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CD36, a Member of Class B Scavenger Receptor Family, Is a Receptor for Advanced Glycation End Products

Abstract: Interaction of advanced glycation end products (AGE) with AGE‐receptors induces several cellular phenomena relating potentially to diabetic complications. Five AGE‐receptors identified so far are RAGE (receptor for AGE), 80 K‐H, OST‐48, galectin‐3, and SR‐A (macrophage scavenger receptor type I and II). Since SR‐A belongs to the class A scavenger receptor family and the scavenger receptor collectively represents a family of multiligand lipoprotein receptors, it is possible that CD36 belonging to the class B scavenger receptor family (SR‐B) can recognize AGE‐proteins as a ligand. This was tested in the present study at the cellular level using CHO (Chinese hamster ovary) cells overexpressing human CD36 (CHO‐CD36 cells). 125I‐AGE‐BSA (bovine serum albumin) was endocytosed in a dose‐dependent fashion and underwent lysosomal degradation by CHO‐CD36 but not wild‐type CHO cells. Endocytic uptake of 125I‐AGE‐BSA by these cells was inhibited 50% by oxidized LDL (Ox‐LDL) and 60% by FA6‐152, an anti‐CD36 antibody inhibiting cellular binding of Ox‐LDL. Our results indicate that CD36 expressed by these cells mediates endocytic uptake and subsequent intracellular degradation of AGE‐proteins. Because CD36 is one of the major Ox‐LDL receptors and is upregulated in macrophage‐ and smooth muscle cell‐derived foam cells in human atherosclerotic lesions, the present results suggest that, like Ox‐LDL, AGE‐proteins generated in situ are recognized by CD36, which might contribute to the pathogenesis of diabetic macrovascular complications.