2023
Multifocal heterotopic ossification in a man with germline variants of LIM Mineralization Protein‐1 (LMP‐1)
Sangadala S, Shore E, Xu M, Bergwitz C, Lozano‐Calderon S, Lin A, Boden S, Kaplan F. Multifocal heterotopic ossification in a man with germline variants of LIM Mineralization Protein‐1 (LMP‐1). American Journal Of Medical Genetics Part A 2023, 191: 2164-2174. PMID: 37218523, DOI: 10.1002/ajmg.a.63304.Peer-Reviewed Original ResearchMeSH KeywordsActivin Receptors, Type IAnimalsCell LineGerm CellsHumansMiceMiddle AgedMyositis OssificansOssification, HeterotopicOsteogenesisSignal TransductionConceptsLIM mineralization protein-1Bone morphogenetic protein (BMP) pathwayGermline variantsBone morphogenetic proteinRecombinant BMP-2LMP-1Gene-disease relationshipsC2C12 cellsGenetic analysisIntracellular proteinsWT proteinHeterotopic ossificationProtein pathwayOsteoblast markersWT cellsBMP-2Protein 1Coding variantsGene-diseaseProtein levelsControl cellsPathogenic variantsLMP-1 variantsCo-transfectionMC3T3 cells
2021
FGF23 signalling and physiology.
Ho BB, Bergwitz C. FGF23 signalling and physiology. Journal Of Molecular Endocrinology 2021, 66: r23-r32. PMID: 33338030, PMCID: PMC8782161, DOI: 10.1530/jme-20-0178.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAnimalsConserved SequenceEvolution, MolecularFibroblast Growth Factor-23HomeostasisHumansPhosphatesSignal TransductionConceptsO-glycosylation of FGF23FGF23 signalingSubtilisin-like proprotein convertase furinSuppressing phosphate reabsorptionProprotein convertase furinPost-translationallyO-glycosylationIntact FGF23C-terminusGenetic activityPrevent proteolysisParacrine FGFsHigh-affinity binding sitesFibroblast growth factor 23Fruit flyActive intact FGF23Convertase furinChronic kidney diseaseFGF23 fragmentsGrowth factor 23Physiological roleEndocrine FGFsDihydroxyvitamin D synthesisHyperphosphatemic disordersIntestinal phosphate absorption
2018
Role of phosphate sensing in bone and mineral metabolism
Chande S, Bergwitz C. Role of phosphate sensing in bone and mineral metabolism. Nature Reviews Endocrinology 2018, 14: 637-655. PMID: 30218014, PMCID: PMC8607960, DOI: 10.1038/s41574-018-0076-3.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsPi transportersSignal transductionPi homeostasisCellular phosphate homeostasisPhosphate homeostasisExpression of Pi transportersPi-sensing mechanismEssential structural componentIntracellular signal transductionPi transportMulticellular organismsInositol pyrophosphatesIntracellular Pi levelsDomain proteinsRegulation of FGF23 expressionPlasma membranePhosphate sensingDisorders of phosphate homeostasisCell metabolismExtracellular matrixCellular levelHomeostasisTransductionGenetic disordersOrganisms
2011
Phosphate Sensing
Bergwitz C, Jüppner H. Phosphate Sensing. Advances In Kidney Disease And Health 2011, 18: 132-144. PMID: 21406298, PMCID: PMC3059779, DOI: 10.1053/j.ackd.2011.01.004.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsAmino acid sequence conservationNumerous cellular functionsMulti-protein complexesDifferent signal transduction cascadesSignal transduction cascadeExpression of genesSignal transduction cascadesEukaryotic organismsMulticellular organismsMetazoan cellsMetazoan orthologsSequence conservationCellular functionsPHO pathwayTransduction cascadePlasma membraneAmbient phosphateCell metabolismExtracellular phosphateYeastGrowth of tissuesPhosphate sensorPhosphate homeostasisPhosphate uptakeCirculating phosphate levels
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
1999
The Cadherin-Catenin System: Implications for Growth and Differentiation of Endocrine Tissues
Pötter E, Bergwitz C, Brabant G. The Cadherin-Catenin System: Implications for Growth and Differentiation of Endocrine Tissues. Endocrine Reviews 1999, 20: 207-239. PMID: 10204118, DOI: 10.1210/edrv.20.2.0362.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsCadherin-catenin systemBeta-catenin/TCF4 complexComplex signal transduction pathwaysCell-cell adhesionNormal cell functionSignal transduction pathwaysLoss-of-functionRegulate cellular differentiationActivation of oncogenesEpigenetic mechanismsExtracellular modulatorsTransduction pathwaysTCF4 complexPosttranscriptional eventsCellular differentiationEndocrine tissuesIntracellular signalingGenetic mouse modelsProcess of tumorigenesisCadherin-cateninsSomatic gene mutationsPreservation of tissue integrityGene silencingCell adhesionC-Myc
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