2010
Acute Down-regulation of Sodium-dependent Phosphate Transporter NPT2a Involves Predominantly the cAMP/PKA Pathway as Revealed by Signaling-selective Parathyroid Hormone Analogs
Nagai S, Okazaki M, Segawa H, Bergwitz C, Dean T, Potts JT, Mahon MJ, Gardella TJ, Jüppner H. Acute Down-regulation of Sodium-dependent Phosphate Transporter NPT2a Involves Predominantly the cAMP/PKA Pathway as Revealed by Signaling-selective Parathyroid Hormone Analogs. Journal Of Biological Chemistry 2010, 286: 1618-1626. PMID: 21047792, PMCID: PMC3020770, DOI: 10.1074/jbc.m110.198416.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleChlorocebus aethiopsCOS CellsCyclic AMPCyclic AMP-Dependent Protein KinasesDown-RegulationHumansIn Vitro TechniquesKidney Tubules, ProximalMaleMiceMice, Inbred C57BLOpossumsOsteoblastsParathyroid HormonePhosphorusPseudohypoparathyroidismRatsSignal TransductionSodiumSodium-Phosphate Cotransporter Proteins, Type IIaConceptsAcute down-regulationNpt2a expressionParathyroid hormoneRenal proximal tubule cellsParathyroid hormone (PTH)/PTH-related peptideCAMP/PKALong-acting PTH analogPTH analogsWild-type miceRenal proximal tubulesIntracellular calcium responsesParathyroid hormone analogProximal tubule cellsOpossum kidney cellsM-PTH(1Prolonged cAMP responsesParathyroid hormone analoguesCAMP/PKA signaling pathwayPTH-dependent regulationRenal brush border membraneClonal cell linesInducing IP(3Pseudohypoparathyroid patientsMembrane expressionCalcium response
2001
Wnts differentially regulate colony growth and differentiation of chondrogenic rat calvaria cells
Bergwitz C, Wendlandt T, Kispert A, Brabant G. Wnts differentially regulate colony growth and differentiation of chondrogenic rat calvaria cells. Biochimica Et Biophysica Acta 2001, 1538: 129-140. PMID: 11336784, DOI: 10.1016/s0167-4889(00)00123-3.Peer-Reviewed Original ResearchConceptsChondrogenic cell lineReporter gene expressionWnt effectsGene expressionCell linesWnt-7aChondrogenic differentiationWnt-5aGreen fluorescence proteinProtein kinase C.Protein kinase CFrizzled-related proteinsCollagen type II promoterLimb patterningSignal transductionEmbryonic developmentRat calvaria cellsWnt familyType II promoterNIH3T3 cellsReporter systemCartilage-specific proteoglycansFluorescence proteinCartilage differentiationKinase C.
2000
A versatile chondrogenic rat calvaria cell line R-tTA-24 that permits tetracycline-regulated gene expression
Bergwitz C, Wendlandt T, Pötter E, Glomb I, Gras K, von zur Mühlen A, Brabant G. A versatile chondrogenic rat calvaria cell line R-tTA-24 that permits tetracycline-regulated gene expression. Histochemistry And Cell Biology 2000, 113: 145-150. PMID: 10766267, DOI: 10.1007/s004180050017.Peer-Reviewed Original ResearchConceptsTetracycline-regulated gene expressionGene expressionTetracycline-regulated gene expression systemStable transfectionChondrogenic differentiationGene expression systemGene of interestBasis of phenotypeTetracycline transactivatorGenetic manipulationHygromycin selectionExpression systemCartilage-specific proteoglycansNeomycin selectionFlexible genetic manipulationLuciferase activityType II expressionCell linesAlcian blue stainingDifferentiationCollagen type II expressionTransfectionExpressionBlue stainingGenes
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
Cloning 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
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 ResearchConceptsParathyroid 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