Publication: Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis
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Date
2007
Authors
Ramp, U. ; Mahotka, C. ; Heikaus, S. ; Shibata, T. ; Grimm, M.O. ; Willers, R. ; Gabbert, H.E.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
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.
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