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Cathepsins (Ancient Greek ''kata-'' "down" and ''hepsein'' "boil"; abbreviated CTS) are proteases (enzymes that degrade proteins) found in all animals as well as other organisms. There are approximately a dozen members of this family, which are distinguished by their structure, catalytic mechanism, and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. Cathepsins have a vital role in mammalian cellular turnover, e.g. bone resorption. They degrade polypeptides and are distinguished by their substrate specificities. == Classification == * Cathepsin A (serine protease) * Cathepsin B (cysteine protease) * Cathepsin C (cysteine protease) * Cathepsin D (aspartyl protease) * Cathepsin E (aspartyl protease) * Cathepsin F (cysteine proteinase) * Cathepsin G (serine protease) * Cathepsin H (cysteine protease) * Cathepsin K (cysteine protease) * Cathepsin L1 (cysteine protease) * Cathepsin L2 (or V) (cysteine protease) * Cathepsin O (cysteine protease) * Cathepsin S (cysteine protease) * Cathepsin W (cysteine proteinase) * Cathepsin Z (or X) (cysteine protease) 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「cathepsin」の詳細全文を読む スポンサード リンク
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