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rdf:type |
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lifeskim:mentions |
umls-concept:C0010749,
umls-concept:C0026237,
umls-concept:C0028778,
umls-concept:C0030685,
umls-concept:C0162638,
umls-concept:C0332206,
umls-concept:C0376515,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1708528,
umls-concept:C1963578
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pubmed:issue |
5303
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pubmed:dateCreated |
1997-3-11
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pubmed:abstractText |
Bcl-2 is an integral membrane protein located mainly on the outer membrane of mitochondria. Overexpression of Bcl-2 prevents cells from undergoing apoptosis in response to a variety of stimuli. Cytosolic cytochrome c is necessary for the initiation of the apoptotic program, suggesting a possible connection between Bcl-2 and cytochrome c, which is normally located in the mitochondrial intermembrane space. Cells undergoing apoptosis were found to have an elevation of cytochrome c in the cytosol and a corresponding decrease in the mitochondria. Overexpression of Bcl-2 prevented the efflux of cytochrome c from the mitochondria and the initiation of apoptosis. Thus, one possible role of Bcl-2 in prevention of apoptosis is to block cytochrome c release from mitochondria.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Etoposide,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1129-32
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:9027314-Apoproteins,
pubmed-meshheading:9027314-Apoptosis,
pubmed-meshheading:9027314-Caspase 3,
pubmed-meshheading:9027314-Caspases,
pubmed-meshheading:9027314-Cysteine Endopeptidases,
pubmed-meshheading:9027314-Cytochrome c Group,
pubmed-meshheading:9027314-Cytochromes c,
pubmed-meshheading:9027314-Cytosol,
pubmed-meshheading:9027314-DNA Fragmentation,
pubmed-meshheading:9027314-Enzyme Activation,
pubmed-meshheading:9027314-Etoposide,
pubmed-meshheading:9027314-HL-60 Cells,
pubmed-meshheading:9027314-HeLa Cells,
pubmed-meshheading:9027314-Humans,
pubmed-meshheading:9027314-Intracellular Membranes,
pubmed-meshheading:9027314-Membrane Potentials,
pubmed-meshheading:9027314-Mitochondria,
pubmed-meshheading:9027314-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:9027314-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:9027314-Staurosporine,
pubmed-meshheading:9027314-Transfection
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pubmed:year |
1997
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pubmed:articleTitle |
Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked.
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pubmed:affiliation |
Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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