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J. Biol. Chem., Vol. 275, Issue 51, 40539-40546, December 22, 2000
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From the Unité 486 INSERM, Transduction Hormonale et
Régulation Cellulaire, Faculté de Pharmacie,
92296 Châtenay-Malabry, France
p38 mitogen-activated protein
kinases (p38-MAPKs) are activated by cytokines, cellular stresses,
growth factors, and hormones. We show here that p38-MAPKs are activated
upon stimulation by thyroid-stimulating hormone (TSH) or cAMP. TSH
caused the phosphorylation of p38-MAPK in Chinese hamster ovary
cells stably transfected with the human TSH receptor but not in
wild-type Chinese hamster ovary cells. The effect of TSH was fully
mimicked by the adenylyl cyclase activator, forskolin, and by a
permeant analog of cAMP. The effect of forskolin was reproduced in
FRTL5 rat thyroid cells. TSH also stimulated the phosphorylation of
MAPK kinase 3 or 6, over the same time scale as that of p38-MAPKs. TSH
and forskolin stimulated the activity of the
Thyroid-stimulating Hormone and Cyclic AMP Activate p38
Mitogen-activated Protein Kinase Cascade
INVOLVEMENT OF PROTEIN KINASE A, Rac1, AND REACTIVE OXYGEN
SPECIES*
,
-isoform of p38-MAPK
assayed by phosphorylation of the transcription factor ATF2. The
activity of MAPK-activated protein kinase-2 was stimulated by TSH and
forskolin. This stimulation was abolished by SB203580, a specific
inhibitor of p38-MAPKs. The protein kinase A inhibitor H89 inhibited
the stimulation of phosphorylation of p38-MAPKs by forskolin, whereas inhibitors of protein kinase C, p70S6k, and
phosphatidylinositol 3-kinase were ineffective. Expression of the
dominant negative form of Rac1, but not that of Ras, blocked forskolin-induced p38-MAPK activation. Diphenylene iodonium, a potent inhibitor of NADPH oxidase(s), and ascorbic acid, an effective free radical scavenger, suppressed TSH- or forskolin-stimulated p38-MAPK phosphorylation, indicating that the generation of reactive oxygen species plays a key role in signaling from cAMP to p38-MAPKs. Inhibition of the p38-MAPK pathway with SB203580 partially but significantly, attenuates cAMP- and TSH-induced expression of the
sodium iodide symporter in FRTL-5 cells. These results point to a new
signaling pathway for the Gs-coupled TSH receptor,
involving cAMP, protein kinase A, Rac1, and reactive oxygen species and resulting in the activation of a signaling kinase cascade that includes
MAPK kinase 3 or 6, p38-MAPK, and MAPK-activated protein kinase-2.
*
This work was supported by Grant 7298 from the Association
pour la Recherche contre le Cancer and by a grant from the Ligue Nationale contre le Cancer.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.
To whom correspondence should be addressed: U486 INSERM, Tour D1,
Faculté de Pharmacie, 5 rue Jean-Baptiste Clément, 92296 Châtenay-Malabry Cédex, France. Tel.: 146835867;
Fax: 146835871; E-mail: martine.pomerance@cep.u-psud.fr.
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