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Vol. 281, Issue 1, 15-23, 1997

Activation of Phospholipase D by Endothelin-1 in Rat Myometrium. Role of Calcium and Protein Kinase C1

Sandrine Naze2, Hervé Le Stunff2, Lien Dokhac, Gisèle Thomas and Simone Harbon

Endocrinologie et Régulations Cellulaires, CNRS URA 1131, Bât 432, Université Paris Sud, 91405 ORSAY Cedex, France

In rat myometrium labeled with [3H]myristic acid, endothelin (ET)-1 via ETA receptors stimulated, in the presence of 0.3% butanol, the formation of [3H]phosphatidylbutanol ([3H]PBut) as a result of phospholipase D activity. Fluoroaluminates increased [3H]PBut generation, which indicated that a heterotrimeric G protein was involved. The ET-1 effect was insensitive to pertussis toxin and was rapidly desensitized. The calcium ionophore ionomycin as well as 4beta -phorbol 12-myristate-13-acetate and 4beta -phorbol 12,13-dibutyrate also stimulated [3H]PBut production. Protein kinase C (PKC) inhibition, particularly with Ro-31-8220, and down-regulation of PKC by 4beta -phorbol 12-myristate-13-acetate, abrogated 4beta -phorbol 12,13-dibutyrate responses but partially reduced (50%) ET-1 and ionomycin stimulatory effects. [3H]PBut production induced by ionomycin depended on Ca++ influx, whereas that induced by 4beta -phorbol 12,13-dibutyrate did not. Decrease of extracellular Ca++ partially reduced (60%) ET-1 stimulation that was additionally attenuated (75%) by chelerythrine, a PKC inhibitor. The data indicate that in myometrium, phospholipase D was activated by PKC and Ca++, which both contribute at least partially to ET-1-mediated phospholipase D activation.

Copyright © by The American Society for Pharmacology and Experimental Therapeutics


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