Characterization of a rat kidney thromboxane A2 receptor: High affinity for the agonist ligand I-BOP

Drew D. D'Angelo, Takayuki Terasawa, Steven J. Carlisle, Gerald W. Dorn, Kevin R. Lynch

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

We have cloned a rat kidney thromboxane A2 receptor (TP) cDNA. This receptor was shown to be functional in that the thromboxane A2 mimetics, U46619 and I-BOP, elicited calcium transients in Xenopus oocytes and HEK293 cells expressing the TP receptor, respectively. Comparison of the affinities of the rat and human TP sites for the agonist radioligand [125I]BOP showed that the rat TP site has about a ten-fold higher affinity for this drug (K(D) = 0.5 vs. 4.4 nM) while the affinities of the two sites for other compounds (U46619, I-PTH-OH) were the same. Our results are significant in that they identify a cloned TP as having a picomolar affinity for [125I]BOP.

Original languageEnglish
Pages (from-to)303-316
Number of pages14
JournalProstaglandins
Volume52
Issue number4
DOIs
StatePublished - Oct 1 1996
Externally publishedYes

Keywords

  • HEK293 cells
  • I-BOP
  • molecular cloning
  • oocyte expression (Xenopus laevis)
  • radioligand binding
  • thromboxane A receptor

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