TITLE

Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event

AUTHOR(S)
Annis, Matthew G; Zamzami, Naoufal; Zhu, Weijia; Penn, Linda Z; Kroemer, Guido; Leber, Brian; Andrews, David W
PUB. DATE
April 2001
SOURCE
Oncogene;4/12/2001, Vol. 20 Issue 16, p1939
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
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. Oncogene (2001) 20, 1939–1952.
ACCESSION #
8916765

 

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