| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
ARTICLES |
Unit on Cell Biology, Laboratory of Genetics, National Institute of Mental Health, National Institutes of Health (S.R.J.H., T.B.U.), Bethesda, Maryland 20892; and Endocrine Unit, Massachusetts General Hospital and Harvard Medical School (D.A.R., H.J.), Boston, Massachusetts 02114
Address all correspondence and requests for reprints to: Dr. Ted B. Usdin, Unit on Cell Biology, Laboratory of Genetics, National Institute of Mental Health, National Institutes of Health, Building 36, Room 3D06, 36 Convent Drive, MSC4094, Bethesda, Maryland 20892-4094. E-mail: usdin{at}codon.nih.gov
Homologs of mammalian PTH1 and PTH2 receptors, and a novel PTH3 receptor have been identified in zebrafish (zPTH1, zPTH2, and zPTH3). zPTH1 receptor ligand specificity is similar to that of mammalian PTH1 receptors. The zPTH2 receptor is selective for PTH over PTH-related protein (PTHrP); however, PTH produces only modest cAMP accumulation. A PTH2 receptor-selective peptide, tuberoinfundibular peptide of 39 residues (TIP39), has recently been purified from bovine hypothalamus. The effect of TIP39 has not previously been examined on zebrafish receptors. The zPTH3 receptor was initially described as PTHrP selective based on comparison with the effects of human PTH. We have now examined the ligand specificity of the zebrafish PTH-recognizing receptors expressed in COS-7 cells using a wide range of ligands. TIP39 is a potent agonist for stimulation of cAMP accumulation at two putative splice variants of the zPTH2 receptor (EC50, 2.6 and 5.2 nM); in comparison, PTH is a partial agonist [maximal effect (Emax) of PTH peptides ranges from 28–49% of the TIP39 Emax]. As TIP39 is much more efficacious than any known PTH-like peptide, a homolog of TIP39 may be the zPTH2 receptor’s endogenous ligand. At the zPTH3 receptor, rat PTH-(1–34) and rat PTH-(1–84) (EC50, 0.22 and 0.45 nM) are more potent than PTHrP (EC50, 1.5 nM), and rPTH-(1–34) binds with high affinity (3.2 nM). PTH has not been isolated from fish. PTHrP-like peptides, which have been identified in fish, may be the natural ligands for zPTH1 and zPTH3 receptors.
This article has been cited by other articles:
 |
|
 |
|
  P. M. Guerreiro, J. L. Renfro, D. M. Power, and A. V. M. Canario The parathyroid hormone family of peptides: structure, tissue distribution, regulation, and potential functional roles in calcium and phosphate balance in fish Am J Physiol Regulatory Integrative Comp Physiol, February 1, 2007; 292(2): R679 - R696. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Fleming, M. Sato, and P. Goldsmith High-Throughput In Vivo Screening for Bone Anabolic Compounds with Zebrafish J Biomol Screen, December 1, 2005; 10(8): 823 - 831. [Abstract] [PDF]
|
|
|
|
 |
|
 T. M. Murray, L. G. Rao, P. Divieti, and F. R. Bringhurst Parathyroid Hormone Secretion and Action: Evidence for Discrete Receptors for the Carboxyl-Terminal Region and Related Biological Actions of Carboxyl- Terminal Ligands Endocr. Rev., February 1, 2005; 26(1): 78 - 113. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. R. Papasani, R. C. Gensure, Y.-L. Yan, Y. Gunes, J. H. Postlethwait, B. Ponugoti, M. R. John, H. Juppner, and D. A. Rubin Identification and Characterization of the Zebrafish and Fugu Genes Encoding Tuberoinfundibular Peptide 39 Endocrinology, November 1, 2004; 145(11): 5294 - 5304. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. C. Gensure, B. Ponugoti, Y. Gunes, M. R. Papasani, B. Lanske, M. Bastepe, D. A. Rubin, and H. Juppner Identification and Characterization of Two Parathyroid Hormone-Like Molecules in Zebrafish Endocrinology, April 1, 2004; 145(4): 1634 - 1639. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. G. Goodman, I. B. Salusky, and H. Juppner New lessons from old assays: parathyroid hormone (PTH), its receptors, and the potential biological relevance of PTH fragments Nephrol. Dial. Transplant., October 1, 2002; 17(10): 1731 - 1736. [Full Text] [PDF]
|
|
|
|
|
|
M. R. John, M. Arai, D. A. Rubin, K. B. Jonsson, and H. Juppner Identification and Characterization of the Murine and Human Gene Encoding the Tuberoinfundibular Peptide of 39 Residues Endocrinology, March 1, 2002; 143(3): 1047 - 1057. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Dobolyi, H. Ueda, H. Uchida, M. Palkovits, and T. B. Usdin Anatomical and physiological evidence for involvement of tuberoinfundibular peptide of 39 residues in nociception PNAS, January 24, 2002; (2002) 42416199. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. P. Goold, T. B. Usdin, and S. R. J. Hoare Regions in Rat and Human Parathyroid Hormone (PTH) 2 Receptors Controlling Receptor Interaction with PTH and with Antagonist Ligands J. Pharmacol. Exp. Ther., November 1, 2001; 299(2): 678 - 690. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. L. Ward, C. J. Small, K. G. Murphy, A. R. Kennedy, M. A. Ghatei, and S. R. Bloom The Actions of Tuberoinfundibular Peptide on the Hypothalamo-Pituitary Axes Endocrinology, August 1, 2001; 142(8): 3451 - 3456. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. B. Jonsson, M. R. John, R. C. Gensure, T. J. Gardella, and H. Juppner Tuberoinfundibular Peptide 39 Binds to the Parathyroid Hormone (PTH)/PTH-Related Peptide Receptor, but Functions as an Antagonist Endocrinology, February 1, 2001; 142(2): 704 - 709. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Dobolyi, H. Ueda, H. Uchida, M. Palkovits, and T. B. Usdin Anatomical and physiological evidence for involvement of tuberoinfundibular peptide of 39 residues in nociception PNAS, February 5, 2002; 99(3): 1651 - 1656. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Endocrinology | Endocrine Reviews | J. Clin. End. & Metab. |
| Molecular Endocrinology | Recent Prog. Horm. Res. | All Endocrine Journals |
