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Immunology |
Units of Immunotherapy of Human Tumors [C. C., F. R., L. R., G. P.] and Immunohematology [A. M.], Istituto Nazionale per lo Studio e la Cura dei Tumori, 20133 Milan, Italy, and Department of Oncology/Pathology, Unit of Experimental Oncology, Karolinska Institutet, S17176 Stockholm, Sweden [A-M. T. C., R. K.].
Members of the heat shock protein 70 (HSP70) family display a broad
cellular localization and thus bind a repertoire of chaperoned peptides
potentially derived from proteins of different cellular compartments.
In this report, we show that HSP70 purified from human melanoma can
activate T cells recognizing melanoma differentiation antigens in an
antigen- and HLA class I-dependent fashion. HLA class I-restricted
antimelanoma T cells were susceptible to MHC-restricted,
HSP70-dependent stimulation, indicating that HSP70 complexed peptides
were able to gain access to the class I HLA presentation pathway. In
addition, MHC matching between the melanoma cells used as a source of
HSP and the responding T cells were not required, indicating that HSP70
activation may occur across MHC barriers. Besides the MHC-restricted
and peptide-dependent activation pathway, HSP70 with no endogenous
complexed peptides or HSP70 purified from antigen-negative cells was
also able to induce IFN-
release by antimelanoma T cells by a
MHC-independent mechanism. In this case, however, higher doses of HSP70
were required. The capacity to activate class I-restricted, antitumor T
cells as well as antigen-presenting cells, together with the finding
that the HSP70 chaperoned peptide repertoire includes melanoma-shared
epitopes, holds promise for a HSP70-based cancer vaccine.
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