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Elaidate, a trans fatty acid, suppresses insulin signaling for glucose uptake in a manner distinct from that of stearate.

Authors
  • Ishibashi, Kenichi1
  • Takeda, Yoshihiro1
  • Nakata, Lisa2
  • Hakuno, Fumihiko2
  • Takahashi, Shin-Ichiro2
  • Atsumi, Gen-Ichi3
  • 1 Department of Molecular Physiology and Pathology, Faculty of Pharma-Science, Teikyo University, Itabashi-ku, Tokyo, 173-8605, Japan. , (Japan)
  • 2 Department of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan. , (Japan)
  • 3 Department of Molecular Physiology and Pathology, Faculty of Pharma-Science, Teikyo University, Itabashi-ku, Tokyo, 173-8605, Japan. Electronic address: [email protected] , (Japan)
Type
Published Article
Journal
Biochimie
Publication Date
Oct 01, 2020
Volume
177
Pages
98–107
Identifiers
DOI: 10.1016/j.biochi.2020.07.021
PMID: 32822725
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The dietary intake of elaidate (elaidic acid), a trans-fatty acid, is associated with the development of various diseases. Since elaidate is a C18 unsaturated fatty acid with a steric structure similar to that of a C18 saturated fatty acid (stearate), we previously revealed that insulin-dependent glucose uptake was impaired in adipocytes exposed to elaidate prior to and during differentiation similar to stearate. However, it is still unknown whether the mechanism of impairment of insulin-dependent glucose uptake due to elaidate is similar to that of stearate. Here, we indicate that persistent exposure to elaidate has particular effects on insulin signaling and GLUT4 dynamics. Insulin-induced accumulation of Akt at the plasma membrane (PM) and elevations of phosphorylated Akt and AS160 levels in whole cells were suppressed in adipocytes persistently exposed to 50 μM elaidate. Interestingly, persistent exposure to the same concentration of stearate has no effect on the phosphorylated Akt and AS160 levels. When cells were exposed to these fatty acids, elaidate suppressed insulin-induced fusion, but not translocation, of GLUT4 storage vesicles in the PM, whereas stearate did not suppress the fusion and translocation of GLUT4 storage, indicating that elaidate has suppressive effects on the accumulation of Akt and fusion of GLUT4 storage vesicles and that both elaidate and stearate vary in the mechanisms by which they impair insulin-dependent glucose uptake. Copyright © 2020 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.

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