CELL DIVISION
CELL DIVISION AND CANCEROUS CELLS
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Question
[CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
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BCL-2 inhibits the extrinsic pathway, making procaspase-3 irrelevant in this process
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The apoptosome that is formed in the intrinsic pathway goes on to stimulate the change from procaspase-3 to caspase-3 (executioner)
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SMAC that is released from the mitochondria inhibits the inhibiting function of IAP (inhibits inactive procaspases to turn into active caspases)
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Extrinsic and intrinsic pathways never cross, it is either one or the other
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Detailed explanation-1: -Caspases are crucial mediators of programmed cell death (apoptosis). Among them, caspase-3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins.
Detailed explanation-2: -Caspase 3 controls DNA fragmentation and morphologic changes of apoptosis, whereas caspase 7 plays little role in these processes. In contrast, caspase 7 appears to be more important to the loss of cellular viability, although the combined role of both caspases is crucial in this area.
Detailed explanation-3: -Caspase-3 is cleaved at an aspartate residue to yield a p12 and a p17 subunit to form the active caspase-3 enzyme [13]. Active caspase-3 degrades multiple cellular proteins and is responsible for morphological changes and DNA fragmentation in cells during apoptosis [9].
Detailed explanation-4: -Once activated, caspase-3 will cleave key structural proteins, cell cycle proteins, and DNase proteins, such as poly(ADP-ribose) polymerase, gelsolin, ICAD/DFF, and DNA-dependent kinase11, 12, 13. These cleavage events result in the blebbing and condensing of cells that ultimately leads to cell death14.