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      Signaling of rat Frizzled-2 through phosphodiesterase and cyclic GMP.

      Science (New York, N.Y.)

      Amino Acid Sequence, Animals, CHO Cells, Calcium, metabolism, Cricetinae, Culture Media, Conditioned, Cyclic GMP, Embryo, Nonmammalian, Frizzled Receptors, Guanosine 5'-O-(3-Thiotriphosphate), pharmacology, Molecular Sequence Data, Pertussis Toxin, Phosphodiesterase Inhibitors, Phosphoric Diester Hydrolases, Rats, Receptors, Adrenergic, beta-2, chemistry, Receptors, G-Protein-Coupled, Receptors, Neurotransmitter, Recombinant Fusion Proteins, Reverse Transcriptase Polymerase Chain Reaction, Signal Transduction, Transducin, genetics, Transfection, Tumor Cells, Cultured, Zebrafish

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          Abstract

          The Frizzled-2 receptor (Rfz2) from rat binds Wnt proteins and can signal by activating calcium release from intracellular stores. We show that wild-type Rfz2 and a chimeric receptor consisting of the extracellular and transmembrane portions of the beta2-adrenergic receptor with cytoplasmic domains of Rfz2 also signaled through modulation of cyclic guanosine 3',5'-monophosphate (cGMP). Activation of either receptor led to a decline in the intracellular concentration of cGMP, a process that was inhibited in cells treated with pertussis toxin, reduced by suppression of the expression of the heterotrimeric GTP-binding protein (G protein) transducin, and suppressed through inhibition of cGMP-specific phosphodiesterase (PDE) activity. Moreover, PDE inhibitors blocked Rfz2-induced calcium transients in zebrafish embryos. Thus, Frizzled-2 appears to couple to PDEs and calcium transients through G proteins.

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          Journal
          12471263
          10.1126/science.1073776

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