Heat shock proteins: Changes related to aging, development of thrombotic complications, and peptide regulation of the genome

Abstract

Heat shock proteins (HSPs), which have been shown by A. Tissieres et al. [78] to be strongly induced by elevated temperatures, have recently attracted spe cial attention from researchers. In addition to temper ature elevation, the biosynthesis of HSPs is induced by other factors: toxins, anoxia, hypoxia, ischemia, che motherapeutic agents, carcinogens, and even con comitantly the differentiation and development of cells and tissues. Intensive HSP synthesis occurs in infectious diseases, inflammation, fever, ultraviolet irradiation, exposure to electromagnetic fields and heavy metal salts, alkalosis and acidosis, exposure to lipopolysaccharides, ischemia, hypoxia, cytokine attack, and exposure to animal and plant toxins. Con sequently, these proteins are also called stress proteins [79]. HSPs are found both inside the cell and on the cell membrane [13,27].According to the universally accepted classification, all HSPs are subdivided into six families depending on their molecular mass in kilodaltons. Heat shock pro teins with molecular mass lower than 40 kDa are included into the small HSP (sHSP) family. Other HSP proteins belong to families called HSP70, HSP80, HSP90, HSP100, and HSP with molecular masses of 1 A review of published data and the authors' own results. 110 kDa and above. HSPs with molecular masses of 70 kDa are of special interest due to the high levels of these proteins in tissues under stressful conditions. These proteins have been studied in the greatest detail and their role in the functioning of organs and tissues has been established. HSP70 was shown to be the main molecular chaperone involved in the utilization of irre versibly damaged proteins, or folding [40,43,44].What do chaperone (chaperone is a French word for an elderly lady accompanying a young girl to the ball) functions include? Newly synthesized proteins are known to have tertiary and quaternary structure. High temperature and stress to which the cell is exposed cause the formation of anomalous proteins due to aggregation. The functions of HSP in the regu lation of correct folding (structure formation) of newly synthesized proteins and the destruction of anomalous protein aggregates are called chaperone functions, and the proteins themselves are called chaperones. There fore, the main function of HSPs is the protection of the cell from damaging factors. Furthermore, HSPs are nonspecific adaptogens that protect the cells from various stressors.In addition to HSP70, the chaperone group includes HSP22, HSP27, HSP60, and HSP90. The propensity for chaperoning is determined by the struc ture of the chaperone proteins, which are able to Abstract-The present review of published data and the authors' own results addresses the role of heat shock proteins in the regulation of cell and tissue homeostasis and considers the decrease in their expression levels as one of the main factors of aging. Heat shock proteins are involved in the regulation of proliferation, apop tosis, and differentiation of cells, as well as in that of intracellular homeos...

Genetic characterization, structural analysis, and detection of positive selection in small heat shock proteins of Cypriniformes and Clupeiformes

“…sHsps showed a low degree of conservation because of the varied evolutionary paths they had taken in the past. The sHsp family of heat shock proteins, exhibits evolutionary divergence and substantial sequence variation (53). In addition, sHsps proteins have a variety of roles because, in contrast to other Hsps, these proteins do not have a known constitutive function and are only activated when the cell is subjected to stress.…”

Evaluating Occupational Morbidity Among Energy Enterprise Employees In Industrial Region Of Kazakhstan

“…A decrease in the synthesis of stress proteins under constant exposure to EMF could predispose to oncogenesis. A few authors noted a decrease in the expression of heat shock proteins with age, which indicated a change in adaptation to the effects of EMF in older age groups, along with an increased risk of various pathogenetic processes [9].…”

Peptides: Prospects for Use in the Treatment of COVID-19

“…Experimental use of thymalin and thymogen and their administration in patients with pneumonia of various etiologies and viral infectious diseases was accompanied by a normalization of the coagulation process and fibrinolytic activity of the blood [ 96 , 97 ]. Combined with the immunoprotective properties of these drugs, this may contribute to the effectiveness of treatment for patients with COVID-19 [ 98 , 99 ].…”