Specific binding of estradiol to rat coronary artery smooth muscle cells

J Steroid Biochem Mol Biol. 1996 Apr;58(1):83-8. doi: 10.1016/0960-0760(96)00005-2.


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 17 beta-estradiol, with a Kd 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] 17 beta-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.

MeSH terms

  • Animals
  • Binding Sites
  • Binding, Competitive
  • Breast Neoplasms / metabolism
  • Coronary Vessels / cytology
  • Coronary Vessels / metabolism*
  • Dexamethasone / metabolism
  • Estradiol / metabolism*
  • Humans
  • Kinetics
  • Ligands
  • Muscle, Smooth, Vascular / cytology
  • Muscle, Smooth, Vascular / metabolism*
  • Progesterone / metabolism
  • RNA, Messenger / analysis
  • Rats
  • Receptors, Estrogen / genetics
  • Receptors, Estrogen / metabolism*
  • Testosterone / metabolism
  • Tumor Cells, Cultured


  • Ligands
  • RNA, Messenger
  • Receptors, Estrogen
  • Testosterone
  • Progesterone
  • Estradiol
  • Dexamethasone