[Dual role of chaperones in the response of a cell and of a whole organism to stress].
Chaperones constitute a class of proteins able to recognize newly synthesized and(or) damaged polypeptides and to transport these to the sites of their allocation or promote the degradation of irreversibly spoiled ones. The members of Hsp70 family can be classified as the first-discovered chaperones, and to date the chaperonic mechanism based on the proteins is well understood. Using this mechanism Hsp70 executes the dual role: it corrects the structure of nascent and damaged polypeptides or promotes degradation of incorrigible polypeptides. Chaperonic activity appears to form key functions of Hsp70, protective and adjuvant ones. The former is proved in a large amount of experiments both in vitro and in vivo. From the beginning of the 2000th, it has become clear that Hsp70 can be released by cells treated by a number of stressful factors, and exogenous chaperone can influence the cells of innate immunity system proving that the protein uses its protective power already at a level of the whole organism. One of the goals of this review is to describe the functions performed by Hsp70 inside and outside a cell. In a view of its properties Hsp70 can be of significant interest for creation of novel therapeutic technologies. This direction to the practical application of the chaperone is also considered in the review.
B A
BA
Margulis
I V
IV
Guzhova
D000818:Animals; D017209:Apoptosis; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D006816:Huntington Disease / Q000378:metabolism / Q000628:therapy; D007113:Immunity, Innate; D018832:Molecular Chaperones / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism / Q000628:therapy; D017510:Protein Folding; D015398:Signal Transduction; D013312:Stress, Physiological
D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones