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*
Rubin D, Hellman P, Zon L, Lobb C, Bergwitz C, Jüppner H. 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*. Journal Of Biological Chemistry 1999, 274: 23035-23042. PMID: 10438471, DOI: 10.1074/jbc.274.33.23035.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiological EvolutionBlotting, SouthernCloning, MolecularDNA ProbesDNA, ComplementaryGTP-Binding ProteinsHumansIctaluridaeMolecular Sequence DataParathyroid HormoneParathyroid Hormone-Related ProteinProteinsRatsReceptor, Parathyroid Hormone, Type 2Receptors, Parathyroid HormoneRNA SplicingSequence Homology, Amino AcidZebrafishConceptsG protein-coupled receptorsAmino acid sequence identityProtein-coupled receptorsCAMP accumulationParathyroid hormoneAmino-terminal extracellular domainGrowth hormone-releasing hormoneCalcium-regulating peptide hormoneCDNA clonesHormone-releasing hormoneSequence identityParathyroid hormone 2 receptorHuman homologPTH/PTHrP receptorFamily of G protein-coupled receptorsHuman parathyroid hormoneAgonist-dependent activationSplice variantsCOS-7COS-7 cellsEncoding portionsExtracellular domainLigand specificityAmino acidsEvolutionary conservation
1998
Identification, functional characterization, and developmental expression of two nonallelic parathyroid hormone (PTH)/PTH-related peptide receptor isoforms in Xenopus laevis (Daudin).
Bergwitz C, Klein P, Kohno H, Forman SA, Lee K, Rubin D, Jüppner H. Identification, functional characterization, and developmental expression of two nonallelic parathyroid hormone (PTH)/PTH-related peptide receptor isoforms in Xenopus laevis (Daudin). Endocrinology 1998, 139: 723-32. PMID: 9449646, DOI: 10.1210/endo.139.2.5733.Peer-Reviewed Original ResearchConceptsReceptor isoformsMammalian COS-7 cellsAfrican clawed frog Xenopus laevisIsoform BXenopus laevisParathyroid hormoneClawed frog Xenopus laevisComplementary DNA librarySubpopulations of mononuclear cellsPTH/PTH-related peptideFrog Xenopus laevisCOS-7 cellsPTH-(1-34Accumulation of cAMPVoltage clamp experimentsNeurula stage embryosMessenger RNA expressionInositol phosphate turnoverRibonuclease protection analysisPTHrP-(1-36DNA libraryTadpole developmentIn situ hybridizationCoding regionIncreased approximately 30-fold
1997
Residues in the Membrane-spanning and Extracellular Loop Regions of the Parathyroid Hormone (PTH)-2 Receptor Determine Signaling Selectivity for PTH and PTH-related Peptide*
Bergwitz C, Jusseaume S, Luck M, Jüppner H, Gardella T. Residues in the Membrane-spanning and Extracellular Loop Regions of the Parathyroid Hormone (PTH)-2 Receptor Determine Signaling Selectivity for PTH and PTH-related Peptide*. Journal Of Biological Chemistry 1997, 272: 28861-28868. PMID: 9360953, DOI: 10.1074/jbc.272.46.28861.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell MembraneCOS CellsCyclic AMPHistidineHumansIsoleucineMolecular Sequence DataMutagenesis, Site-DirectedParathyroid HormoneParathyroid Hormone-Related ProteinPeptide FragmentsProteinsReceptor, Parathyroid Hormone, Type 2Receptors, Parathyroid HormoneSequence Homology, Amino AcidSignal TransductionConceptsPTH-2 receptorPTH-1 receptorParathyroid hormoneCOOH-terminal portionCOS-7 cellsCassette substitutionsPTH 1Membrane-spanningPoint mutationsTransmembrane helix 3Helix 3Divergent residuesPTHCOS-7Receptor selectivityResidues 5ReceptorsPTH-related peptideFunctional interactionsPTHrP-(1-36Receptor DetermineReceptor chimerasCAMP responseExtracellular loop 2PTH-2Cloning and characterization of the vitamin D receptor from Xenopus laevis.
Li Y, Bergwitz C, Jüppner H, Demay M. Cloning and characterization of the vitamin D receptor from Xenopus laevis. Endocrinology 1997, 138: 2347-53. PMID: 9165021, DOI: 10.1210/endo.138.6.5210.Peer-Reviewed Original ResearchMeSH KeywordsAgingAmino Acid SequenceAnimalsBase SequenceBone and BonesChickensCloning, MolecularDimerizationEmbryo, NonmammalianFemaleGene Expression Regulation, DevelopmentalHumansIntestine, SmallKidneyMiceMolecular Sequence DataOrgan SpecificityPolymerase Chain ReactionRatsReceptors, CalcitriolReceptors, Retinoic AcidRecombinant ProteinsRetinoic Acid Receptor alphaSequence Homology, Amino AcidSkinSpecies SpecificityXenopus laevisConceptsVitamin D response elementRat osteocalcin vitamin D response elementVitamin D receptorOsteocalcin vitamin D response elementLower vertebrate speciesMessenger RNA speciesHuman vitamin D receptorMouse retinoid X receptor alphaAmino acid residuesRetinoid X receptor alphaRat osteocalcin vitamin D responsive elementAmino acid levelsX receptor alphaVertebrate speciesRNA speciesMammalian cellsTransfected mammalian cellsXenopus developmentDependent transactivationD response elementNuclear receptor superfamilyXenopus tissuesDNA bindingIon homeostasisNorthern analysis