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J Biol Chem, Vol. 274, Issue 33, 23035-23042, August 13, 1999

A G Protein-coupled Receptor from Zebrafish Is Activated by Human Parathyroid Hormone and Not by Human or Teleost Parathyroid Hormone-related Peptide
IMPLICATIONS FOR THE EVOLUTIONARY CONSERVATION OF CALCIUM-REGULATING PEPTIDE HORMONES

David A. Rubin, Per Hellman, Leonard I. Zon, Craig J. Lobb^**, Clemens Bergwitz, and Harald Jüppner^§§

From the  Endocrine Unit, ^§§ Pediatric Services, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114,  Howard Hughes Medical Institute and Children's Hospital of Boston, Harvard Medical School, Boston, Massachusetts 02115, and ^** Department of Microbiology, University of Mississippi Medical Center, Jackson, Mississippi 39216

Genomic and cDNA clones encoding portions of a putative catfish parathyroid hormone (PTH) 2 receptor (PTH2R) led to the isolation of a cDNA encoding a full-length zebrafish PTH2R (zPTH2R). The zPTH2R shared 63 and 60% amino acid sequence identity with human and rat PTH2Rs, respectively, 47-52% identity with mammalian and frog PTH/PTHrP receptors (PTH1R), and less than 37% with other members of this family of G protein-coupled receptors. COS-7 cells expressing zPTH2R(43), a 5' splice variant that lacked 17 amino acids in the amino-terminal extracellular domain, showed cAMP accumulation when challenged with [Tyr³⁴]hPTH(1-34)-amide (hPTH) (EC₅₀, 1.64 ± 0.95 nM) and [Ile⁵,Trp²³,Tyr³⁶]hPTHrP-(1-36)-amide ([Ile⁵, Trp²³]hPTHrP) (EC₅₀, 46.8 ± 12.1 nM) but not when stimulated with [Tyr³⁶]hPTHrP-(1-36)-amide (hPTHrP), [Trp²³,Tyr³⁶]hPTHrP-(1-36)-amide ([Trp²³]hPTHrP), or [Ala²⁹,Glu³⁰,Ala³⁴,Glu³⁵,Tyr³⁶]fugufish PTHrP-(1-36)amide (fuguPTHrP). FuguPTHrP also failed to activate the human PTH2R but had similar efficiency and efficacy as hPTH and hPTHrP when tested with cells expressing the human PTH1R. Agonist-dependent activation of zPTH2R was less efficient than that of zPTH2R(43), and both receptor variants showed no cAMP accumulation when stimulated with either secretin, growth hormone-releasing hormone, or calcitonin. The zPTH2R thus has ligand specificity similar to that of the human homolog, which raises the possibility that a PTH-like molecule exists in zebrafish, species which lack parathyroid glands.

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