Arteriosclerosis, Thrombosis, and Vascular Biology. 1995;15:269-275
© 1995 American Heart Association, Inc.
Articles |
Oxidized LDL Binds to CD36 on Human Monocyte-Derived Macrophages and Transfected Cell Lines
Evidence Implicating the Lipid Moiety of the Lipoprotein as the Binding Site
From the Departments of Pathology (A.C.N.) and Medicine (S.F.A.P., R.L.S.), Cornell University Medical College, New York, NY.
Correspondence to Andrew C. Nicholson, Cornell University Medical College, Department of Pathology, Room A-626, New York, NY 10021.
Abstract Accumulating evidence strongly implicates oxidized LDL (Ox-LDL) in the pathogenesis of atherosclerosis. Several receptors have been identified that bind and internalize Ox-LDL, but their relative importance in vivo is unclear. CD36 is an 88-kD transmembrane glycoprotein expressed on monocytes/macrophages, platelets, and microvascular endothelium that has been implicated as a putative receptor for Ox-LDL. We demonstrate that an anti-CD36 monoclonal antibody inhibited 50% of the specific binding and 26% of the specific degradation of Ox-LDL by human monocyte–derived macrophages. To characterize more completely this binding we evaluated interactions between CD36 and Ox-LDL in murine NIH-3T3 cells stably transfected with human CD36 cDNA. Ox-LDL bound to CD36-transfected 3T3 cells in a saturable manner. Specific binding, internalization, and degradation of Ox-LDL were increased fourfold in CD36-transfected cell lines compared with 3T3 cells transfected with vector alone. Binding of Ox-LDL to CD36-transfected 3T3 cells was inhibited by a panel of anti-CD36 antibodies and by soluble CD36 but not by thrombospondin. Specificity of binding was demonstrated by the equivalent binding of LDL and acetylated LDL to control and CD36-transfected 3T3 cells. The epitope or epitopes on Ox-LDL recognized by CD36 are undefined. Two observations suggest that CD36 recognizes a lipid moiety or that the lipid portion of the lipoprotein is essential for apoprotein recognition. The first is that the increased binding of Ox-LDL to CD36-transfected 3T3 cells is abrogated by delipidation of the lipoprotein, and the second is that oleic acid competes for the binding of Ox-LDL to CD36-transfected 3T3 cells. These data demonstrate that CD36 functions as an Ox-LDL receptor and suggest that CD36 may play a functional role in lipid accumulation by human macrophages and subsequent foam cell development during atherosclerosis.
Key Words: CD36 • oxidized LDL • macrophage • scavenger receptor • atherosclerosis
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S. S. Davies, A. V. Pontsler, G. K. Marathe, K. A. Harrison, R. C. Murphy, J. C. Hinshaw, G. D. Prestwich, A. St. Hilaire, S. M. Prescott, G. A. Zimmerman, et al. Oxidized Alkyl Phospholipids Are Specific, High Affinity Peroxisome Proliferator-activated Receptor gamma Ligands and Agonists J. Biol. Chem., May 4, 2001; 276(19): 16015 - 16023. [Abstract] [Full Text] [PDF]
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