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- W60872003 abstract "Virtually all anticancer drugs induce apoptosis in susceptible cell types. This biochemically distinct form of cell death reflects, in large part, activation of caspases, a distinct family of intracellular cysteine proteases. At least two separable processes, one starting with ligation of specific cell surface receptors (so-called death receptors) and the other involving release of cytochrome c from mitochondria, result in transduction of various signals into caspase activity. The mitochondrial or intrinsic pathway appears to play a predominant role in the apoptotic response to anticancer drugs. Bcl-2 family members regulate this pathway by modulating the release of key proapoptotic polypeptides, including cytochrome c and second mitochondrial activator of caspases (Smac)/direct inhibitor of apoptosis (IAP)-binding protein with low pI (DIABLO), from mitochondria. Several Bcl-2 family members that facilitate mitochondrial permeabilization are transcriptional targets of the p53 tumor suppressor gene, providing a partial explanation for the ability of DNA-damaging agents to induce apoptosis. Other proapoptotic Bcl-2 family members are released from cytoskeletal sites upon treatment with paclitaxel or loss of adherence. The antiapoptotic protein XIAP (X chromosome-linked IAP) binds procaspase 9 and prevents its activation. The gene encoding XIAP is activated by nuclear factor-κB, contributing to the antiapoptotic effects of this transcription factor. In this chapter, the various components of the intrinsic pathway are reviewed, alterations in this pathway in various cancers are described, and evidence that some of these same antiapoptotic alterations might contribute to anticancer drug resistance under certain circumstances is discussed." @default.
- W60872003 created "2016-06-24" @default.
- W60872003 creator A5054370710 @default.
- W60872003 date "2007-10-19" @default.
- W60872003 modified "2023-09-26" @default.
- W60872003 title "The Intrinsic Pathway of Apoptosis" @default.
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