y chromosome. The FASEB Journal. [Online] 23(11). p. 4029-4038. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775015/ [Accessed 18/10/2015]</ref>. Thus, MAO<sub>A</sub> and MAO<sub>B</sub> are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen &amp; Ridd, 1999)<ref>Shih, J. C., Chen, K. &amp; Ridd. M. J. (1999) Monoamine Oxidase: From Genes to Behavior. Annu Rev Neurosci. [Online] 22. p. 197-217. Available from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844879/ [Accessed 18/10/2015]</ref>. </div></td></tr>
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