NURSING ANM AND GNM

Detailed explanation-1: -Apoptosis is mediated by proteolytic enzymes called caspases, which trigger cell death by cleaving specific proteins in the cytoplasm and nucleus. Caspases exist in all cells as inactive precursors, or procaspases, which are usually activated by cleavage by other caspases, producing a proteolytic caspase cascade.

Detailed explanation-2: -Caspases, a unique family of cysteine proteases, execute programmed cell death (apoptosis). Caspases exist as inactive zymogens in cells and undergo a cascade of catalytic activation at the onset of apoptosis. The activated caspases are subject to inhibition by the inhibitor-of-apoptosis (IAP) family of proteins.

Detailed explanation-3: -Caspases are a family of cysteine proteases that serve as primary effectors during apoptosis to proteolytically dismantle most cellular structures, including the cytoskeleton, cell junctions, mitochondria, endoplasmic reticulum, Golgi, and the nucleus (Taylor et al., 2008).

Detailed explanation-4: -Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death.

Detailed explanation-5: -Caspases are involved in cell death mediated by apoptosis, pyroptosis, necroptosis and autophagy. Caspase function is not limited to cell death. Non-apoptotic roles of caspases include proliferation, tumor suppression, differentiation, neural development and axon guidance and aging.