Differences in adaptive stabilization of structures in response to stress and hypoxia relate with the accumulation of hsp70 isoforms.
The phenomenon of adaptive stabilization of structures (PhASS) develops during adaptation of the organism to intermittent restraint stress. The PhASS manifests itself in a considerably increased resistance of the heart to a broad spectrum of harmful factors. In the present work, the content of hsp70 and their role in the development of PhASS during adaptation to intermittent restraint stress and to intermittent hypoxia were studied. In adaptation to restraint stress, five hsp70 isoforms with pI ranging from 5.7 to 6.3 were accumulated in the myocardium. The heart simultaneously became strikingly resistant to reperfusion paradox and heat shock. In adaptation to hypoxia, only two hsp70 isoforms with pI about 5.8 were accumulated. The resistance to reperfusion paradox was not increased and the resistance to heat shock was increased only moderately. These data suggest a role of different hsp70 isoforms in the mechanism of PhASS as well as adaptive protection of the heart.
Meerson
F Z
FZ
Institute of General Pathology and Pathological Physiology, USSR Academy of Medical Sciences, Moscow.
Malyshev IYu
Zamotrinsky
A V
AV
D000222:Adaptation, Physiological / Q000502:physiology*; D000818:Animals; D003402:Creatine Kinase / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000302:isolation & purification / Q000378:metabolism*; D000860:Hypoxia / Q000378:metabolism* / Q000503:physiopathology; D066298:In Vitro Techniques; D007511:Ischemia / Q000503:physiopathology; D008297:Male; D009200:Myocardial Contraction; D051381:Rats; D011919:Rats, Inbred Strains; D012149:Restraint, Physical / Q000009:adverse effects; D013312:Stress, Physiological / Q000378:metabolism* / Q000503:physiopathology
D006360:Heat-Shock Proteins; D003402:Creatine Kinase