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Vol. 57, Issue 2, 353-358, February 2000

Differential Regulation of Prostaglandin F2alpha Receptor Isoforms by Protein Kinase C

Hiromichi Fujino, Dinesh Srinivasan, Kristen L. Pierce, and John W. Regan

Department of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, Arizona (H.F., D.S., J.W.R.); and Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina (K.L.P.).

Prostaglandin F2alpha receptors (FP) are G protein-coupled receptors that bind prostaglandin F2alpha (PGF2alpha ), resulting in the activation of an inositol phosphate (IP) second messenger pathway. Alternative mRNA splicing generates two FP receptor isoforms. These isoforms, designated FPA and FPB, are otherwise identical except for their carboxyl termini. FPB is essentially a truncated version of FPA that lacks the 46 carboxyl-terminal amino acids, including four putative protein kinase C (PKC) phosphorylation sites. Until now, functional differences between these FP receptor isoforms have not been identified. We now report that pretreatment with the PKC inhibitor bisindolylmaleimide I enhanced PGF2alpha -stimulated IP accumulation in transfected cells stably expressing the FPA isoform but not in cells stably expressing the FPB isoform. Whole-cell phosphorylation experiments showed a strong agonist-dependent phosphorylation of the FPA isoform but little or no phosphorylation of the FPB. Pretreatment of cells with bisindolylmaleimide I decreased PGF2alpha -stimulated phosphorylation of the FPA isoform consistent with a PKC-dependent phosphorylation. In vitro phosphorylation of an FPA carboxyl-terminal fusion protein by recombinant PKCalpha showed that the carboxyl terminus of the FPA is a substrate for PKC. These results suggest that PKC-dependent phosphorylation is responsible for differential regulation of second messenger signaling by FP prostanoid receptor isoforms.

Copyright © 2000 by The American Society for Pharmacology and Experimental Therapeutics


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