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Activation of natural killer cells by heat shock protein 70.
Int. J. Hyperthermia 25, 169-175 (2009)
Intracellular heat shock proteins (HSP) function as molecular chaperones, they support folding and transport mechanisms of other proteins under physiological conditions and following physical or chemical stress. More recently, extracellular localized HSP have been found to play key roles in the induction of a cellular immune response. Either they act as carrier molecules for immunogenic peptides that are presented on Antigen Presenting Cells (APC) to cytotoxic T-cells or they themselves act as activatory molecules for the innate immune system. Binding of uncomplexed HSP to HSP-receptors on APC has been found to induce the secretion of inflammatory cytokines. Furthermore, an unusual tumor-selective membrane-localization of non-conserved regions of the 72 000 Da HSP (Hsp70) has been found to act as a recognition structure for natural killer (NK) cells. In this review the interaction of NK cells with Hsp70 or peptides derived thereof will be eluciated in more detail.
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Publication type
Article: Journal article
Document type
Review
Keywords
NK cells; Hsp70-receptor; Hsp70 activatory peptide; tumor kill; heat-shock-protein; human tumor-cells; inducible immunogenic determinant; nk cells; antigen presentation; surface expression; t-lymphocytes; sarcoma-cells; in-vivo; receptor
ISSN (print) / ISBN
0265-6736
e-ISSN
1464-5157
Quellenangaben
Volume: 25,
Issue: 3,
Pages: 169-175
Publisher
Informa Healthcare
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
CCG Innate Immunity in Tumor Biology (PATH-KTB)