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| Capsases belong to a subfamily of [[Proteases|proteases]] known as endopeptidases which cleave target [[Protein|proteins]] at specific [[Aspartic acid|aspartic acids]]. They hydrolze petide bonds C-terminally in aspartate residues.<ref>Marks F, Klingmuller U, Muller-Decker K, (2009)fckLRCellular Signalling Processing 1st edition page 465fckLRGarland Science 2009</ref> The caspases have [[Cysteine|cysteine]] at their [[Enzyme active site|active site]] and are named due to the 'C' for [[Cysteine|cysteine]] and the 'asp' for [[Aspartic acid|aspartic acid]]. Caspases are synthesised in the cell as [[Procaspases|procaspases]] <ref>Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science</ref>.<br>
| | See [[Caspases]] |
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| === Capases and [[Apoptosis|Apoptosis]] ===
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| Capases are responsible for the programmed death of a cell. In their inactive state capases are present as zymogens, precapases or blocked by specific capases inhibitors. When [[Javascript:void(0);/*1448212232783*/|apoptosis]] is triggered the capases activate each other forming a cascade. The signal becomes amplified along the cascade and leads to the death of the cell.
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| === References ===
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| <references />
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Latest revision as of 04:24, 23 November 2015