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Human monocyte scavenger receptors are pattern recognition receptors for (1→3)‐β‐D‐glucans
Author(s) -
Rice Peter J.,
Kelley Jim L.,
Kogan Grigorij,
Ensley Harry E.,
Kalbfleisch John H.,
Browder I. William,
Williams David L.
Publication year - 2002
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.72.1.140
Subject(s) - scavenger receptor , receptor , biology , laminarin , biochemistry , u937 cell , monocyte , microbiology and biotechnology , pattern recognition receptor , innate immune system , glucan , surface plasmon resonance , biophysics , lipoprotein , immunology , polysaccharide , materials science , cholesterol , in vitro , nanotechnology , nanoparticle
Glucans are cell wall constituents of fungi and bacteria that bind to pattern recognition receptors and modulate innate immunity, in part, by macrophage activation. We used surface plasmon resonance to examine the binding of glucans, differing in fine structure and charge density, to scavenger receptors on membranes isolated from human monocyte U937 cells. Experiments were performed at 25°C using a biosensor surface with immobilized acetylated low density lipoprotein (AcLDL). Inhibition of the binding by polyinosinic acid, but not polycytidylic acid, confirmed the interaction of scavenger receptors. Competition studies showed that there are at least two AcLDL binding sites on human U937 cells. Glucan phosphate interacts with all sites, and the CM‐glucans and laminarin interact with a subset of sites. Polymer charge has a dramatic effect on the affinity of glucans with macrophage scavenger receptors. However, it is also clear that human monocyte scavenger receptors recognize the basic glucan structure independent of charge.