Source:http://linkedlifedata.com/resource/pubmed/id/14646222
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2003-12-3
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pubmed:abstractText |
A post-irradiation treatment of the human leukemia cell line MOLT-4 with the antioxidant Trolox attenuated caspase-3 dependent apoptosis. The increase in the p53 expression and SAPK/JNK activation after X irradiation was also inhibited by a Trolox treatment, but the expression of BCL-2 and BAX, which would occur downstream from p53, was not changed. Studies on the effects of the intracellular calcium chelator BAPTA-AM on the induction of apoptosis and the activation of SAPK/JNK and caspase-3 proved that the chelation of calcium merely delayed the onset of radiation-induced apoptosis and the activation of SAPK/JNK and caspase-3. When the effects of the protein synthesis inhibitor cycloheximde on the apoptotic signaling pathways, including the activation of caspase family proteins and SAPK/JNK, were investigated, the expression of death receptor Fas through SAPK/JNK activation was found to be required for radiation-induced apoptosis. Finally, the relationship between the amounts of DNA dsb and induction of apoptosis was examined by irradiating BrdU-incorporated cells. An increase in DNA dsb caused by BrdU was found, but the induction of apoptosis was not enhanced. From these data, we could get no positive evidence for DNA as a target of X-rays and p53 as an indispensable factor to induced apoptosis in X-irradiated MOLT-4 cells.
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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/6-hydroxy-2,5,7,8-tetramethylchroman...,
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/Chromans,
http://linkedlifedata.com/resource/pubmed/chemical/Death Domain Receptor Signaling...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0449-3060
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
203-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14646222-Apoptosis,
pubmed-meshheading:14646222-Caspase 3,
pubmed-meshheading:14646222-Caspases,
pubmed-meshheading:14646222-Cell Line, Tumor,
pubmed-meshheading:14646222-Chromans,
pubmed-meshheading:14646222-Death Domain Receptor Signaling Adaptor Proteins,
pubmed-meshheading:14646222-Enzyme Activation,
pubmed-meshheading:14646222-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:14646222-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:14646222-Humans,
pubmed-meshheading:14646222-Leukemia, T-Cell,
pubmed-meshheading:14646222-Mitogen-Activated Protein Kinases,
pubmed-meshheading:14646222-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:14646222-Signal Transduction,
pubmed-meshheading:14646222-Tumor Suppressor Protein p53,
pubmed-meshheading:14646222-X-Rays
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pubmed:year |
2003
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pubmed:articleTitle |
Induction of apoptosis through the activation of SAPK/JNK followed by the expression of death receptor Fas in X-irradiated cells.
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pubmed:affiliation |
Laboratory of Radiation Biology, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan. kuwabara@vetmed.hokudai.ac.jp
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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