Saturation, Competition, and Specificity in Interaction of Heat Shock Proteins (hsp) gp96, hsp90, and hsp70 with CD11b+ Cells

Heat shock proteins (hsp(s)) have been postulated to interact with APCs through specific receptors, although the receptors are yet to be identified. Specificity, saturation, and competition are the three defining attributes of a receptor-ligand interaction. We demonstrate here that the interaction o...

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Bibliographic Details
Published in:The Journal of immunology (1950) 2000-09, Vol.165 (5), p.2582-2587
Main Authors: Binder, Robert J, Harris, Michelle L, Menoret, Antoine, Srivastava, Pramod K
Format: Article
Language:English
Subjects:
Animals
Antigen-Presenting Cells - immunology
Antigen-Presenting Cells - metabolism
Antigens, Neoplasm - administration & dosage
Antigens, Neoplasm - immunology
Antigens, Neoplasm - metabolism
Binding, Competitive - immunology
Cell Membrane - immunology
Cell Membrane - metabolism
Endocytosis - immunology
Epitopes - immunology
Epitopes - metabolism
Fluorescein-5-isothiocyanate - metabolism
Heat-Shock Proteins - administration & dosage
Heat-Shock Proteins - immunology
Heat-Shock Proteins - metabolism
HSP70 Heat-Shock Proteins - administration & dosage
HSP70 Heat-Shock Proteins - immunology
HSP70 Heat-Shock Proteins - metabolism
HSP90 Heat-Shock Proteins - administration & dosage
HSP90 Heat-Shock Proteins - immunology
HSP90 Heat-Shock Proteins - metabolism
Injections, Intraperitoneal
Macrophage-1 Antigen - biosynthesis
Mice
Mice, Inbred C57BL
Peritoneal Cavity - cytology
Protein Binding - immunology
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Summary:Heat shock proteins (hsp(s)) have been postulated to interact with APCs through specific receptors, although the receptors are yet to be identified. Specificity, saturation, and competition are the three defining attributes of a receptor-ligand interaction. We demonstrate here that the interaction of the heat shock proteins gp96 and hsp90 with CD11b+ cells is specific and saturable and that gp96 can compete with itself in gp96-macrophage interaction. Interestingly, the phylogenetically related hsp90 also competes quite effectively with gp96 for binding to macrophages, whereas the unrelated hsp70 does so relatively poorly, although it binds CD11b+ cells just as effectively. These data provide evidence that the heat shock proteins interact with APCs with specificity and for the existence of at least two distinct receptors, one for gp96 and hsp90 and the other for hsp70.
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.165.5.2582