Constitutive and Inducible hsp70s are Involved in Oxidative Resistance Evoked by Heat Shock or Ethanol

• Published in: Journal of molecular and cellular cardiology Vol. 30; no. 3; pp. 587 - 598
• Main Authors: Su, Ching-Yuan, Chong, Kowit-Yu, Owen, Oliver E, Dillmann, Wolfgang H, Chang, Chawnshang, Lai, Chen-Ching
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01-03-1998
• Subjects: Animals; Antioxidants - metabolism; Catalase; Cell Line; Cell Nucleus - metabolism; Cytoplasm - metabolism; Ethanol - pharmacology; Glutathione peroxidase; Heart - drug effects; Heat shock protein; Hot Temperature; HSP70 Heat-Shock Proteins - biosynthesis; HSP70 Heat-Shock Proteins - metabolism; Hydrogen Peroxide - toxicity; Ischemic Preconditioning, Myocardial; Myocardial Reperfusion Injury - metabolism; Myocardial Reperfusion Injury - prevention & control; Myocardium - metabolism; Oxidative damage; Oxidative Stress; Rats; Reperfusion injury; The stress response; Glutathione peroxidase; The stress response; Catalase; Oxidative damage; Reperfusion injury; Heat shock protein
• ISSN: 0022-2828; 1095-8584
• DOI: 10.1006/jmcc.1997.0622

Improved cardiac post-ischemic recovery after whole-body hyperthermia is correlated with an increased expression of the heat shock proteins (hsps). The inducible hsp70 (hsp70i) has a known cardioprotective effect against ischemia/reperfusion injury. Here, we studied whether other hsps are also involved in cardioprotection. Using rat heart-derived H9c2 myocytes, we observed that preheating at 43°C for 20 min conferred resistance to hydrogen peroxide (H2O2). The resistance to mild H2O2toxicity (3–5μmol/107cells) appeared early and persisted, whereas the resistance to moderate H2O2toxicity (6–9μmol/107cells) was detectable only at 20–44 h post heat shock. No resistance was observed at higher doses of hydrogen peroxide (10–12μmol/107cells), indicating that severe toxicity exceeds the capacity of the induced protective mechanism. Coincidentally, this thermal regimen elicited a rapid and prolonged increase in the cellular level of hsp70i, and a delayed and transient induction of the constitutive hsp70 (hsp70c). Nuclear translocations of hsp70i and hsp70c also occurred upon heat stimulation. A homogeneous distribution of the accumulated hsp70i and hsp70c throughout the nuclei and cytoplasm paralleled the development of heat-induced resistance to moderate H2O2challenge. Application of another hsp inducer, ethyl alcohol, evoked a similar pattern of H2O2resistance, and hsp induction and distribution. Our results suggest that induction and subcellular distribution of hsp70s contribute importantly to cellular antioxidant defenses, and that a co-operation between hsp70i and hsp70c may improve cardiac preservation during oxidative insult.