T Cell Response with Stress Proteins

我们的研究表明，70ka热休克蛋白（hsp70）在将主要组织相容性抗原复合物（MHC） i类结合的抗原肽提供给与抗原加工相关的转运体（TAP）方面发挥了重要作用，并揭示了一种新的可能性，即MHC i类结合的肽库可能在细胞质中受到限制，至少部分限制是由于它们与分子伴侣hsp70的亲和力。我们还发现多胺参与了hsp70和TAP之间的相互作用，提示多胺可能在肿瘤逃逸机制中发挥作用。也有人认为，某种形式的hsp70在细胞表面表达，但机制尚不清楚。我们目前的数据支持这样一种观点，即hsp70样分子可以与细胞肽抗原一起呈递给具有T细胞受体(TCR) γδ链的特定T细胞。由于这种hsp70样分子在细胞表面的表达通常伴随着被激活的癌基因的细胞转化而被诱导，因此具有TCR Vδ6家族的T细胞很可能有助于宿主对肿瘤细胞的抵抗。

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.