Caspases: enemies within.
Apoptosis, an evolutionarily conserved form of cell suicide, requires specialized machinery. The central component of this machinery is a proteolytic system involving a family of proteases called caspases. These enzymes participate in a cascade that is triggered in response to proapoptotic signals and culminates in cleavage of a set of proteins, resulting in disassembly of the cell. Understanding caspase regulation is intimately linked to the ability to rationally manipulate apoptosis for therapeutic gain.
Department of Biochemistry, Merck Research Laboratories, R80W-250, Post Office Box 2000, Rahway, NJ 07065, USA.
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Thornberry
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Lazebnik
D000818:Animals; D017209:Apoptosis; D002384:Catalysis; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000378:metabolism / Q000494:pharmacology / Q000627:therapeutic use; D004358:Drug Therapy; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy; D013379:Substrate Specificity
D015853:Cysteine Proteinase Inhibitors; D004792:Enzyme Precursors; D003546:Cysteine Endopeptidases