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Retinoic Acid Leads to Cytoskeletal Rearrangement through AMPK-Rac1 and Stimulates Glucose Uptake through AMPK-p38 MAPK in Skeletal Muscle Cells

Authors
Lee, Yun MiLee, Jung OkJung, Jin-HeeKim, Ji HaePark, Sun-HwaPark, Ji ManKim, Eung-KyunSuh, Pann-GhillKim, Hyeon Soo
Issue Date
5-12월-2008
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.283, no.49, pp.33969 - 33974
Indexed
SCIE
SCOPUS
Journal Title
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume
283
Number
49
Start Page
33969
End Page
33974
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/122239
DOI
10.1074/jbc.M804469200
ISSN
0021-9258
Abstract
Retinoic acid (RA) is one of the major components of vitamin A. In the present study, we found that retinoic acid activated AMP-activated protein kinase (AMPK). RA induced Rac1-GTP formation and phosphorylation of its downstream target, p21-activated kinase (PAK), whereas the inhibition of AMPK blocked RA-induced Rac1 activation. Moreover, cofilin, an actin polymerization regulator, was activated when incubated with RA. We then showed that inhibition of AMPK by compound C, a selective inhibitor of AMPK, or small interfering RNA of AMPK alpha 1 blocked RA-induced cofilin phosphorylation. Additionally, we found that retinoic acid-stimulated glucose uptake in differentiated C2C12 myoblast cells and activated p38 mitogen-activated protein kinase (MAPK). Finally, the inhibition of AMPK and p38 MAPK blocked retinoic acid-induced glucose uptake. In summary, our results suggest that retinoic acid may have cytoskeletal roles in skeletal muscle cells via stimulation of the AMPK-Rac1-PAK-cofillin pathway and may also have beneficial roles in glucose metabolism via stimulation of the AMPK-p38 MAPK pathway.
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