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Caspases are a group of cysteine proteases, enzymes that can cleave other proteins. Caspases are essential in cells for apoptosis, one of the main types of programmed cell death in development. Because of their role in tumor suppression and potential application to cancer prevention, interest in caspases has boomed since the 1990s.
Caspases derive their name from cysteine-aspartic-acid-proteases. They initiate apoptosis by cleaving inactive pro-forms of other caspases, thus activating them. These caspases, in turn, start the apoptotic process by cleaving pro-forms of other enzymes. The initiation of that cascade reaction is usually blocked by caspase inhibitors. Induction of apoptosis thus means overexpression of the initial caspases, overcoming the inhibition.
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Caspases were first identified as the enzyme that activates (converts) Interleukin 1-beta (ICE). It is activated by a protease, and the substrates include themselves and other caspases.
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Natural or Synthesized?
Caspases are synthesized as inactive proenzymes.
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