Abstract:
:Cytochrome C is a mitochondrial protein that induces apoptosis when released into the cytosol or when added to cell-free extracts. Here we show that cells that overexpress the Bcl-2-related protein Bcl-xL fail to accumulate cytosolic cytochrome C or undergo apoptosis in response to genotoxic stress. Coimmunoprecipitation studies demonstrate that Bcl-xL associates with cytochrome C. Cytochrome C binds directly and specifically to Bcl-xL and not to the proapoptotic Bcl-xs protein. The results also demonstrate that Bcl-xs blocks binding of cytochrome C to Bcl-xL. Our findings support a role for Bcl-xL in protecting cells from apoptosis by inhibiting the availability of cytochrome C in the cytosol.
journal_name
Proc Natl Acad Sci U S Aauthors
Kharbanda S,Pandey P,Schofield L,Israels S,Roncinske R,Yoshida K,Bharti A,Yuan ZM,Saxena S,Weichselbaum R,Nalin C,Kufe Ddoi
10.1073/pnas.94.13.6939subject
Has Abstractpub_date
1997-06-24 00:00:00pages
6939-42issue
13eissn
0027-8424issn
1091-6490journal_volume
94pub_type
杂志文章abstract::Arachidonic acid (AA) metabolites derived from both cyclooxygenase (COX) and lipoxygenase (LOX) pathways transduce a variety of signals related to cell growth. Here, we report that the AA LOX pathway also functions as a critical regulator of cell survival and apoptosis. Rat Walker 256 (W256) carcinosarcoma cells expre...
journal_title:Proceedings of the National Academy of Sciences of the United States of America
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2020-01-07 00:00:00