Heat shock proteins in the obesity pathogenesis

The pathogenesis of obesity is complex and includes multiple links. Recent research has shown that the mechanisms of inflammation and responses to cellular stress are closely interrelated and form a vicious cycle, which largely explains the development of obesity-associated diseases. A family of highly conserved proteins called heat shock proteins (HSPs) protects tissues and organs from stress by performing their biological functions. In pathological processes, this protective system is decompensated. Objective. To analyze the results of non-clinical and clinical studies of the role of heat shock proteins 70, 72, 60, 40, and 27 in the pathogenesis of obesity. Materials and methods. Scientific papers were searched using the PubMed and eLibrary databases with the following keywords: heat shock proteins 70, 72, 60, 40, 27; chaperone; obesity; obesity markers; adipose tissue; metabolic syndrome. Results. Studies have shown that HSP70 and glucose-regulated HSP of 78 kDa (GRP 78) contribute to decreased insulin sensitivity, increased glycemia, and the development of hepatic steatosis through activation of stress kinases and phosphorylation of insulin receptor substrates. The opposite effect was observed with HSP72 induction, which is considered a potential way to prevent and treat obesity and type 2 diabetes mellitus. It was reported that HSP60 acts as a mediator of the immune response in obesity, type 2 diabetes, cancer, and atherosclerosis, and that this protein belongs to the class of adipokines with adverse metabolic effects. The progression of obesity involves HSP27, a marker of inflammation. Conclusion. Identification of serum heat shock proteins as biological markers in overweight and obese individuals with or without various interventions will help clarify the natural course of obesity.