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Volume 272, Number 2, Issue of January 10, 1997 pp. 883-887
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Cloning of a Carboxyl-terminal Isoform of the Prostanoid FP Receptor

(Received for publication, August 20, 1996, and in revised form, October 29, 1996)

Kristen L. Pierce Dagger , Thomas J. Bailey Dagger , Patricia B. Hoyer , Daniel W. Gil par , David F. Woodward par and John W. Regan Dagger

From the Dagger  Departments of Pharmacology and Toxicology and  Physiology, The University of Arizona, Tucson, Arizona 85721 and par  Allergan, Inc., Department of Biological Sciences, Irvine, California 92713-9534

An FP prostanoid receptor isoform, which appears to arise from alternative mRNA splicing, has been cloned from a mid-cycle ovine large cell corpus luteum library. The isoform, named the FPB receptor, is identical to the original isoform, the FPA, throughout the seven transmembrane domains, but diverges nine amino acids into the carboxyl terminus. In contrast to FPA, whose carboxyl terminus continues for another 46 amino acids beyond the nine shared residues, the FPB terminates after only one amino acid. The FPA isoform appears to arise by the failure to utilize a potential splice site, while a 3.2-kilobase pair intron is spliced out from the FP gene to generate the FPB isoform mRNA. The two isoforms have indistinguishable radioligand binding properties, but seem to differ in functional coupling to phosphatidylinositol hydrolysis. Thus, in COS-7 cells transiently transfected with either the FPA or the FPB receptor cDNAs, prostaglandin F2alpha stimulates inositol phosphate accumulation to the same absolute maximum, but the basal level of inositol phosphate accumulation is approximately 1.3-fold higher in cells transfected with the FPB as compared with cells transfected with the FPA isoform. Using the polymerase chain reaction, mRNA encoding the FPB isoform was identified in the ovine corpus luteum.


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