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Indexed/Abstracted in: EMBASE, PubMed/MEDLINE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 0,536
Online ISSN 1827-1758
Kelly K. J.
From the Indiana University School of Medicine Department of Medicine, Division of Nephrology Indianapolis, IN, USA
Acute renal failure is a frequent clinical entity with an increasing incidence and an unacceptably high mortality, yet there is no specific treatment. The induction of stress response (heat shock) proteins (HSPs) is a highly conserved response that protects many cell types from diverse physiological and environmental stressors. Diverse HSP families of different sizes function as molecular chaperones that facilitate the folding of enzymes and other proteins into the functional conformation. After injury, HSPs are believed to facilitate the restoration of normal function by assisting in the refolding of denatured proteins and degradation of irreparably damaged proteins and toxic metabolites, limitation of aggregation of damaged peptides and aiding the appropriate folding of newly synthesized essential polypeptides. We have recently demonstrated protection from the functional deficits and histologic evidence of experimental ischemic renal injury with heat stress 6 hours but not 48 hours prior to the ischemic insult. Limitation of the induction of HSPs (either with a short period of hyperthermia or pharmacologically) attenuated the protection observed. Other investigators have demonstrated a correlation between the levels of HSP 25 and renal ischemic preconditioning in the mouse. Several pharmacologic agents have been shown to increase HSP expression. Enhancement of these endogenous protective mechanisms has potential benefit in human disease.