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Originally published online as doi:10.1189/jlb.0109005 on March 10, 2009

Published online before print March 10, 2009
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(Journal of Leukocyte Biology. 2009;85:905-910.)
© 2009 by Society for Leukocyte Biology

Heat shock proteins and immune system

Min-Fu Tsan1 and Baochong Gao

Research Service, Veterans Affairs Medical Center, Washington, DC, USA

1 Correspondence: Mid-Atlantic Regional Office (10R), Office of Research Oversight, Department of Veterans Affairs, 50 Irving Street, N.W., Washington, DC 20422, USA. E-mail: min-fu.tsan2{at}va.gov

Heat shock proteins (HSPs) such as HSP 60 (Hsp60), Hsp70, Hsp90, and gp96, have been reported to play important roles in antigen presentation and cross-presentation, activation of macrophages and lymphocytes, and activation and maturation of dendritic cells. HSPs contain peptide-binding domains that bind exposed hydrophobic residues of substrate proteins. As part of their molecular chaperone functions, HSPs bind and deliver chaperoned, antigenic peptides to MHC class I molecules at the cell surface for presentation to lymphocytes. HSPs also bind nonprotein molecules with exposed hydrophobic residues including lipid-based TLR ligands. Recombinant HSP products may be contaminated with pathogen-associated molecules that contain exposed hydrophobic residues such as LPS (a TLR4 ligand), lipoprotein (a TLR2 ligand), and flagellin (a TLR5 ligand). These contaminants appear to be responsible for most, if not all, reported in vitro cytokine effects of HSPs, as highly purified HSPs do not show any cytokine effects. We propose that HSPs are molecular chaperones that bind protein and nonprotein molecules with exposed hydrophobic residues. The reported antigen presentation and cross-presentation and in vitro HSP cytokine functions are a result of molecules bound to or chaperoned by HSPs but not a result of HSPs themselves.

Key Words: molecular chaperone • antigen presentation • macrophages • dendritic cells • cytokines




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