Monoamine oxidase: Difference between revisions
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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; 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, [[ | 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 [[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; 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>. | ||
[[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> | [[Image:MAO.png|center|Two isoforms of monoamine oxidase (MAO) in human - MAO-A and MAO-B]]<br> | ||
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 & 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> | 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 & 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> | ||
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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 & 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>. | 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 & 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>. | ||
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Revision as of 14:51, 18 October 2015
Monoamine oxidase (MAO), an integral mitochondrial flavoprotein, can be found anchored to the outer membrane of mitochondria in neurones, glia and other cells through a transmembrane helix located within the carboxyl-terminal domain (Siegel et al., 2015)[1]. 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 – MAOA and MAOB – have been identified in human, both having different substrate preference, inhibitor sensitivity and distribution in tissue and brain (Tong et al., 2015)[2].
5-HT is preferably metabolised by MAOA whereas catecholamines are metabolised by MAOB. 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 MAOB than MAOA are observed in human brain (Shih, Chen & Ridd, 1999; Siegel et al., 2015)[3][1].
MAOA and MAOB are encoded by two independent genes that are located on the X-chromosome and they have 70% homology (Wu et al., 2009)[4]. Thus, MAOA and MAOB are not the same protein that are modified differently but made up of two different polypeptides (Shih, Chen & Ridd, 1999)[3].
References
- ↑ 1.0 1.1 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]
- ↑ 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]
- ↑ 3.0 3.1 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]
- ↑ 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]