pubmed-article:12391142 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12391142 | lifeskim:mentions | umls-concept:C0018850 | lld:lifeskim |
pubmed-article:12391142 | lifeskim:mentions | umls-concept:C0532128 | lld:lifeskim |
pubmed-article:12391142 | lifeskim:mentions | umls-concept:C1564881 | lld:lifeskim |
pubmed-article:12391142 | lifeskim:mentions | umls-concept:C0205160 | lld:lifeskim |
pubmed-article:12391142 | lifeskim:mentions | umls-concept:C1415755 | lld:lifeskim |
pubmed-article:12391142 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:12391142 | pubmed:dateCreated | 2002-10-22 | lld:pubmed |
pubmed-article:12391142 | pubmed:abstractText | Heat shock protein 72 (Hsp72) is thought to protect cells against cellular stress. The protective role of Hsp72 was investigated by determining the effect of this protein on the stress-activated protein kinase signaling pathways. Prior exposure of NIH 3T3 cells to mild heat shock (43 degrees C for 20 min) resulted in inhibition of H(2)O(2)-induced activation of apoptosis signal-regulating kinase 1 (ASK1). Overexpression of Hsp72 also inhibited H(2)O(2)-induced activation of ASK1 as well as that of downstream kinases in the p38 mitogen-activated protein kinase (MAPK) signaling cascade. Recombinant Hsp72 bound directly to ASK1 and inhibited ASK1 activity in vitro. Furthermore, coimmunoprecipitation analysis revealed a physical interaction between endogenous Hsp72 and ASK1 in NIH 3T3 cells exposed to mild heat shock. Hsp72 blocked both the homo-oligomerization of ASK1 and ASK1-dependent apoptosis. Hsp72 antisense oligonucleotides prevented the inhibitory effects of mild heat shock on H(2)O(2)-induced ASK1 activation and apoptosis. These observations suggest that Hsp72 functions as an endogenous inhibitor of ASK1. | lld:pubmed |
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pubmed-article:12391142 | pubmed:language | eng | lld:pubmed |
pubmed-article:12391142 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12391142 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12391142 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12391142 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12391142 | pubmed:month | Nov | lld:pubmed |
pubmed-article:12391142 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:ParkHee-SaeHS | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:KimMi-SungMS | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:HuhSung-HoSH | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:ChoiEui-JuEJ | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:KimSunghoonS | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:KoYoung-GyuYG | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:KimEun... | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:SeoJeong-SunJ... | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:LeeJae-SeonJS | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:ChoSsang-GooS... | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:KimChang... | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:HwangHyun... | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:NohKyung... | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:KimMyung... | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:RyooKanghyunK | lld:pubmed |
pubmed-article:12391142 | pubmed:author | pubmed-author:KangWoo JinWJ | lld:pubmed |
pubmed-article:12391142 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12391142 | pubmed:volume | 22 | lld:pubmed |
pubmed-article:12391142 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12391142 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12391142 | pubmed:pagination | 7721-30 | lld:pubmed |
pubmed-article:12391142 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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