Heat Shock Protein HSP70 in Oxidative Stress in Apnea Patients
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Bulletin of Experimental Biology and Medicine, Vol. 169, No. 5, September, 2020 EXPERIMENTAL METHODS FOR CLINICAL PRACTICE
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Heat Shock Protein HSP70 in Oxidative Stress in Apnea Patients I. M. Madaeva1, N. A. Kurashova1, N. V. Semenova1, E. B. Ukhinov1, S. I. Kolesnikov2,3, and L. I. Kolesnikova1
Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 169, No. 5, pp. 627-630, May, 2020 Original article submitted January 16, 2020 We studied the level of heat shock protein HSP70 under conditions of oxidative stress in 47 patients with apnea. The control group included 13 healthy subjects without verified apnea. Blood serum, plasma, and erythrocyte hemolysate were used to determine LPO and antioxidant protection components by spectrophotometrical and spectrofluorometrical methods. HSP70 was assayed by ELISA. A direct relationship was established between the intensity of oxidative stress and HSP70 expression in patients with apnea. Quantitative determination of HSP70 can be used as a molecular marker in the early diagnosis and prognosis of the development of various pathological conditions in hypoxia. Key Words: hypoxia; heat shock proteins; oxidative stress; apnea The body response to the action of stress factors is characterized by the level of stress response, orga nism’s reactivity, and its adaptive capabilities [1]. Expression of heat shock proteins, e.g. HSP70, is one of the first cell reactions to stress [15]. We have previously demonstrated that the main stress factor in the form of long-term and “intermittent” limitation of oxygen supply to cells in obstructive sleep apnea leads to the redox balance dysregulation [3,4,11]. Heat shock proteins HSP are synthesized in response to any situation that threatens cell survival [5,8]. Heavy metals, ethanol, oxygen radicals, and peroxides are far from a complete list of agents that cause heat shock reaction. HSP70 family proteins exhibit the properties of enzymes that correct conformational changes in proteins by utilizing ATP energy and promote transmembrane translocation of proteins. These proteins are among the first to respond to oxidative stress, protecting enzymes and other proteins from exposure to ROS [13-15]. Research Centre for Family Health and Human Reproduction Problems, Irkutsk; 2M. V. Lomonosov Moscow State University; 3Moscow State Regional University, Moscow, Russia. Address for correspondence: [email protected]. I. M. Madaeva 1
It is known that HSP70 plays an important role in restoring sleep [5]. Close integration of HSP70 molecular systems in the “sleep-promoting center” in the preoptic region of the hypothalamus and their compensatory relationships contribute significantly to the maintenance of sleep homeostasis [9,10]. Cyclic changes in the rate of protein synthesis (in episodes of deep slow-wave sleep) and the expression of HSP70 chaperones (in wakeful episodes) that occur daily throughout life are critical for all vital processes of homeotherms, including restoration of the structure and function of the nervous system [6]
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