Hsp70 CHAPERONE AND THE PROSPECTS OF ITS APPLICATION IN ANTICANCER THERAPY
I. V. Guzhova,1 S. S. Novoselov, B. A. Margulis
Institute of Cytology RAS, St. Petersburg, Russia;
1 e-mail: guzhova@mail.cytspb.rssi.ru
Major stress protein Hsp70 is known to possess two important properties: ATP-dependent activity and protective
activity; these two are thought to play a significant role in anticanccr therapy. Many malignant tumors contain high amounts of
intracellular Hsp70. Moreover, many anticancer drugs themselves are able to elevate Hsp70 expression in tumor cells. Since Hsp70 was
found to disturb many signal pathways of apoptosis in many points, the high chaperone expression may lead to an increased resistance
of tumor cells to anticancer drugs. On the other hand, when overexpressed by a certain mechanism, Hsp70 is able to emerge at the cell
surface by itself or together with tumor antigens and present these to immune cells T-lymphocytes and natural killers, in such a
manner that makes cancer cell recognized and abolished. These properties make Hsp70 very promising instrument in designing some
novel anticancer vaccines.
Key words: chaperone, heat shock protein Hsp70, tumor cell, anticancer therapy, immunomodulator
|
