2000
DOI: 10.1006/excr.2000.5036
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Apoptosis of Mo7e Leukemia Cells Is Associated with the Cleavage of Bcl-2 into a Shortened Fragment That Is Not Functional for Heterodimerization with Bcl-2 and Bax

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Cited by 10 publications
(5 citation statements)
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“…Cleavage of Bcl-2 [66] is a well known factor that may amplify apoptosis [69]. Bax can then undergo conformational changes and translocation to the mitochondria [70]. In addition, cleaved Bcl-2, lacking its N-terminal peptide, may acquire itself a pro-apoptotic function most likely by adapting a Bax-like conformation [71,72].…”
Section: Discussionmentioning
confidence: 99%
“…Cleavage of Bcl-2 [66] is a well known factor that may amplify apoptosis [69]. Bax can then undergo conformational changes and translocation to the mitochondria [70]. In addition, cleaved Bcl-2, lacking its N-terminal peptide, may acquire itself a pro-apoptotic function most likely by adapting a Bax-like conformation [71,72].…”
Section: Discussionmentioning
confidence: 99%
“…Cellular stress induced proapoptotic Bcl-2 family members to translocate from the cytosol to the mitochondria, where they induced the release of cytochrome c, while the antiapoptotic Bcl-2 proteins worked to prevent cytochrome c release from mitochondria, and thereby preserved cell survival (21). Especially, unlike Bcl-2, the cleaved Bcl-2 fragment was no longer functional for dimerization with either Bcl-2 or Bax (23).…”
Section: Discussionmentioning
confidence: 99%
“…The latter phenomenon was at least partially due to the caspase 3-dependent cleavage of Bcl-2 because of the appearance of characteristic 22-kd Bcl-2 fragment, 61 which can further accelerate apoptosis. 62,63 In addition to its antiapoptotic effect, BCR/ABL also regulates the cell cycle. 57 Pim-1 may contribute to this process through phosphorylation and activation of Cdc25A.…”
Section: Discussionmentioning
confidence: 99%