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
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
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