Hsp70 chaperone as a survival factor in cell pathology.

Abstract

Heat shock protein Hsp70 is implicated in the mechanism of cell reaction to a variety of cytotoxic factors. The protective function of Hsp70 is related to its ability to promote folding of nascent polypeptides and to remove denatured proteins. Many types of cancer cells contain high amounts of Hsp70, whose protective capacity may pose a problem for therapy in oncology. Hsp70 was shown to be expressed on the surface of cancer cells and to participate in the presentation of tumor antigens to immune cells. Therefore, the chaperone activity of Hsp70 is an important factor that should be taken into consideration in cancer therapy. The protective role of Hsp70 is also evident in neuropathology. Many neurodegenerative processes are associated with the accumulation of insoluble aggregates of misfolded proteins in neural cells. These aggregates hamper intracellular transport, inhibit metabolism, and activate apoptosis through diverse pathways. The increase of Hsp70 content results in the reduction of aggregate size and number and ultimately enhances cell viability.