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

Akihiko Kuniyasu; Nobutaka Ohgami; Shigeki Hayashi; Akira Miyazaki; Seikoh Horiuchi; Hitoshi Nakayama

doi:10.1016/S0014-5793(03)00096-6

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

Akihiko Kuniyasu, Nobutaka Ohgami, Shigeki Hayashi, Akira Miyazaki, Seikoh Horiuchi, Hitoshi Nakayama

Research output: Contribution to journal › Article › peer-review

83 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	85-90
Number of pages	6
Journal	FEBS Letters
Volume	537
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(03)00096-6
Publication status	Published - 27-02-2003
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0014-5793(03)00096-6

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title = "CD36-mediated endocytic uptake of advanced glycation end products (AGE) in mouse 3T3-L1 and human subcutaneous adipocytes",

abstract = "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.",

author = "Akihiko Kuniyasu and Nobutaka Ohgami and Shigeki Hayashi and Akira Miyazaki and Seikoh Horiuchi and Hitoshi Nakayama",

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T1 - CD36-mediated endocytic uptake of advanced glycation end products (AGE) in mouse 3T3-L1 and human subcutaneous adipocytes

AU - Kuniyasu, Akihiko

AU - Ohgami, Nobutaka

AU - Hayashi, Shigeki

AU - Miyazaki, Akira

AU - Horiuchi, Seikoh

AU - Nakayama, Hitoshi

PY - 2003/2/27

Y1 - 2003/2/27

N2 - 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.

AB - 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.

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JF - FEBS Letters

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ER -

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

Abstract

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UN SDGs

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