Retinoic acid leads to cytoskeletal rearrangement through AMPK-Rac1 and stimulates glucose uptake through AMPK-p38 MAPK in skeletal muscle cells

Mi Lee Yun, Ok Lee Jung, Jin Hee Jung, Hae Kim Ji, Sun-Hwa Park, Man Park Ji, Eung Kyun Kim, Pann Ghill Suh, Hyeon Soo Kim

Research output: Contribution to journalArticle

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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 α1 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.

Original languageEnglish
Pages (from-to)33969-33974
Number of pages6
JournalJournal of Biological Chemistry
Volume283
Issue number49
DOIs
Publication statusPublished - 2008 Dec 5

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AMP-Activated Protein Kinases
p38 Mitogen-Activated Protein Kinases
Tretinoin
Muscle Cells
Muscle
Skeletal Muscle
Cells
Glucose
p21-Activated Kinases
Actin Depolymerizing Factors
Phosphorylation
eIF-2 Kinase
Myoblasts
Guanosine Triphosphate
Vitamin A
Metabolism
Polymerization
Protein Kinase C
Small Interfering RNA
Actins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Retinoic acid leads to cytoskeletal rearrangement through AMPK-Rac1 and stimulates glucose uptake through AMPK-p38 MAPK in skeletal muscle cells. / Yun, Mi Lee; Jung, Ok Lee; Jung, Jin Hee; Ji, Hae Kim; Park, Sun-Hwa; Ji, Man Park; Kim, Eung Kyun; Suh, Pann Ghill; Kim, Hyeon Soo.

In: Journal of Biological Chemistry, Vol. 283, No. 49, 05.12.2008, p. 33969-33974.

Research output: Contribution to journalArticle

Yun, Mi Lee ; Jung, Ok Lee ; Jung, Jin Hee ; Ji, Hae Kim ; Park, Sun-Hwa ; Ji, Man Park ; Kim, Eung Kyun ; Suh, Pann Ghill ; Kim, Hyeon Soo. / Retinoic acid leads to cytoskeletal rearrangement through AMPK-Rac1 and stimulates glucose uptake through AMPK-p38 MAPK in skeletal muscle cells. In: Journal of Biological Chemistry. 2008 ; Vol. 283, No. 49. pp. 33969-33974.
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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 α1 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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AU - Kim, Eung Kyun

AU - Suh, Pann Ghill

AU - Kim, Hyeon Soo

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