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Biology of Reproduction 59, 153-159 (1998)
©Copyright 1998 Society for the Study of Reproduction, Inc.

Role of Protein Kinase C in Endothelin-1-Induced Contraction of Human Myometrium1

M. Breuiller-Fouché2,a, C. Tertrin-Clarya, V. Héluya, T. Fourniera, , and F. Ferréa

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

The role of protein kinase C (PKC) in the contraction of human myometrium induced by endothelin-1 was investigated. The PKC inhibitor, calphostin C, reduced the sustained phase of endothelin-1-induced contraction. The expression and subcellular distribution of PKC isoforms were determined in unstimulated myometrium by Western blotting using isoform-specific antisera. At least five PKC isoforms (PKC{alpha}, PKCß1, PKCß2, PKC{zeta}, and trace amounts of PKC{epsilon}) were detected. Quantitative immunoblotting revealed that all these isoforms were diversely distributed between the cytosolic and particulate fractions. After stimulation with phorbol 12,13-dibutyrate (PDB) and endothelin-1, differential redistribution occurred, suggesting a selective role of these isoforms in the physiological function of the myometrium. Biochemical assay confirmed that PDB as well as endothelin-1 evoked a decrease in cytosolic PKC activity. Taken together, these results suggest that PKC may play a role in endothelin-1-induced contraction of human uterine smooth muscle.

1 Supported by Institut National de la Santé et de la Recherche Médicale and by University René-Descartes.

2 Correspondence: M. Breuiller-Fouché, INSERM U. 361, Pavillon Baudelocque, 123, Bd de Port-Royal, 75014 Paris, France. FAX: 00.1.43.26.44.08; u361{at}cochin.inserm.fr




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