Cytoprotective Mechanism of Heat Shock Protein 70 against Hypoxia/Reoxygenation Injury
| Autor: | Yoko Han-no, Ken-ichiro Kawana, Yuki Miyamoto, Kouichi Tanonaka, Hiroyuki Yoshida, Masaya Takahashi, Satoshi Takeo |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Male
Hyperthermia Hot Temperature Time Factors Fever Blotting Western Biology Phosphates chemistry.chemical_compound Heat shock protein medicine Animals HSP70 Heat-Shock Proteins Enzyme Inhibitors Rats Wistar Creatine Kinase Molecular Biology Cell Nucleus Myocardium Temperature Hypoxia (medical) medicine.disease Cytoprotection Cell Hypoxia Rats Hsp70 Cell biology medicine.anatomical_structure chemistry Biochemistry 3-Aminobenzamide Benzamides Electrophoresis Polyacrylamide Gel Hypoxia reoxygenation Poly(ADP-ribose) Polymerases medicine.symptom Cardiology and Cardiovascular Medicine Nucleus |
| Zdroj: | Journal of Molecular and Cellular Cardiology. 32:2229-2237 |
| ISSN: | 0022-2828 |
| DOI: | 10.1006/jmcc.2000.1250 |
| Popis: | The role of heat shock protein 70 (HSP70) in the cytoprotection against hypoxia/reoxygenation injury was examined. Adult rat cardiomyocytes were isolated, subjected to hyperthermia at 42 degrees C for 15 min (heat shock treatment), and then incubated at 37 degrees C for 3 to 24 h (HSP production process). Heat shock treatment increased HSP70 production (80-260% increase); the peak increase was seen after 9 h of HSP production process. Thereafter, the cells were subjected to 120-min hypoxia and 15-min reoxygenation. Heat shock treatment increased the survival of the cells subjected to hypoxia/reoxygenation (1.5-2.5-fold); the maximal cytoprotection was observed after 12 h of HSP production process. Heat shock treatment increased HSP70 content in the nucleus when cells were subjected to 12 h of HSP production process. To examine the role of HSP70 accumulation in the nuclear fraction, the activity of poly(ADP-ribose) synthetase (PARS), which functions in the nucleus and consumes high-energy phosphates excessively in the reoxygenated state, were measured in the cells with heat shock and 12 h of HSP production process. Heat shock treatment attenuated the hypoxia/reoxygenation-induced increase in the PARS activity (50% decrease). Treatment of the cells with 3-aminobenzamide, an inhibitor of PARS, exerted the effects similar to those of heat shock treatment. These results suggest that attenuation of the PARS activity in the nucleus may play an important role in the cytoprotective effect of HSP70 on hypoxia/reoxygenation injury. |
| Databáze: | OpenAIRE |
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