| pubmed-article:10638661 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10638661 | lifeskim:mentions | umls-concept:C0534519 | lld:lifeskim |
| pubmed-article:10638661 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
| pubmed-article:10638661 | lifeskim:mentions | umls-concept:C2610925 | lld:lifeskim |
| pubmed-article:10638661 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10638661 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10638661 | pubmed:dateCreated | 2000-2-3 | lld:pubmed |
| pubmed-article:10638661 | pubmed:abstractText | Sepsis induces extensive lymphocyte cell death that may contribute to immune depression and morbidity/mortality in the disorder. bcl-2 is a member of a new class of oncogenes that prevents cell death from an array of noxious stimuli. Transgenic mice that overexpress BCL-2 in T lymphocytes are resistant to sepsis-induced T cell apoptosis, and mortality was decreased in sepsis. The purpose of this study was to identify key initiator and executioner "caspases" involved in sepsis-induced lymphocyte apoptosis and to determine if BCL-2 acts prior to caspase activation. Thymi were removed 5-22 h post-cecal ligation and puncture (CLP) or sham surgery. Apoptosis was evaluated in thymocytes by annexin-V FITC labeling and flow cytometry. Caspase-1 activity was determined by western blot analysis of the procaspase protein and p20 subunit of the activated caspase; activities of caspases -2, -6, and -9 were determined by colorimetric assays using specific substrates conjugated to a color reporter molecule. Caspase-3 activity was determined both by western blot and by a fluorogenic assay in which a fluorescent compound was generated. Thymocytes from CLP mice had markedly increased apoptosis and activation of caspases -2, -3, -6, and -9 in comparison with thymocytes of sham-operated mice. Caspase-1 was not activated. BCL-2 prevented sepsis-induced thymocyte apoptosis and inhibited activation of all caspases. We conclude that sepsis causes activation of multiple caspases and that BCL-2 acts upstream as an inhibitor of caspase activation. The pattern of caspase activation suggests a mitochondrial mediated pathway. | lld:pubmed |
| pubmed-article:10638661 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10638661 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10638661 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10638661 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10638661 | pubmed:issn | 1073-2322 | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:KarlI EIE | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:ChengS LSL | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:BuchmanT GTG | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:ChingC CCC | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:SwansonP EPE | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:ORYR LRL | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:HotchkissR... | lld:pubmed |
| pubmed-article:10638661 | pubmed:author | pubmed-author:TinsleyK WKW | lld:pubmed |
| pubmed-article:10638661 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10638661 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:10638661 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10638661 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10638661 | pubmed:pagination | 1-7 | lld:pubmed |
| pubmed-article:10638661 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10638661 | pubmed:meshHeading | pubmed-meshheading:10638661... | lld:pubmed |
| pubmed-article:10638661 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10638661 | pubmed:articleTitle | Caspases -2, -3, -6, and -9, but not caspase-1, are activated in sepsis-induced thymocyte apoptosis. | lld:pubmed |
| pubmed-article:10638661 | pubmed:affiliation | Department of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:10638661 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10638661 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10638661 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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