| pubmed-article:17616937 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C0033325 | lld:lifeskim |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C0080103 | lld:lifeskim |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C0007134 | lld:lifeskim |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C0243043 | lld:lifeskim |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C0178874 | lld:lifeskim |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:17616937 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:17616937 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:17616937 | pubmed:dateCreated | 2007-7-9 | lld:pubmed |
| pubmed-article:17616937 | pubmed:abstractText | Heat shock proteins (HSPs) play an important role in the cellular response to environmental stress and exert a cytoprotective effect. Especially HSP70 is an effective inhibitor of apoptosis, suggesting a role of HSP70 in carcinogenesis and tumor progression. To explore the relevance of HSP70 in renal cell carcinomas (RCCs), we analyzed nuclear and cytoplasmic HSP70 protein expression in formalin-fixed tissue from 145 clear cell RCCs by immunohistochemistry as well as Western blot analysis. Nuclear HSP70 expression was found in all RCCs and 75% of the tumors also exhibited a cytoplasmic HSP70 staining. Importantly, RCCs showed significantly reduced cytoplasmic (p=0.001) and combined nuclear/cytoplasmic (p=0.0022) HSP70 expression when compared with their cells of origin. A significant (p=0.0176) decrease of nuclear HSP70 expression became evident from well to poorly differentiated clear cell RCCs. Quite similarly, a trend (p=0.0558) for reduced combined nuclear/cytoplasmic HSP70 expression was shown from early (pT1) to advanced (pT3) tumor stages. Nevertheless, no correlation between HSP70 expression and patients survival became evident. In conclusion, our investigation demonstrates a significant decrease of antiapoptotic HSP70 protein expression during carcinogenesis and during progression from well (G1) to poorly (G3) differentiated clear cell RCCs. Our results suggest that HSP70-mediated inhibition of apoptosis seems to be of minor importance for carcinogenesis and tumor progression in RCCs. | lld:pubmed |
| pubmed-article:17616937 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17616937 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17616937 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17616937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17616937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17616937 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17616937 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17616937 | pubmed:issn | 1699-5848 | lld:pubmed |
| pubmed-article:17616937 | pubmed:author | pubmed-author:ShibataTT | lld:pubmed |
| pubmed-article:17616937 | pubmed:author | pubmed-author:RambCC | lld:pubmed |
| pubmed-article:17616937 | pubmed:author | pubmed-author:GabbertH EHE | lld:pubmed |
| pubmed-article:17616937 | pubmed:author | pubmed-author:WillersRR | lld:pubmed |
| pubmed-article:17616937 | pubmed:author | pubmed-author:MahotkaCC | lld:pubmed |
| pubmed-article:17616937 | pubmed:author | pubmed-author:GrimmM OMO | lld:pubmed |
| pubmed-article:17616937 | pubmed:author | pubmed-author:HeikausSS | lld:pubmed |
| pubmed-article:17616937 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17616937 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:17616937 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17616937 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17616937 | pubmed:pagination | 1099-107 | lld:pubmed |
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| pubmed-article:17616937 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17616937 | pubmed:articleTitle | Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis. | lld:pubmed |
| pubmed-article:17616937 | pubmed:affiliation | Institute of Pathology, Heinrich-Heine University Hospital, Duesseldorf, Germany. Ramp@med.uni-duesseldorf.de | lld:pubmed |
| pubmed-article:17616937 | pubmed:publicationType | Journal Article | lld:pubmed |
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