Bcl-2 targeted to the endoplasmic reticulum can inhibit apoptosis induced by Myc but not etoposide in Rat-1 fibroblasts View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-06-10

AUTHORS

Si Tuen Lee, Klaus P Hoeflich, Gihane W Wasfy, James R Woodgett, Brian Leber, David W Andrews, David W Hedley, Linda Z Penn

ABSTRACT

Bcl-2 is a key inhibitor of a broad range of apoptotic pathways, yet neither the mechanism of action nor the role of Bcl-2 subcellular localization are well understood. The subcellular localization of Bcl-2 includes the mitochondrial membrane as well as the contiguous membrane of the endoplasmic reticulum and nuclear envelope. Most studies suggest that the ability of Bcl-2 to confer cell survival is dependent upon its localization to the mitochondria. In this manuscript, we show that Bcl-2 targeted to the endoplasmic reticulum can inhibit Myc-, but not etoposide-induced apoptosis in the Rat-1 fibroblast cell line. By contrast, wild type Bcl-2 can inhibit apoptosis triggered by either death agonist. We further show both Myc and etoposide trigger disruption of mitochondrial membrane potential (MMP) and induce poly-ADP ribose polymerase (PARP) cleavage, but release of calcium was not evident. Bcl-2 abrogates apoptosis at or upstream of MMP depletion showing that Bcl-2 does not have to reside at the mitochondria to prevent apoptosis. These results further elucidate the biochemical events associated with Myc- and etoposide-induced apoptosis and significantly advance our understanding of Bcl-2 function. More... »

PAGES

3520-3528

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.onc.1202716

DOI

http://dx.doi.org/10.1038/sj.onc.1202716

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028837167

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10376530


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