Specific binding of estradiol to rat coronary artery smooth muscle cells

Mian Bei, Mark C. Lavigne, Marie L. Foegh, Peter W. Ramwell, Robert Clarke

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

We report the expression and characteristics of the estrogen receptor in rat coronary artery-derived smooth muscle cells. Polymerase chain reaction analyses of total and poly(A)+ mRNA from rat coronary artery-derived smooth muscle cells indicate the presence of estrogen receptor mRNA. Binding analyses reveal the presence of high affinity binding sites for 17β-estradiol, with a K,equivalent to that observed for authentic estrogen receptors in other estrogen responsive tissues. Scatchard and Hill plot analyses of the properties of receptor-ligand binding indicate the presence of a single site, and the absence of cooperative binding. Unlabeled E2 but not testosterone, dexamethasone or progesterone compete with [3H] 17β-estradiol for binding sites. The affinity, specificity and non-cooperative nature of the estrogen binding sites are identical to those observed in other estrogen-responsive tissues. These cells may provide a novel model in which to study the effects of estrogens on the proliferation, differentiation and function of vascular smooth muscle cells.

Original languageEnglish (US)
Pages (from-to)83-88
Number of pages6
JournalJournal of Steroid Biochemistry and Molecular Biology
Volume58
Issue number1
DOIs
StatePublished - Apr 1996
Externally publishedYes

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