title: Contractile function of rat myocardium is less susceptible to hypoxia/reoxygenation after acute infarction.
abstract: In this study we tested the hypothesis that induction of heat shock proteins (HSPs) and antioxidant enzymes is a compensatory mechanism, which preserves the contractility of the surviving myocardium after acute myocardial infarction. For this purpose, mechanical function of isolated rat papillary muscles was tested 15 h after experimental myocardial infarction and sham operation, respectively. Contractility of the preparations was compared to the expression of HSP25, HSP72, and glutathione peroxidase activity (GSH-Px) at normoxia and during hypoxia/reoxygenation. At normoxic conditions, rates of isometric contraction and, in particular, of relaxation were significantly higher after acute myocardial infarction than after sham operation. Improved relaxation rates were reflected in 2- to 3-fold higher heat shock protein levels in papillary muscles from rats with myocardial infarction compared to sham operated animals. During hypoxia/reoxygenation, the rates of contraction and relaxation were better preserved after myocardial infarction than after sham surgery. Recovery of relaxation rates during reoxygenation was associated with increased HSP25 levels and enhanced GSH-Px activity after myocardial infarction. In conclusion, heat shock proteins exert a beneficial effect on cardiac muscle relaxation after acute myocardial infarction. Enhanced heat shock protein expression and GSH-Px activity may protect the contractile function of the surviving myocardium against the damaging influence of hypoxia/reoxygenation during the early post-infarct period.
authors.affiliation: Institute of Physiology, Humboldt-University, Charité, Berlin, Germany. kay-dietrich.wagner@charite.de
authors.forename: K D
authors.initials: KD
authors.lastname: Wagner
authors.forename: G
authors.initials: G
authors.lastname: Gmehling
authors.forename: J
authors.initials: J
authors.lastname: Günther
authors.forename: H M
authors.initials: HM
authors.lastname: Stauss
authors.forename: K
authors.initials: K
authors.lastname: Mydlak
authors.forename: H
authors.initials: H
authors.lastname: Theres
authors.forename: H
authors.initials: H
authors.lastname: Scholz
authors.forename: I
authors.initials: I
authors.lastname: Schimke
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism; D006332:Cardiomegaly / Q000378:metabolism / Q000503:physiopathology; D002908:Chronic Disease; D003402:Creatine Kinase / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000378:metabolism; D055551:HSP27 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism; D015151:Immunoblotting; D008297:Male; D009200:Myocardial Contraction / Q000502:physiology*; D009203:Myocardial Infarction / Q000378:metabolism*; D015428:Myocardial Reperfusion Injury / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism; D010210:Papillary Muscles / Q000201:enzymology / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013482:Superoxide Dismutase / Q000378:metabolism; D016277:Ventricular Function, Left
chemical_list: D055551:HSP27 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; D009363:Neoplasm Proteins; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D003402:Creatine Kinase; D010100:Oxygen; D002118:Calcium