The proteases involved in initiating and carrying out programmed cell death are called as caspases.
A strictly controlled cell dying mechanism known as programmed cell death, or apoptosis, is used by multicellular organisms to eliminate unwanted or dangerous cells. The proteolytic enzymes known as caspases, which cause cell death by cleaving certain proteins in the cytoplasm and nucleus, mediate apoptosis.
All cells contain the inactive precursors of caspases known as procaspases. These procaspases are typically activated by cleavage by other caspases, resulting in a proteolytic caspase cascade. Either extracellular or intracellular death signals trigger the activation process, which results in the accumulation of intracellular adaptor molecules and the activation of procaspases. Bcl-2 and IAP protein family members control the activation of caspase.
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