5-HT1B and 5-HT2 serotonin binding sites in cultured Wistar-Kyoto rat aortic smooth muscle cells. Academic Article

abstract

• We studied [3H]serotonin [( 3H]5-HT) binding on cultured arterial smooth muscle cells from rat aorta. We found a high and low affinity binding site. Binding to the higher affinity site could be displaced by drugs in an order corresponding most closely with the 5-HT1B subtype, and high affinity [125I]iodo-cyanopindolol binding was also found. We found evidence for a 5-HT2 subtype using [3H]ketanserin binding, with similar results whether specific binding was determined using unlabelled ketanserin, methysergide or mianserin.

authors

• Kent, Thomas

published proceedings

• Eur J Pharmacol

author list (cited authors)

• Jazayeri, A., Meyer, W. J., & Kent, T. A.

citation count

• 11

complete list of authors

• Jazayeri, A||Meyer, WJ||Kent, TA

publication date

• October 1989

publisher

• Elsevier  Publisher

published in

• European Journal of Pharmacology  Journal

keywords

• 8-Hydroxy-2-(di-n-propylamino)tetralin
• Animals
• Aorta, Thoracic
• Cell Membrane
• Cells, Cultured
• Iodine Radioisotopes
• Iodocyanopindolol
• Kinetics
• Muscle, Smooth, Vascular
• Pindolol
• Rats
• Rats, Inbred WKY
• Receptors, Serotonin
• Tetrahydronaphthalenes

PubMed Central ID

• 2532143

Digital Object Identifier (DOI)

• 10.1016/0014-2999(89)90832-7

start page

• 183

end page

• 187

volume

• 169

issue

• 1

URL

• http://dx.doi.org/10.1016/0014-2999(89)90832-7