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Am J Physiol Endocrinol Metab 276: E503-E511, 1999;
0193-1849/99 $5.00
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Vol. 276, Issue 3, E503-E511, March 1999

Contribution of protein kinase C to ET-1-induced proliferation in human myometrial cells

C. Tertrin-Clary, I. Eude, T. Fournier, B. Paris, M. Breuiller-Fouché, and F. Ferré

Institut National de la Santé et de la Recherche Médicale Unité 361, Université René Descartes, 75014 Paris, France

The role of protein kinase C (PKC) in endothelin-1 (ET-1)-induced proliferation of human myometrial cells was investigated. ET-1 dose dependently stimulated DNA synthesis and the number of cultured myometrial cells. Inhibition of PKC by calphostin C or Ro-31-8220 or downregulation of PKC eliminated the proliferative effects of ET-1. The failure of two protein tyrosine kinase (PTK) inhibitors (tyrphostin 51 and tyrphostin 23) to affect ET-1-induced proliferation supports the hypothesis of noninvolvement of the tyrosine kinase signaling pathway in this process. The expression and distribution of PKC isoforms were examined by Western blot analysis. The five PKC isoforms (PKC-alpha , -beta 1, -beta 2, -zeta , -epsilon ) evidenced in human myometrial tissue were found to be differentially expressed in myometrial cells, with a predominant expression of PKC-alpha and PKC-zeta . Treatment with phorbol 12,13-dibutyrate (PDBu) resulted in the translocation of all five isoforms to the particulate fraction, whereas ET-1 induced a selective increase in particulate PKC-beta 1, PKC-beta 2, and PKC-epsilon . Our findings that multiple PKC isoforms are differentially responsive to ET-1 or PDBu suggest that they play distinct roles in the myometrial growth process.

endothelin; myometrium


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