| Contractile function of rat myocardium is less susceptible to hypoxia/reoxygenation after acute infarction. | |
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MedLine Citation:
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PMID: 11855741 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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K D Wagner; G Gmehling; J Günther; H M Stauss; K Mydlak; H Theres; H Scholz; I Schimke |
Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Molecular and cellular biochemistry Volume: 228 ISSN: 0300-8177 ISO Abbreviation: Mol. Cell. Biochem. Publication Date: 2001 Dec |
Date Detail:
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Created Date: 2002-02-21 Completed Date: 2002-08-08 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0364456 Medline TA: Mol Cell Biochem Country: Netherlands |
Other Details:
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Languages: eng Pagination: 49-55 Citation Subset: IM |
Affiliation:
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Institute of Physiology, Humboldt-University, Charité, Berlin, Germany. kay-dietrich.wagner@charite.de |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Calcium / metabolism Cardiomegaly / metabolism, physiopathology Chronic Disease Creatine Kinase / metabolism Glutathione Peroxidase / metabolism HSP27 Heat-Shock Proteins HSP72 Heat-Shock Proteins Heat-Shock Proteins / metabolism Immunoblotting Male Myocardial Contraction / physiology* Myocardial Infarction / metabolism* Myocardial Reperfusion Injury / metabolism* Neoplasm Proteins / metabolism Oxygen / metabolism Papillary Muscles / enzymology, metabolism Rats Rats, Wistar Superoxide Dismutase / metabolism Ventricular Function, Left |
| Chemical | |
Reg. No./Substance:
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0/HSP27 Heat-Shock Proteins; 0/HSP72 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Hspb1 protein, rat; 0/Neoplasm Proteins; 7440-70-2/Calcium; 7782-44-7/Oxygen; EC 1.11.1.9/Glutathione Peroxidase; EC 1.15.1.1/Superoxide Dismutase; EC 2.7.3.2/Creatine Kinase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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