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Vol. 292, Issue 1, 247-253, January 2000

Characterization of a Novel Porcine EndothelinB Receptor Splice Variant

Ponnal Nambi1 , Hsiao-Ling Wu, Diana Ye, Alison Gagnon and Nabil Elshourbagy

Departments of Renal Pharmacology (P.N., H.-L.W., D.Y.) and Molecular Biology (A.G., N.E.), SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania

Screening of porcine cerebellum cDNA library with porcine endothelinB (ETB) receptor cDNA revealed a novel ETB receptor cDNA that is distinctly different from the wild-type ETB receptor in length and the amino acid sequence at the C-terminal end. This sequence appears to represent alternate splicing of the carboxy terminal end of ETB receptor, resulting in a polypeptide of 429 amino acids in length, which is 14 amino acids shorter than the wild-type porcine ETB receptor. Characterization of the wild-type and alternately spliced ETB receptors expressed in COS cells revealed that both receptors displayed very similar binding [apparent dissociation constant (Kd) and maximum binding (Bmax) for 125I-ET-1 were 71 pM and 1.6 pmol/mg protein for wild-type and 81 pM and 1.2 pmol/mg protein for splice variant ETB receptors] as well as functional properties. These data suggest that the differences in the amino acids at the C-terminal end had no effect on binding or functional coupling of these alternately spliced ETB receptors.

1 Present address: Cardiovascular Sciences, DuPont Pharmaceuticals Company, Experimental Station, E 400/3237, Wilmington, DE 19880-0400.

0022-3565/0/2921-0247$03.00/0
THE JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
Copyright © 2000 by The American Society for Pharmacology and Experimental Therapeutics


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