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Originally published In Press as doi:10.1074/jbc.M008010200 on January 12, 2001

J. Biol. Chem., Vol. 276, Issue 14, 10853-10860, April 6, 2001
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The Regulation of Uncoupling Protein-2 Gene Expression by omega -6 Polyunsaturated Fatty Acids in Human Skeletal Muscle Cells Involves Multiple Pathways, Including the Nuclear Receptor Peroxisome Proliferator-activated Receptor beta *

Emmanuel ChevillotteDagger , Jennifer Rieusset, Marina Roques, Michel Desage§, and Hubert Vidal

From the INSERM U449, Faculté de Médecine René Laennec, Université Claude Bernard Lyon-1, and § CRNHL Faculté de Médecine René Laennec, Université Claude Bernard Lyon-1, 69372 Lyon, France

Fatty acids have been postulated to regulate uncoupling protein (UCP) gene expression in skeletal muscle in vivo. We have identified, at least in part, the mechanism by which polyunsaturated fatty acids increase UCP-2 expression in primary culture of human muscle cells. omega -6 fatty acids and arachidonic acid induced a 3-fold rise in UCP-2 mRNA levels possibly through transcriptional activation. This effect was prevented by indomethacin and mimicked by prostaglandin (PG) E2 and carbaprostacyclin PGI2, consistent with a cyclooxygenase-mediated process. Incubation of myotubes for 6 h with 100 µM arachidonic acid resulted in a 150-fold increase in PGE2 and a 15-fold increase in PGI2 in the culture medium. Consistent with a role of cAMP and protein kinase A, both prostaglandins induced a marked accumulation of cAMP in human myotubes, and forskolin reproduced the effect of arachidonic acid on UCP-2 mRNA expression. Inhibition of protein kinase A with H-89 suppressed the effect of PGE2, whereas cPGI2 and arachidonic acid were still able to increase ucp-2 gene expression, suggesting additional mechanisms. We found, however, that the MAP kinase pathway was not involved. Prostaglandins, particularly PGI2, are potent activators of the peroxisome proliferator-activated receptors. A specific agonist of peroxisome proliferator-activated receptor (PPAR) beta  (L165041) increased UCP-2 mRNA levels in myotubes, whereas activation of PPARalpha or PPARgamma was ineffective. These results suggest thus that ucp-2 gene expression is regulated by omega -6 fatty acids in human muscle cells through mechanisms involving at least protein kinase A and the nuclear receptor PPARbeta .

* This work was supported in part by grants from ALFEDIAM-Novo Nordisc, from Institut de Recherche Servier, and from INSERM Progres 4P020D.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of a Ph.D. grant from the French Ministère de la Recherche et de l'Enseignement Supérieur. To whom correspondence should be addressed: INSERM U449, Faculté de Médecine René Laennec, Rue G. Paradin, F-69372 Lyon Cedex 08, France. Tel.: 33 478 77 86 29; Fax: 33 478 77 87 62; E-mail: vidal@laennec.univ-lyon1.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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