Saturation, competition, and specificity in interaction of heat shock proteins (hsp) gp96, hsp90, and hsp70 with CD11b(+) cells

Citation
Rj. Binder et al., Saturation, competition, and specificity in interaction of heat shock proteins (hsp) gp96, hsp90, and hsp70 with CD11b(+) cells, J IMMUNOL, 165(5), 2000, pp. 2582-2587
Citations number
27
Categorie Soggetti
Immunology
Journal title
JOURNAL OF IMMUNOLOGY
ISSN journal
00221767 → ACNP
Volume
165
Issue
5
Year of publication
2000
Pages
2582 - 2587
Database
ISI
SICI code
0022-1767(20000901)165:5<2582:SCASII>2.0.ZU;2-D
Abstract
Heat shock proteins (hsp(s)) have been postulated to interact with APCs thr ough specific receptors, although the receptor are yet to be identified. Sp ecificity, 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 interac tion, Interestingly, the phylogenetically related hsp90 also competes quite effectively with gp96 for binding to macrophages, whereas the unrelated hs p70 does so relatively poorly, although it binds CD11b(+) cells just as eff ectively, 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.