title: Exercise training modulates heat shock protein response in diabetic rats.
abstract: Strenuous exercise induces oxidative stress and modification of intracellular proteins. Exercise training, however, upregulates endogenous antioxidant defenses and heat shock protein (HSP) expression. In diabetes, perturbations in the endogenous antioxidant and HSP protection have been reported. The aim of this study was to examine the effect of 8 wk of endurance training on HSP expression and oxidative stress markers in the skeletal muscle, heart, and liver of streptozotocin-induced diabetic (SID) and nondiabetic control rats. Induction of diabetes decreased HSP72 expression in heart, liver, and vastus lateralis muscles. SID increased heme oxygenase-1, an oxidative stress-inducible HSP, in liver, red gastrocnemius muscle, and vastus lateralis muscle and glucose-regulated protein 75 in liver. SID increased HSP90 levels in the heart, but levels decreased in the liver. Diabetes induced oxidative stress marker protein carbonyl levels and tissue inflammation. Although endurance training increased the expression of HSP72 in all of the tissues examined, this induction was less pronounced in diabetic rats than in nondiabetic controls. Furthermore, endurance training induced the activation and expression of transcriptional regulator heat shock factor-1 only in nondiabetic control animals. In summary, diabetes may increase susceptibility to oxidative damage and impair HSP protection, but endurance training may offset some of the adverse effects of diabetes by upregulating tissue HSP expression. Our results suggest that diabetes impairs HSP protection, possibly via transcriptionally mediated mechanisms.
authors.affiliation: Department of Physiology, University of Kuopio, Finland.
authors.forename: Mustafa
authors.initials: M
authors.lastname: Atalay
authors.forename: Niku K J
authors.initials: NK
authors.lastname: Oksala
authors.forename: David E
authors.initials: DE
authors.lastname: Laaksonen
authors.forename: Savita
authors.initials: S
authors.lastname: Khanna
authors.forename: Chitose
authors.initials: C
authors.lastname: Nakao
authors.forename: Jani
authors.initials: J
authors.lastname: Lappalainen
authors.forename: Sashwati
authors.initials: S
authors.lastname: Roy
authors.forename: Osmo
authors.initials: O
authors.lastname: Hänninen
authors.forename: Chandan K
authors.initials: CK
authors.lastname: Sen
mesh_terms: D000818:Animals; D021461:Animals, Outbred Strains; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism* / Q000503:physiopathology*; D050884:HSP72 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D018869:Heat-Shock Response / Q000502:physiology; D008099:Liver / Q000378:metabolism; D008297:Male; D018482:Muscle, Skeletal / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D018384:Oxidative Stress / Q000502:physiology; D010807:Physical Endurance / Q000502:physiology; D005082:Physical Exertion / Q000502:physiology*; D051381:Rats; D017208:Rats, Wistar
chemical_list: D050884:HSP72 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D006360:Heat-Shock Proteins