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CD36‐mediated endocytic uptake of advanced glycation end products (AGE) in mouse 3T3‐L1 and human subcutaneous adipocytes
Author(s) -
Kuniyasu Akihiko,
Ohgami Nobutaka,
Hayashi Shigeki,
Miyazaki Akira,
Horiuchi Seikoh,
Nakayama Hitoshi
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00096-6
Subject(s) - glycation , endocytic cycle , cd36 , microbiology and biotechnology , chemistry , adipogenesis , 3t3 l1 , 3t3 cells , medicine , biochemistry , biology , endocytosis , cell , adipose tissue , transfection , receptor , gene
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 [ 125 I]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 [ 125 I]AGE‐BSA binding showed a sharp contrast to that on [ 125 I]‐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.