Interaction of advanced glycation end products (AGE) with AGE receptors induces several cellular phenomena potentially relating to diabetic complications. We here show that AGE‐modified bovine serum albumin (BSA) is endocytosed by adipocytes via CD36. Upon differentiation, 3T3‐L1 and human subcutaneous adipose cells showed marked increases in endocytic uptake and subsequent degradation of [125I]AGE‐BSA, which were inhibited effectively by the anti‐CD36 antibody. Ligand specificity of CD36 for modified BSAs was compared with that of LOX‐1 and scavenger receptor class A. Effect of fucoidan on [125I]AGE‐BSA binding showed a sharp contrast to that on [125I]‐oxidized low density lipoprotein. These results implicate that CD36‐mediated interaction of AGE‐modified proteins with adipocytes might play a pathological role in obesity or insulin‐resistance.