2012
Fanconi-Bickel Syndrome and Autosomal Recessive Proximal Tubulopathy with Hypercalciuria (ARPTH) Are Allelic Variants Caused by GLUT2 Mutations
Mannstadt M, Magen D, Segawa H, Stanley T, Sharma A, Sasaki S, Bergwitz C, Mounien L, Boepple P, Thorens B, Zelikovic I, Jüppner H. Fanconi-Bickel Syndrome and Autosomal Recessive Proximal Tubulopathy with Hypercalciuria (ARPTH) Are Allelic Variants Caused by GLUT2 Mutations. The Journal Of Clinical Endocrinology & Metabolism 2012, 97: e1978-e1986. PMID: 22865906, PMCID: PMC3462928, DOI: 10.1210/jc.2012-1279.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAmino Acid SequenceAnimalsFamilial Hypophosphatemic RicketsFamily HealthFanconi SyndromeFemaleGenes, RecessiveGenetic VariationGenome-Wide Association StudyGlucose Transporter Type 1Glucose Transporter Type 2HumansHypercalciuriaHypophosphatemia, FamilialKidney Tubules, ProximalMaleMiceMice, TransgenicMolecular Sequence DataOocytesPedigreeRicketsSodium-Phosphate Cotransporter Proteins, Type IIaSodium-Phosphate Cotransporter Proteins, Type IIcXenopus laevisConceptsGlucose transporter 2Sequence analysis of candidate genesCandidate genesSequence analysisGenome-wide linkage scanAnalysis of candidate genesFanconi-Bickel syndromeProximal renal tubulopathyRenal tubulopathyNucleotide sequence analysisGenetic mappingHomozygous mutationPhosphate importLinkage scanMolecular basisXenopus oocytesTransport of glucoseGLUT2 mutationsMolecular levelGenesGlucose transportUrinary phosphate excretionAllelic variantsPhosphate homeostasisDirect nucleotide sequence analysis
2009
Defective O-Glycosylation due to a Novel Homozygous S129P Mutation Is Associated with Lack of Fibroblast Growth Factor 23 Secretion and Tumoral Calcinosis
Bergwitz C, Banerjee S, Abu-Zahra H, Kaji H, Miyauchi A, Sugimoto T, Jüppner H. Defective O-Glycosylation due to a Novel Homozygous S129P Mutation Is Associated with Lack of Fibroblast Growth Factor 23 Secretion and Tumoral Calcinosis. The Journal Of Clinical Endocrinology & Metabolism 2009, 94: 4267-4274. PMID: 19837926, PMCID: PMC2775647, DOI: 10.1210/jc.2009-0961.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsBase SequenceCalcinosisCarrier StateChlorocebus aethiopsCodonCOS CellsDNA PrimersExonsFibroblast Growth Factor-23Fibroblast Growth FactorsGlycosylationHomozygoteHumansHypophosphatemia, FamilialMolecular Sequence DataNeoplasmsPolymorphism, Single NucleotideProlineSerineConceptsExpression vectors encoding wild-typeSerine to prolineHomozygous mutationFraction of lysatesCOS-7 cellsGlycoprotein fractionDefective O-glycosylationMutant hormoneO-glycosylationProtein speciesExon 2Poor secretionCOS-7Western blot analysisGenetic causeCodon 129Hyperphosphatemic tumoral calcinosisMutationsWild-typeFGF23 mutationsAssociated with lackBlot analysisCarriers in vivoFibroblast growth factorLysates
2005
SLC34A3 Mutations in Patients with Hereditary Hypophosphatemic Rickets with Hypercalciuria Predict a Key Role for the Sodium-Phosphate Cotransporter NaPi-IIc in Maintaining Phosphate Homeostasis
Bergwitz C, Roslin NM, Tieder M, Loredo-Osti JC, Bastepe M, Abu-Zahra H, Frappier D, Burkett K, Carpenter TO, Anderson D, Garabédian M, Sermet I, Fujiwara TM, Morgan K, Tenenhouse HS, Jüppner H. SLC34A3 Mutations in Patients with Hereditary Hypophosphatemic Rickets with Hypercalciuria Predict a Key Role for the Sodium-Phosphate Cotransporter NaPi-IIc in Maintaining Phosphate Homeostasis. American Journal Of Human Genetics 2005, 78: 179-192. PMID: 16358214, PMCID: PMC1380228, DOI: 10.1086/499409.Peer-Reviewed Original ResearchConceptsConsanguineous BedouinFirst membrane-spanning domainMembrane-spanning domainsPhosphate homeostasisRenal sodium-phosphate cotransporterNucleotide sequence analysisDihydroxyvitamin D levelsSingle nucleotide deletionHereditary hypophosphatemic ricketsCompound heterozygous missenseSLC34A3 mutationsHomozygous single nucleotide deletionHypophosphatemic ricketsLinkage scanCandidate genesGenomic DNASodium-phosphate cotransporterSequence analysisD levelsHomozygosity mappingDeletion mutationsGenomewide linkage scanKey roleChromosome 9q34Mutations
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
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