Dynamics of formation and reversion of the phenomenon of adaptational stabilization of structures correlates with changes in HSP70 content in the myocardium
Autor: | O. P. Budanova, F. Z. Meerson, I. Yu. Malyshev, A. V. Zamotrinskii |
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Rok vydání: | 1993 |
Předmět: | |
Zdroj: | Bulletin of Experimental Biology and Medicine. 116:919-923 |
ISSN: | 1573-8221 0007-4888 |
Popis: | The phenomenon of adaptational stabilization of structures (PASS) implies that adaptation of the organism to stress influences enhances the resistance not only of the whole organism but also of isolated organs, primarily of the heart, to a broad spectrum of damaging factors from toxic concentrations of catecholamines to the reperfusion paradox and heat damage [2,3,8]. The resistance of cell structures such as the sarcoplasmic reticulum, mitochondria [3,7], and nuclei [1] also increases. PASS has been found to be realized against the background of a considerably increased content of heat-shock proteins (hsp70) in the myocardium, together with alterations in their isoform composition and subceUular distribution [1,8]. However, some essential questions are not yet answered. How rapid is the rate of formation of PASS and of the cardioprotective effects and how long do they persist after termination of the adaptation sessions? What is the pattern of dynamics of hsp70 isoform composition during adaptation and after its termination? Does the dynamics of the protective adaptation effect follow the changes in the hspT0 content in the myocardium? Answers to these questions are necessary not only for understanding the |
Databáze: | OpenAIRE |
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