| pubmed-article:14623896 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14623896 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:14623896 | lifeskim:mentions | umls-concept:C0259419 | lld:lifeskim |
| pubmed-article:14623896 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
| pubmed-article:14623896 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:14623896 | pubmed:dateCreated | 2004-2-2 | lld:pubmed |
| pubmed-article:14623896 | pubmed:abstractText | STAT1 (signal transducer and activator of transcription 1) has been implicated as a mediator of a variety of biological responses in response to stimulation by specific growth factors and cytokines. To understand better the role of STAT1 in the interferon-gamma (IFN-gamma)-induced phenotype, we generated an active form of STAT1 (STAT1C) by substituting Cys residues for both Arg-656 and Asn-658 within the C-terminal loop of the STAT1 SH2 domain. The IFN-gamma activation site element was stimulated and bound efficiently by STAT1C without IFN-gamma treatment. STAT1C was found to be tyrosine-phosphorylated in the nucleus for more than 30 h after IFN-gamma stimulation. STAT1-negative U3A cells reexpressing STAT1C showed retarded cell growth and underwent apoptosis when treated with IFN-gamma. Further analysis demonstrated that apoptosis was preceded by proteolytic cleavage of caspases 2, 3, and 7, and wild type STAT1 also induced cleavage of caspase 7 when expressed in STAT1-negative U3A cells, indicating that STAT1C augments potential activity of wild type STAT1. Studies with cycloheximide treatment showed that protein synthesis induced in the first 24 h after IFN-gamma treatment was required for apoptosis under these conditions. Finally, we found that STAT1C-induced apoptosis was, in part, mediated by caspase 2, 3, and 7 because benzyloxycarbonyl-valyl-aspartyl-valyl-alanyl-aspartic acid fluoromethyl ketone (Z-VDVAD-FMK) treatment partially blocked apoptosis. These results suggest that prolonged nuclear localization of activated STAT1 results in apoptosis involving specific regulation of caspase pathway. | lld:pubmed |
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| pubmed-article:14623896 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:14623896 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14623896 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14623896 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:14623896 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14623896 | pubmed:author | pubmed-author:OuchiToruT | lld:pubmed |
| pubmed-article:14623896 | pubmed:author | pubmed-author:SironiJuan... | lld:pubmed |
| pubmed-article:14623896 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14623896 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:14623896 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:14623896 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14623896 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14623896 | pubmed:pagination | 4066-74 | lld:pubmed |
| pubmed-article:14623896 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:14623896 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14623896 | pubmed:articleTitle | STAT1-induced apoptosis is mediated by caspases 2, 3, and 7. | lld:pubmed |
| pubmed-article:14623896 | pubmed:affiliation | Derald H. Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York University, New York, New York 10029, USA. | lld:pubmed |
| pubmed-article:14623896 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14623896 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14623896 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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