Source:http://linkedlifedata.com/resource/pubmed/id/10812002
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rdf:type | |
lifeskim:mentions |
umls-concept:C0007600,
umls-concept:C0024623,
umls-concept:C0030946,
umls-concept:C0086418,
umls-concept:C0127400,
umls-concept:C0162638,
umls-concept:C0205263,
umls-concept:C0291573,
umls-concept:C0334227,
umls-concept:C1314939,
umls-concept:C1413132,
umls-concept:C1456820,
umls-concept:C1879547,
umls-concept:C2717971
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pubmed:issue |
6
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pubmed:dateCreated |
2000-6-27
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pubmed:abstractText |
In the present study, we investigated the role of caspase-3/CPP32 and serine protease(s) in cell death induced by TNF-alpha in SNU-16 human gastric adenocarcinoma cells. Apoptosis induced in SNU-16 cells by TNF-alpha was accompanied by the activation of caspase-3/CPP32. After treatment with TNF-alpha, PKCdelta cleaved to its characteristic 40 kDa fragment in a caspase-3/CPP32 dependent manner. Incubation with z-DEVD-fmk completely abrogated TNF-alpha-induced DNA fragmentation, indicating that activation of caspase-3/CPP32 was crucially involved in TNF-alpha-induced apoptosis. In addition, serine protease inhibitor, 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF), clearly inhibited all the features of apoptosis including DNA fragmentation and chromatin condensation. Furthermore, in the AEBSF treated SNU-16 cells, only intact PKCdelta was detected by immunoblot analysis, suggesting that activation of caspase-3/CPP32 was blocked. Thus, the AEBSF-sensitive step may involve an upstream caspase-3/CPP32 protease activation. Taken together, these results suggest that both caspase-3/CPP32 and serine protease(s) are activated and play an important role in TNF-alpha induced apoptosis in SNU-16 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/4-(2-aminoethyl)benzenesulfonylfluor...,
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/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfones,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1019-6439
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1243-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10812002-Adenocarcinoma,
pubmed-meshheading:10812002-Apoptosis,
pubmed-meshheading:10812002-Caspase 3,
pubmed-meshheading:10812002-Caspases,
pubmed-meshheading:10812002-Humans,
pubmed-meshheading:10812002-Neoplasm Proteins,
pubmed-meshheading:10812002-Serine Proteinase Inhibitors,
pubmed-meshheading:10812002-Stomach Neoplasms,
pubmed-meshheading:10812002-Sulfones,
pubmed-meshheading:10812002-Tumor Cells, Cultured,
pubmed-meshheading:10812002-Tumor Necrosis Factor-alpha
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pubmed:year |
2000
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pubmed:articleTitle |
TNF-alpha induces apoptosis mediated by AEBSF-sensitive serine protease(s) that may involve upstream caspase-3/CPP32 protease activation in a human gastric cancer cell line.
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pubmed:affiliation |
Laboratory of Cell Biology, Korea Cancer Center Hospital, Nowon-gu, Seoul 139-706, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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