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This Article Full Text Full Text (PDF) All Versions of this Article: 285/3/C599    most recent 00040.2003v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (4) Citing Articles via Google Scholar Google Scholar Articles by Liberto, G. D. Articles by Breuiller-Fouché, M. Search for Related Content PubMed PubMed Citation Articles by Liberto, G. D. Articles by Breuiller-Fouché, M.

MUSCLE CELL BIOLOGY AND CELL MOTILITY

A critical role for PKC in endothelin-1-induced uterine contractions at the end of pregnancy

¹Institut National de la Santé et de la Recherche Médicale (INSERM) U361, Université René Descartes, Pavillon Baudelocque, and ²Maternité Port-Royal, Hôpital Cochin, 75014 Paris, France

Submitted 28 January 2003 ; accepted in final form 30 April 2003

We have previously shown that protein kinase C (PKC) and/or PKC are necessary for endothelin-1 (ET-1)-induced human myometrial contraction at the end of pregnancy (Eude I, Paris P, Cabrol D, Ferré F, and Breuiller-Fouché M. Biol Reprod 63: 1567–1573, 2000). Here, we report that the selective inhibitor of PKC isoform, Rottlerin, does not prevent ET-1-induced contractions, whereas LY-294002, a phosphatidylinositol (PI) 3-kinase inhibitor, affects the contractile response. This study characterized the in vitro contractile response of cultured human pregnant myometrial cells to ET-1 known to induce in vitro contractions of intact uterine smooth muscle strips. Cultured myometrial cells incorporated into collagen lattices have the capacity to reduce the size of these lattices, referred to as lattice contraction. Neither the selective conventional PKC isoform inhibitor, Gö-6976, or rottlerin affected myometrial cell-mediated gel contraction by ET-1, whereas this effect was blocked by LY-294002. We found that treatment of myometrial cell lattices with an inhibitory peptide specific for PKC or with an antisense against PKC resulted in a significant loss of ET-1-induced contraction. Evidence is also presented by using confocal microscopy that ET-1 induced translocation of PKC to a structure coincident with the actin-rich microfilaments of the cytoskeleton. We have shown that PKC has a role in the actin organization in ET-1-stimulated cells. Accordingly, our results suggest that PKC plays a role in myometrial contraction in pregnant women.

protein kinase C; uterine smooth muscle; parturition

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