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Endocrinology Vol. 138, No. 8 3103-3111
Copyright © 1997 by The Endocrine Society

ARTICLES

Role of Mitogen-Activated Protein Kinase Pathway in Prostaglandin F2{alpha}-Induced Rat Puerperal Uterine Contraction

Masahide Ohmichi, Koji Koike, Akiko Kimura, Kanji Masuhara, Hiromasa Ikegami, Yoshihide Ikebuchi, Tohru Kanzaki, Kazushige Touhara, Motoyoshi Sakaue, Yuzuru Kobayashi, Masuo Akabane, Akira Miyake and Yuji Murata

Department of Obstetrics and Gynecology, Osaka University Medical School (M.O., K.K., A.K., K.M., H.I., T.K., A.M., Y.M.), 2–2, Yamadaoka, Suita-shi, Osaka 565; Department of Biochemistry, Institute for Brain Research, Faculty of Medicine, The University of Tokyo (K.T.), 7–3-1 Hongo, Bunkyo-ku, Tokyo 113; Second Department of Internal Medicine, Kobe University School of Medicine (M.S.),Chuo-ku, Kobe 650; and Kissei Pharmaceutical Company Limited (Y.K., M.A.), 43665–1, Kashiwabara, Hotaka, Minamiazumi, Nagano 399–83, Japan

Address all correspondence and requests for reprints to: Masahide Ohmichi, Osaka University Medical School, 2–2 Yamadaoka, Suita, Osaka 565, Japan.

In this study, prostaglandin (PG) F2{alpha} was found to activate mitogen-activated protein (MAP) kinase and MAP kinase kinase (MEK) in cultured rat puerperal uterine myometrial cells. PGF2{alpha} stimulation also led to an increase in phosphorylation of raf-1, son of sevenless (SOS), and Shc. Furthermore, we examined the mechanism by which PGF2{alpha} induced MAP kinase phosphorylation. Both pertussis toxin (10 ng/ml), which inactivates Gi/Go proteins, and expression of a peptide derived from the carboxyl terminus of the ß-adrenergic receptor kinase 1 (ßARK1), which specifically blocks signaling mediated by the ß{gamma} subunits of G proteins, blocked the PGF2{alpha}-induced activation of MAP kinase. Ritodrine (1 µM), which is known to relax uterine muscle contraction, attenuated PGF2{alpha}-induced tyrosine phosphorylation of MAP kinase. Moreover, to examine the role of MAP kinase pathway in uterine contraction, an inhibitor of MEK activity, PD098059, was used. Although MEK inhibitor had no effect on PGF2{alpha}-induced calcium mobilization, this inhibitor partially inhibited PGF2{alpha}-induced uterine contraction. These results provide evidence that PGF2{alpha} stimulates the MAP kinase signaling pathway in cultured rat puerperal uterine myometrial cells through Gß{gamma} protein, suggesting that this new pathway may play an important role in the biological action of PGF2{alpha} on these cells.




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