A 14-mer peptide from HSP70 protein is the critical epitope which enhances NK activity against tumor cells in vivo.
Heat shock protein 70 (Hsp70) has been found to play key roles in tumor immunity due its chaperone function of binding antigenic peptides. Here we report it can also stimulate NK cells in vivo, which is another role in Hsp70s' anti-tumor response. Injecting Hsp70 into mice increased splenic NK cell populations, which may be reason for anti-tumor effect of Hsp70. The Hsp70 14-mer peptide (aa450-463, TRD) was identified as the critical epitope for this stimulatory activity. It was the murine Hsp70 14-mer peptide TRD instead of the corresponding human Hsp70 14-mer peptide TKD that functioned in the mouse experimental model.
Zhang
Honghai
H
Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai, PR China.
Liu
Rui
R
Huang
Weida
W
D000818:Animals; D003602:Cytotoxicity, Immunologic / Q000187:drug effects; D000939:Epitopes / Q000032:analysis; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000276:immunology / Q000494:pharmacology*; D007694:Killer Cells, Natural / Q000187:drug effects* / Q000276:immunology; D008213:Lymphocyte Activation; D051379:Mice; D010455:Peptides / Q000494:pharmacology; D013601:T-Lymphocytes / Q000187:drug effects / Q000276:immunology
D000939:Epitopes; D018840:HSP70 Heat-Shock Proteins; D010455:Peptides