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ROLE OF CASPASE IN PROGRAMMED CELL DEATH IN MULTICELLULAR ORGANISMS

DOI: 10.7439/ijbr.v2i7.123

Keywords: Apoptotic protein , Bcl-2 family proteins , Calpain , Interleukin-1β converting enzyme , Cysteine rich protease-caspase

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Abstract:

Apoptosis or programmed cell death is a regulatory process in a multicellular organism that involves aspartate specific cysteine rich protease called caspase are members of the interleukin-1β-converting enzyme family. Apoptosis is induced via two main routes involving either the mitochondria (the intrinsic pathway) or the activation of death receptors (the extrinsic pathway). Both pathways converge to induce the activation of caspases the final executioners of cell death, although, it should be noted that caspase-independent forms of apoptosis have been reported. Ultimately, apoptotic cells are ingested by neighboring cells and phagocytes, preventing inflammation and tissue damage that might ensue upon cell-lysis. The activation and function of caspases, involved in the delicate caspase-cascade system, are regulated by various kinds of molecules, such as the inhibitor of apoptosis protein, Bcl-2 family proteins, calpain and calcium.

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