AP BIOLOGY

Detailed explanation-1: -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-2: -Caspases are enzymes from subclasses of the cysteine-dependent protease family. Their proposed mechanism is to hydrolyze peptide bonds. Caspases are regarded as proenzymes, and their performance depends on activation. Therefore, activation of caspases via mitochondria is of significant importance.

Detailed explanation-3: -The key difference between caspase and procaspase is that caspase is an active protease enzyme that is essential in apoptosis or programmed cell death, while procaspase is an inactive protease enzyme that is an inactive precursor of caspase.

Detailed explanation-4: -Initiator caspases initiate the apoptosis signal while the executioner caspases carry out the mass proteolysis that leads to apoptosis. Inflammatory caspases do not function in apoptosis but are rather involved in inflammatory cytokine signaling and other types of cell death such as pyroptosis.

Detailed explanation-5: -Finally, apoptosis is a coordinated and often energy-dependent process that involves the activation of a group of cysteine proteases called “caspases” and a complex cascade of events that link the initiating stimuli to the final demise of the cell.