
DOI . ORG {
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Title[redir]:
Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event | Oncogene
Description:
The disruption of mitochondrial function is a key component of apoptosis in most cell types. Localization of Bcl-2 to the outer mitochondrial and endoplasmic reticulum membranes is consistent with a role in the inhibition of many forms of apoptosis. In Rat-1 cells, a Bcl-2 mutant targeted exclusively to the endoplasmic reticulum (Bcl-cb5) was effective at inhibiting apoptosis induced by serum starvation/myc, or ceramide but not apoptosis induced by etoposide. The former conditions cause a decrease in mitochondrial transmembrane potential (Δψm) as an early event that precedes the release of cytochrome c from mitochondria. By contrast, when cells are exposed to etoposide, a situation in which cytochrome c release and membrane localization of the pro-apoptotic protein Bax precede loss of Δψm, wild type Bcl-2 but not Bcl-cb5 prevents apoptosis. Therefore, Bcl-2 functions in spatially distinct pathways of apoptosis distinguished by the order of cytochrome c release and loss of Δψm.
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Keywords {🔍}
nature, kroemer, bcl, apoptosis, zamzami, cell, oncogene, article, access, biol, med, susin, content, leber, exp, cookies, cytochrome, andrews, mitochondrial, embo, privacy, endoplasmic, reticulum, zhu, penn, castedo, research, canada, data, open, chem, green, marchetti, wang, advertising, information, journal, subscribe, prevents, event, annis, brian, cells, δψm, release, loss, institution, buy, proteins, bossywetzel,
Topics {✒️}
nature portfolio permissions reprints privacy policy medical research council author information authors advertising 1997 nature med social media 1998 nature 391 2000 nature 403 1997 nature 386 1999 nature 399 nature bcl-cb5 prevents apoptosis personal data data protection permissions springerlink instant access brian leber & david endoplasmic reticulum membranes mitochondrial apoptosis gauri privacy mitochondrial transmembrane potential bcl-2 family proteins wild type bcl-2 explore content subscription content inhibiting apoptosis induced apoptosis-related genes european economic area serum starvation/myc spatially distinct pathways issue learn institutional subscriptions read drs radhey gupta senior scientist award institut gustave roussy lysophosphatidic acid synthesis chronic liver disease accepting optional cookies journals search log manage preferences endoplasmic reticulum b-cell malignancies content late event matthew bcl-2 proteins https bcl-cb5 article purchase
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description:The disruption of mitochondrial function is a key component of apoptosis in most cell types. Localization of Bcl-2 to the outer mitochondrial and endoplasmic reticulum membranes is consistent with a role in the inhibition of many forms of apoptosis. In Rat-1 cells, a Bcl-2 mutant targeted exclusively to the endoplasmic reticulum (Bcl-cb5) was effective at inhibiting apoptosis induced by serum starvation/myc, or ceramide but not apoptosis induced by etoposide. The former conditions cause a decrease in mitochondrial transmembrane potential (ÎÏm) as an early event that precedes the release of cytochrome c from mitochondria. By contrast, when cells are exposed to etoposide, a situation in which cytochrome c release and membrane localization of the pro-apoptotic protein Bax precede loss of ÎÏm, wild type Bcl-2 but not Bcl-cb5 prevents apoptosis. Therefore, Bcl-2 functions in spatially distinct pathways of apoptosis distinguished by the order of cytochrome c release and loss of ÎÏm.
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headline:Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event
description:The disruption of mitochondrial function is a key component of apoptosis in most cell types. Localization of Bcl-2 to the outer mitochondrial and endoplasmic reticulum membranes is consistent with a role in the inhibition of many forms of apoptosis. In Rat-1 cells, a Bcl-2 mutant targeted exclusively to the endoplasmic reticulum (Bcl-cb5) was effective at inhibiting apoptosis induced by serum starvation/myc, or ceramide but not apoptosis induced by etoposide. The former conditions cause a decrease in mitochondrial transmembrane potential (ÎÏm) as an early event that precedes the release of cytochrome c from mitochondria. By contrast, when cells are exposed to etoposide, a situation in which cytochrome c release and membrane localization of the pro-apoptotic protein Bax precede loss of ÎÏm, wild type Bcl-2 but not Bcl-cb5 prevents apoptosis. Therefore, Bcl-2 functions in spatially distinct pathways of apoptosis distinguished by the order of cytochrome c release and loss of ÎÏm.
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- https://s100.copyright.com/AppDispatchServlet?title=Endoplasmic%20reticulum%20localized%20Bcl-2%20prevents%20apoptosis%20when%20redistribution%20of%20cytochrome%20c%20is%20a%20late%20event&author=Matthew%20G%20Annis%20et%20al&contentID=10.1038%2Fsj.onc.1204288©right=Macmillan%20Publishers%20Limited&publication=0950-9232&publicationDate=2001-04-12&publisherName=SpringerNature&orderBeanReset=true's financial summary
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