title: [Role of heat shock proteins in the mechanism of cardioprotective effect of transient hyperthermia and delayed preconditioning].
abstract: This review article focuses on discussing the role of the heat shock proteins (HSP) in myocardial protection against ischemia-reperfusion injury. In the present time, it has also been recognized that HSP may responsible for the increase in cardiac tolerance to ischemia-reperfusion after heat shock or after delayed ischemic preconditioning. The enhancement of the HSP expression in transgenic mice promotes an elevation of cardiac resistance to ischemia-reperfusion. The same effect is induced by transfection of the HSP genes. It has been established that deletion of the HSP70.1 and HSP70.3 genes abolishes a cardioprotective effect of delayed preconditioning. The mechanism by which HSP protect the heart against ischemia-reperfusion remains obscure. It has been proposed that HSP protect the heart via refolding proteins, an increase in 5'-nucleotidase activity, an improvement of Ca(2+)-pump function in sarcoplasmic reticulum during ischemia-reperfusion.
authors.forename: L N
authors.initials: LN
authors.lastname: Maslov
authors.forename: I G
authors.initials: IG
authors.lastname: Khaliulin
authors.forename: J -M
authors.initials: J-
authors.lastname: Pei
authors.forename: I
authors.initials: I
authors.lastname: Zhang
mesh_terms: D000818:Animals; D015220:Calcium Channels / Q000378:metabolism; D005334:Fever / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D019157:Ischemic Preconditioning, Myocardial; D051379:Mice; D015428:Myocardial Reperfusion Injury / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D015220:Calcium Channels; D018840:HSP70 Heat-Shock Proteins; C498550:Hsp70.3 protein, mouse; C081884:heat-shock protein 70.1