Source:http://linkedlifedata.com/resource/pubmed/id/12048164
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2002-6-5
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pubmed:abstractText |
The protein kinase C (PKC)-specific inhibitor, Ro-31-8220, has been shown to induce anti-proliferation and apoptosis of human cancer cell lines. In the present study, we determined the molecular pathways that lead to apoptosis after treatment of cells with the PKC-specific inhibitor RO-31-8220. For this, we used the U937 human leukemia cell line and a phorbolmyristate acetate (PMA)-resistant derivative cell line, R-U937. Ro-31-8220 treatment of U937 cells leads to apoptosis, which is accompanied by activation of caspase 3 (as measured by decreased levels of the 32kDa inactive form and increased proteolytic cleavage of phospholipase C (PLC)-gamma1). The broad-range caspase inhibitor z-VAD-fmk inhibits this induction of apoptosis, supporting a direct link between caspase activation and Ro-31-8220 induction of apoptosis. This activation of apoptosis is also accompanied by release of cytochrome c, but not by altered expression of Bcl-2 family protein or IAP family proteins. In R-U937 cells, Ro-31-8220 fails to cause release of cytochrome c, activation of caspase 3, or apoptosis. Activation of Akt occurs to a greater extent in the R-U937 cells than the U937 cells and thus might be related to protection from Ro-31-8220-induced apoptosis.
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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/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Indoles,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Ro 31-8220,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0304-3835
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
182
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
183-91
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12048164-Apoptosis,
pubmed-meshheading:12048164-Caspase 3,
pubmed-meshheading:12048164-Caspases,
pubmed-meshheading:12048164-Cell Nucleus,
pubmed-meshheading:12048164-Drug Resistance,
pubmed-meshheading:12048164-Enzyme Activation,
pubmed-meshheading:12048164-Enzyme Inhibitors,
pubmed-meshheading:12048164-Humans,
pubmed-meshheading:12048164-Indoles,
pubmed-meshheading:12048164-Protein Kinase C,
pubmed-meshheading:12048164-Tetradecanoylphorbol Acetate,
pubmed-meshheading:12048164-U937 Cells
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pubmed:year |
2002
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pubmed:articleTitle |
Failure to activate caspase 3 in phorbol ester-resistant leukemia cells is associated with resistance to apoptotic cell death.
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pubmed:affiliation |
Department of Immunology, School of Medicine, Keimyung University, 194 DongSan-Dong Jung-Gu, 700-712, Taegu, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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