Heat shock proteins and the antitumor T cell response |
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Authors: | Mamoru Harada Genki Kimura Kikuo Nomoto |
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Institution: | (1) Departments of Virology and Immunology, Medical Institute of Bioregulation, Kyushu University, 812-82 Fukuoka, Japan |
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Abstract: | Heat shock proteins (HSP) have been shown to participate in the antitumor T cell response. First, HSP play a crucial role
in the intracellular pathway for antigen processing where HSP can make complexes with a broad spectrum of cellular proteins
and peptides through their chaperone functions. In this pathway, macrophages are required for processing the chaperoned peptides
to make stable molecules with the major histocompatibility complex (MHC) class I molecules, even when HSP-peptide complexes
are exogenously administered. Through this pathway, vaccination with HSP-peptide complexes is thus able to elicit the response
of CD8+ T cells specific for the chaperoned peptides. These findings suggest an essential role of HSP in ‘cross-priming’ and their
usefulness for antitumor vaccination with tumor peptides. Second, HSP have been suggested to be expressed on the cell surface
by transformation and, in addition, to function as antigen-presenting molecules for double negative T cells. Third, HSP derived
from tumor cells have reportedly been recognized by T cells with either T cell receptor (TCR)-αβ or TCR-γδ. These lines of evidence therefore indicate that HSP may be potentially promising target molecules for antitumor T cell immunotherapy. |
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Keywords: | heat shock protein chaperone peptide cross-priming |
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