PT - JOURNAL ARTICLE AU - Ponnal Nambi AU - Hsiao-Ling Wu AU - Diana Ye AU - Alison Gagnon AU - Nabil Elshourbagy TI - Characterization of a Novel Porcine Endothelin<sub>B</sub>Receptor Splice Variant DP - 2000 Jan 01 TA - Journal of Pharmacology and Experimental Therapeutics PG - 247--253 VI - 292 IP - 1 4099 - http://jpet.aspetjournals.org/content/292/1/247.short 4100 - http://jpet.aspetjournals.org/content/292/1/247.full SO - J Pharmacol Exp Ther2000 Jan 01; 292 AB - 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 ETBreceptor, 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 ETBreceptors. The American Society for Pharmacology and Experimental Therapeutics