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Home > Art, Film & Photography > EC 3.4.22: Caspase, Cathepsin A, Papain, Bromelain, Cathepsin K, the Proteolysis Map, Cathepsin B, Cysteine Protease, Autophagin, TeV Protease
EC 3.4.22: Caspase, Cathepsin A, Papain, Bromelain, Cathepsin K, the Proteolysis Map, Cathepsin B, Cysteine Protease, Autophagin, TeV Protease

EC 3.4.22: Caspase, Cathepsin A, Papain, Bromelain, Cathepsin K, the Proteolysis Map, Cathepsin B, Cysteine Protease, Autophagin, TeV Protease


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About the Book

Chapters: Caspase, Cathepsin A, Papain, Bromelain, Cathepsin K, the Proteolysis Map, Cathepsin B, Cysteine Protease, Autophagin, Tev Protease, Cancer Procoagulant, Ficain, Clostripain. Source: Wikipedia. Pages: 54. Not illustrated. Free updates online. Purchase includes a free trial membership in the publisher's book club where you can select from more than a million books without charge. Excerpt: Caspases, or cysteine-aspartic proteases or cysteine-dependent aspartate-directed proteases are a family of cysteine proteases, which play essential roles in apoptosis (programmed cell death), necrosis and inflammation. Caspases are essential in cells for apoptosis, or programmed cell death, in development and most other stages of adult life, and have been termed "executioner" proteins for their roles in the cell. Some caspases are also required in the immune system for the maturation of cytokines. Failure of apoptosis is one of the main contributions to tumour development and autoimmune diseases; this coupled with the unwanted apoptosis that occurs with ischemia or Alzheimer's disease, has stimulated interest in caspases as potential therapeutic targets since they were discovered in the mid 1990s. As of November 2009, twelve caspases have been identified in humans. There are two types of apoptotic caspases: initiator (apical) caspases and effector (executioner) caspases. Initiator caspases (e.g. CASP2, CASP8, CASP9 and CASP10) cleave inactive pro-forms of effector caspases, thereby activating them. Effector caspases (e.g. CASP3, CASP6, CASP7) in turn cleave other protein substrates within the cell, to trigger the apoptotic process. The initiation of this cascade reaction is regulated by caspase inhibitors. CASP4 and CASP5, which are overexpressed in some cases of vitiligo and associated autoimmune diseases caused by NALP1 variants, are not currently classified as initiator or effector in MeSH, because they are inflammatory enzymes...More: http: //booksllc.net/?id=29111


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Product Details
  • ISBN-13: 9781155527833
  • Publisher: Books LLC
  • Publisher Imprint: Books LLC
  • Height: 152 mm
  • Sub Title: Caspase, Cathepsin A, Papain, Bromelain, Cathepsin K, the Proteolysis Map, Cathepsin B, Cysteine Protease, Autophagin, TeV Protease
  • Width: 229 mm
  • ISBN-10: 1155527836
  • Publisher Date: 15 Sep 2010
  • Binding: Paperback
  • Spine Width: 3 mm
  • Weight: 95 gr


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EC 3.4.22: Caspase, Cathepsin A, Papain, Bromelain, Cathepsin K, the Proteolysis Map, Cathepsin B, Cysteine Protease, Autophagin, TeV Protease
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