Source:http://linkedlifedata.com/resource/pubmed/id/15350550
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-9-7
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pubmed:abstractText |
Bcl-2 family proteins regulate apoptosis at the level of mitochondria. To examine the mechanism of Bcl-2 function, we investigated the effects of the protonophore carbonyl cyanide m-chlorophenyl hydrazone (CCCP) on two hematopoietic cell lines and Bcl-2 overexpressing transfectants. CCCP directly interferes with mitochondrial function and induces apoptosis. We show that Bcl-2 inhibits apoptosis and that the antiapoptotic effect of Bcl-2 takes place upstream of caspase activation and nuclear changes associated with apoptosis, since these were markedly inhibited in cells overexpressing Bcl-2. Bcl-2 does not prevent the decrease in mitochondrial membrane potential nor the alterations in cellular ATP content induced by CCCP in FL5.12 and Jurkat cells. A higher number of mitochondria was observed in untreated Bcl-2 transfected cells compared to parental cells, as shown by electron microscopy. Exposure to CCCP induced a dramatic decrease in the number of mitochondria and severely disrupted mitochondrial ultrastructure, with apparent swelling and loss of cristae in parental cells. Bcl-2 clearly diminished the disruption of mitochondrial structure and preserved a higher number of mitochondria. These data suggest that CCCP induces apoptosis by structural disruption of mitochondria and that Bcl-2 prevents apoptosis and mitochondrial degeneration by preserving mitochondrial integrity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonyl Cyanide m-Chlorophenyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-4827
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pubmed:author |
pubmed-author:BirkenkampKim UKU,
pubmed-author:DijkmanHenry B P MHB,
pubmed-author:JansenJoop HJH,
pubmed-author:SmeitinkJan A MJA,
pubmed-author:de AbreuRonney ARA,
pubmed-author:de GraafAniek OAO,
pubmed-author:de WitteTheoT,
pubmed-author:van den HeuvelLambert PLP,
pubmed-author:van der ReijdenBert ABA
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
299
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
533-40
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:15350550-Adenosine Triphosphate,
pubmed-meshheading:15350550-Animals,
pubmed-meshheading:15350550-Apoptosis,
pubmed-meshheading:15350550-Carbonyl Cyanide m-Chlorophenyl Hydrazone,
pubmed-meshheading:15350550-Caspases,
pubmed-meshheading:15350550-Cell Nucleus,
pubmed-meshheading:15350550-Enzyme Activation,
pubmed-meshheading:15350550-Humans,
pubmed-meshheading:15350550-Jurkat Cells,
pubmed-meshheading:15350550-Lymphoma, B-Cell,
pubmed-meshheading:15350550-Membrane Potentials,
pubmed-meshheading:15350550-Mice,
pubmed-meshheading:15350550-Mitochondria,
pubmed-meshheading:15350550-Proto-Oncogene Proteins c-bcl-2
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pubmed:year |
2004
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pubmed:articleTitle |
Bcl-2 prevents loss of mitochondria in CCCP-induced apoptosis.
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pubmed:affiliation |
Central Hematology Laboratory, Department of Hematology, University Medical Center Nijmegen, Nijmegen 6500 HB, The Netherlands.
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pubmed:publicationType |
Journal Article
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