1. Elaidate, a trans fatty acid, suppresses insulin signaling for glucose uptake in a manner distinct from that of stearate.
- Author
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Ishibashi K, Takeda Y, Nakata L, Hakuno F, Takahashi SI, and Atsumi GI
- Subjects
- 3T3-L1 Cells, Adipocytes drug effects, Adipocytes metabolism, Adipocytes ultrastructure, Animals, Carbohydrate Metabolism drug effects, Cell Membrane metabolism, Glucose Transporter Type 4 metabolism, Mice, Oleic Acids chemistry, Phosphorylation drug effects, Protein Transport drug effects, Proto-Oncogene Proteins c-akt metabolism, Stearates chemistry, Transport Vesicles drug effects, Glucose metabolism, Insulin metabolism, Oleic Acids pharmacology, Signal Transduction drug effects, Stearates pharmacology
- 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., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)
- Published
- 2020
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