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3)-ß-D-glucans
,
,**,**
* Departments of Pharmacology,
Surgery,
Internal Medicine, and
# Medical Education, East Tennessee State University, James H. Quillen College of Medicine, Johnson City;
|| Department of Chemistry, Tulane University, New Orleans, Louisiana;
Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia; and
** James H. Quillen Veterans Administration Medical Center, Mountain Home, Tennessee
Correspondence: Peter J. Rice, Pharm.D., Ph.D., Department of Pharmacology, East Tennessee State University, James H. Quillen College of Medicine, Dogwood Lane, Building 119, Room 1-29, Johnson City, TN 37614-1708. E-mail: rice{at}etsu.edu
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.
Key Words: macrophage • acetylated LDL • binding • surface plasmon resonance
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