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-2
1996
Full Activation of Chimeric Receptors by Hybrids between Parathyroid Hormone and Calcitonin EVIDENCE FOR A COMMON PATTERN OF LIGAND-RECEPTOR INTERACTION*
Bergwitz C, Gardella T, Flannery M, Potts J, Kronenberg H, Goldring S, Jüppner H. Full Activation of Chimeric Receptors by Hybrids between Parathyroid Hormone and Calcitonin EVIDENCE FOR A COMMON PATTERN OF LIGAND-RECEPTOR INTERACTION*. Journal Of Biological Chemistry 1996, 271: 26469-26472. PMID: 8900113, DOI: 10.1074/jbc.271.43.26469.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcitoninCOS CellsParathyroid HormoneRatsReceptors, CalcitoninReceptors, Parathyroid HormoneRecombinant Fusion ProteinsConceptsParathyroid hormoneG protein-coupled receptorsProtein-coupled receptorsReceptor chimerasPTH receptorFamily of G protein-coupled receptorsLigand-receptor interactionsPatterns of ligand-receptor interactionsCalcitoninParathyroid hormone receptorReceptorsCommon patternChimeric receptorsHormoneHybrid ligandsAmino acid sequence homologyFull activationSame family
1995
Pseudohypoparathyroidism type Ib is not caused by mutations in the coding exons of the human parathyroid hormone (PTH)/PTH-related peptide receptor gene
Schipani E, Weinstein LS, Bergwitz C, Iida-Klein A, Kong XF, Stuhrmann M, Kruse K, Whyte MP, Murray T, Schmidtke J. Pseudohypoparathyroidism type Ib is not caused by mutations in the coding exons of the human parathyroid hormone (PTH)/PTH-related peptide receptor gene. The Journal Of Clinical Endocrinology & Metabolism 1995, 80: 1611-1621. PMID: 7745008, DOI: 10.1210/jcem.80.5.7745008.Peer-Reviewed Original ResearchConceptsPseudohypoparathyroidism type IbPHP-IbCoding exonsExon GNucleotide sequenceBase changesHuman genomic DNA clonesExon E2Receptor geneTemperature gradient gel electrophoresisGenomic DNA clonesRestriction enzyme mappingReceptor cytoplasmic tailPHP-Ib patientsPTH/PTH-related peptideReverse transcriptase-polymerase chain reactionSplice donor sitePTH/PTHrP receptor geneTranscriptase-polymerase chain reactionGradient gel electrophoresisType IbChain reactionDirect nucleotide sequencingWild-type receptorNorthern blot analysis
1994
Polymorphism in exon M7 of the PTHR gene
Schipani E, Hustmyer FG, Bergwitz C, Jūppner H. Polymorphism in exon M7 of the PTHR gene. Human Molecular Genetics 1994, 3: 1210-1210. PMID: 7981709, DOI: 10.1093/hmg/3.7.1210-a.Peer-Reviewed Original ResearchBase SequenceChromosomes, Human, Pair 3ExonsHumansMolecular Sequence DataPolymerase Chain ReactionPolymorphism, GeneticReceptors, Parathyroid HormoneRapid desensitization of parathyroid hormone dependent adenylate cyclase in perifused human osteosarcoma cells (SaOS-2)
Bergwitz C, Abou-Samra A, Hesch R, Jüppner H. Rapid desensitization of parathyroid hormone dependent adenylate cyclase in perifused human osteosarcoma cells (SaOS-2). Biochimica Et Biophysica Acta 1994, 1222: 447-456. PMID: 8038214, DOI: 10.1016/0167-4889(94)90053-1.Peer-Reviewed Original ResearchMeSH Keywords8-Bromo Cyclic Adenosine MonophosphateAdenylyl CyclasesCyclic AMPHumansOsteosarcomaParathyroid HormonePerfusionReceptors, Parathyroid HormoneTetradecanoylphorbol AcetateTumor Cells, CulturedConceptsApplication of parathyroid hormoneParathyroid hormonePTH(1-34CAMP releasePerifusion systemIncrease bone mass in vivoHormone-dependent adenylate cyclaseAdenylate cyclaseSaos-2 cellsReceptor internalizationPMA pre-treatmentDose-dependent increaseCyclic AMP accumulationBone mass in vivoStimulated cAMP accumulationHuman osteosarcoma cell line Saos-2Saos-2Osteosarcoma cell line Saos-2Cells in vitroMass in vivoBone massPerifusion experimentsBPTH(3-34Human osteosarcoma cellsHomologous desensitization