| pubmed-article:20363884 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20363884 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:20363884 | lifeskim:mentions | umls-concept:C0018801 | lld:lifeskim |
| pubmed-article:20363884 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:20363884 | lifeskim:mentions | umls-concept:C0282498 | lld:lifeskim |
| pubmed-article:20363884 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:20363884 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:20363884 | pubmed:dateCreated | 2010-5-20 | lld:pubmed |
| pubmed-article:20363884 | pubmed:abstractText | Treating cancer patients with chemotherapeutics, such as doxorubicin (Dox), cause dilated cardiomyopathy and congestive heart failure because of oxidative stress. On the other hand, heat shock factor-1 (HSF-1), a transcription factor for heat shock proteins (Hsps), is also known to be activated in response to oxidative stress. However, the possible role of HSF-1 activation and the resultant Hsp25 in chemotherapeutic-induced heart failure has not been investigated. Using HSF-1 wild-type (HSF-1(+/+)) and knock-out (HSF-1(-/-)) mice, we tested the hypothesis that activation of HSF-1 plays a role in the development of Dox-induced heart failure. Higher levels of Hsp25 and its phosphorylated forms were found in the failing hearts of Dox-treated HSF-1(+/+) mice. More than twofold increase in Hsp25 mRNA level was found in Dox-treated hearts. Proteomic analysis showed that there is accumulation and aggregation of Hsp25 in Dox-treated failing hearts. Additionally, Hsp25 was found to coimmunoprecipitate with p53 and vice versa. Further studies indicated that the Dox-induced higher levels of Hsp25 transactivated p53 leading to higher levels of the pro-apoptotic protein Bax, but other p53-related proteins remained unaltered. Moreover, HSF-1(-/-) mice showed significantly reduced Dox-induced heart failure and higher survival rate, and there was no change in Bax upon treating with Dox in HSF-1(-/-) mice. From these results we propose a novel mechanism for Dox-induced heart failure: increased expression of Hsp25 because of oxidant-induced activation of HSF-1 transactivates p53 to increase Bax levels, which leads to heart failure. | lld:pubmed |
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| pubmed-article:20363884 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:20363884 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20363884 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20363884 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:20363884 | pubmed:issn | 1522-1539 | lld:pubmed |
| pubmed-article:20363884 | pubmed:author | pubmed-author:ZweierJay LJL | lld:pubmed |
| pubmed-article:20363884 | pubmed:author | pubmed-author:IlangovanGovi... | lld:pubmed |
| pubmed-article:20363884 | pubmed:author | pubmed-author:KhanMahmoodM | lld:pubmed |
| pubmed-article:20363884 | pubmed:author | pubmed-author:MoldovanNican... | lld:pubmed |
| pubmed-article:20363884 | pubmed:author | pubmed-author:DruhanLawrenc... | lld:pubmed |
| pubmed-article:20363884 | pubmed:author | pubmed-author:NishijimaYosh... | lld:pubmed |
| pubmed-article:20363884 | pubmed:author | pubmed-author:VedamKaushikK | lld:pubmed |
| pubmed-article:20363884 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20363884 | pubmed:volume | 298 | lld:pubmed |
| pubmed-article:20363884 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20363884 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20363884 | pubmed:pagination | H1832-41 | lld:pubmed |
| pubmed-article:20363884 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
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| pubmed-article:20363884 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20363884 | pubmed:articleTitle | Role of heat shock factor-1 activation in the doxorubicin-induced heart failure in mice. | lld:pubmed |
| pubmed-article:20363884 | pubmed:affiliation | Division of Cardiovascular medicine, Davis Heart & Lung Research Institute, Department of Internal Medicine, The Ohio State University, Columbus, OH, USA. | lld:pubmed |
| pubmed-article:20363884 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20363884 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:15499 | entrezgene:pubmed | pubmed-article:20363884 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20363884 | lld:pubmed |
