Exogenously delivered heat shock protein 70 displaces its endogenous analogue and sensitizes cancer cells to lymphocytes-mediated cytotoxicity.

摘要: // Maxim A. Shevtsov 1,* , Elena Y.Komarova Darya Meshalkina Natalia V. Bychkova 2 Nikolai D. Aksenov 1 Sergey Abkin Boris Margulis Irina Guzhova Institute of Cytology Russian Academy Sciences, St. Petersburg, Russia Laboratory Clinical Immunology, EMERCOM Russia, St.Petersburg, * These authors contributed equally to this work Correspondence: Guzhova, email: Keywords : heat shock protein 70, intra-, extracellular transport, cytotoxic lymphocytes, cancer cell. Received January 18, 2014 Accepted March 20, Published 22, Abstract Hsp70 chaperone is known stimulate anti-tumour immunity in a variety models. Here we demonstrated that the addition purified recombinant culture medium facilitated cell cytolysis by lymphocytes. Importantly, exogenous triggered secretion intracellular surface and milieu, which played role because down-regulation endogenous reduced both its presence at lymphocyte-mediated cytolysis. Inhibitors target ATPase peptide-binding domains molecule potently decreased anti-tumor effect. Using transport markers inhibitors, showed exchange supported classical non-classical pathways, with particular lipid rafts chaperone’s transport. In conclusion, can eject Hsp70, thus exerting anticancer activity.