6-keto-prostaglandin E1-sensitive adenylate cyclase and binding sites in membranes from platelets and cultured smooth muscle cells

D. Oliva, F. Bernini, A. Corsini, S. Nicosia

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

6-keto-PGE1 elicits the same biological effects as PGI2 in human platelets and in rabbit aorta and mesenteric artery, being, however, less potent. We report here that 6-keto-PGE1 dose-dependently stimulates adenylate cyclase activity in membranes of human platelets and cultured myocytes from rabbit aorta and mesenteric artery. The extent of stimulation of the enzyme by 6-keto-PGE1 is the same as elicited by PGI2 while the apparent affinity is lower than that of prostacyclin, both in platelets and in vascular smooth muscle cells. At the level of platelet membranes, 6-keto-PGE1 interacts with the binding sites labelled by PGI2. However, in platelets as well as in mesenteric artery myocytes, 6-keto-PGE1 interacts with only one class of sites as demonstrated either by binding or by adenylate cyclase studies, whereas PGI2 in the same conditions recognizes two different classes.

Original languageEnglish
Pages (from-to)3755-3758
Number of pages4
JournalBiochemical Pharmacology
Volume33
Issue number23
DOIs
Publication statusPublished - Dec 1 1984

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Epoprostenol
Platelets
Adenylyl Cyclases
Smooth Muscle Myocytes
Muscle
Blood Platelets
Binding Sites
Cells
Mesenteric Arteries
Membranes
Muscle Cells
Aorta
Rabbits
Vascular Smooth Muscle
6-ketoprostaglandin E1
Enzymes

ASJC Scopus subject areas

  • Pharmacology

Cite this

6-keto-prostaglandin E1-sensitive adenylate cyclase and binding sites in membranes from platelets and cultured smooth muscle cells. / Oliva, D.; Bernini, F.; Corsini, A.; Nicosia, S.

In: Biochemical Pharmacology, Vol. 33, No. 23, 01.12.1984, p. 3755-3758.

Research output: Contribution to journalArticle

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