Apoptosis Senescence and Cancer by David A Gewirtz (Editor), Shawn Edan Holt (Editor), Steven

By David A Gewirtz (Editor), Shawn Edan Holt (Editor), Steven Grant (Editor)

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24 Part I / Apoptosis and Alternative Modes of Cell Death 112. Hockenbery DM, Oltvai ZN, Yin X-M, Milliman CL, Korsmeyer SJ. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell 1993; 75:241–52. 113. Bossy-Wetzel E, Newmeyer DD, Green DR. Mitochondrial cytochrome C release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 1998; 17(1):37–49. 114. Ricci JE, Munoz-Pinedo C, Fitzgerald P, et al. Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain.

Instead, mismatch repair-deficient tumors appear to have inactivating mutations in a single BAX allele (249), and it is unclear whether the resulting cells or cell lines completely lack Bax protein. If Bax is incompletely downregulated in human tumors, then models in which Bax is downregulated might be more pertinent to clinical anticancer drug resistance than those containing BAX deletions. Similar comments apply to Bak. Information regarding the role of BH3-only protein alterations in drug resistance is likewise incomplete.

Although many intrinsic pathway components, including Bax, Apaf-1, Bid, and caspase-6, have been identified as p53 transcriptional targets (256–258), gene-targeting studies have identified the BH3-only polypeptides Puma and, to a lesser extent, Noxa, as the most important contributors to p53-induced apoptosis (105–107). It currently appears that Puma plays a predominant role in p53-induced apoptosis after certain DNA-damaging stimuli (106), but further study is required to determine whether similar results are obtained after all types of DNA damage and in all cell types.

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Apoptosis Senescence and Cancer by David A Gewirtz (Editor), Shawn Edan Holt (Editor), Steven
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