Regulation of a common, low-affinity binding site for primary prostanoids on bovine aortic endothelial cells

Gilad Rimon, Mazal Rubin

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Bovine aortic endothelial cells contain a prostaglandin site which binds with similar low-affinity PGE2, PGF2α and the thromboxane agonist U- 46619. Treatment of the cells with agents that increase the level of cellular cAMP such as forskolin, a direct activator of adenylate cyclase or IBMX, a phosphodiesterase inhibitor, decreased the binding of PGE2 to the cells. Addition of dibutyryl cAMP to intact cells caused a quick reduction in PGE2 binding with a half time of less than 2 min. The reduction in PGE2 binding was completely reversible after removing the dibutyryl cAMP. The reduction in PGE2 binding after addition of dibutyryl cAMP to the intact cells was also observed after a mechanical disruption of the cells or after permeabilization with digitonin. Incubation of the cells with myristoylated PKI(14-22) amide, a specific protein kinase A inhibitor, resulted in partial suppression of the reduction of PGE2 binding by dibutyryl cAMP. Pretreatment of intact cells for 24 h with 10-6 M PGE2 or a PKC activator did not reduce the specific binding of [3H]-PGE2. These results suggest that PKA, but not PKC, is involved in a fast reversible regulation of the common prostanoid receptor on bovine endothelial cells.

Original languageEnglish
Pages (from-to)289-296
Number of pages8
JournalBiochimica et Biophysica Acta - General Subjects
Issue number2
StatePublished - 10 Apr 1998


  • Common binding site
  • Desensitization
  • Dibutyryl cAMP
  • Endothelial cell
  • Prostanoid receptor
  • Protein kinase A

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Regulation of a common, low-affinity binding site for primary prostanoids on bovine aortic endothelial cells'. Together they form a unique fingerprint.

Cite this