T Cell Response with Stress Proteins

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Our study indicated the important role of the 70 kA heat shock proteins (hsp70) for feeding the major histocompatibility antigen complexes (MHC) class I-bound antigenic peptides to the transporters associated with the antigen processing (TAP), and revealed a novel possibility that the repertoire of MHC class I-bound peptides may be limited, at least in part, in the cytosol by their affinity to molecular chaperone hsp70. We also indicated an involvement of polyamines in the interaction between hsp70 and TAP, suggesting the possible role of polyamines in the tumor escape mechanisms.It was also suggested that some form of hsp70 is expressed on the cell surface with as yet unknown mechanism. Our current data support the notion that an hsp70-like molecule could be presented together with the cellular peptides antigens to particular T cells with the T-cell receptor (TCR) γδ chains. Since the expression of this hsp70-like molecule on the cell surface is usually induced along with cell transformation by activated oncogenes, it is likely that T cells with the TCR Vδ6 family contribute to the host's resistance to tumor cells.