CD36‐mediated endocytic uptake of advanced glycation end products (AGE) in mouse 3T3‐L1 and human subcutaneous adipocytes

FEBS Letters

Kuniyasu, Akihiko¹  Nakayama, Hitoshi¹  Horiuchi, Seikoh²  Ohgami, Nobutaka¹  Hayashi, Shigeki¹  Miyazaki, Akira² 

[1] Department of Biofunctional Chemistry, Faculty of Pharmaceutical Sciences, Kumamoto University, 5-1 Ohe-Honmachi, Kumamoto 862-0973, Japan;Department of Biochemistry, Kumamoto University School of Medicine, 2-2-1 Honjo, Kumamoto 860-0811, Japan

关键词: Adipocytes;    Advanced glycation end product;    CD36;    Receptor for advanced glycation end product;    AGE;    advanced glycation end product;    AGE-BSA;    advanced glycation end product-modified bovine serum albumin;    LDL;    low density lipoprotein;    OxLDL;    oxidized LDL;    SR-A;    scavenger receptor class A;   

DOI  :  10.1016/S0014-5793(03)00096-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown