Featured Publications
Bone marrow sinusoidal endothelial cells are a site of Fgf23 upregulation in a mouse model of iron deficiency anemia
Li X, Lozovatsky L, Tommasini S, Fretz J, Finberg K. Bone marrow sinusoidal endothelial cells are a site of Fgf23 upregulation in a mouse model of iron deficiency anemia. Blood Advances 2023, 7: 5156-5171. PMID: 37417950, PMCID: PMC10480544, DOI: 10.1182/bloodadvances.2022009524.Peer-Reviewed Original ResearchConceptsSinusoidal endothelial cellsEndothelial cellsBone marrowBM sectionsFGF23 upregulationFibroblast growth factor 23Iron deficiencyElevated serum erythropoietinFGF23 promoter activityBM endothelial cellsGrowth factor 23Vitamin D metabolismIron deficiency anemiaSystemic iron deficiencyKnockout mice exhibitBone marrow sinusoidal endothelial cellsNormal iron balanceNonanemic controlsChronic anemiaFactor 23D metabolismEndothelial cell populationErythropoietin treatmentDeficiency anemiaMouse modelIL‐1β Drives Production of FGF‐23 at the Onset of Chronic Kidney Disease in Mice
McKnight Q, Jenkins S, Li X, Nelson T, Marlier A, Cantley LG, Finberg KE, Fretz JA. IL‐1β Drives Production of FGF‐23 at the Onset of Chronic Kidney Disease in Mice. Journal Of Bone And Mineral Research 2020, 35: 1352-1362. PMID: 32154933, PMCID: PMC7363582, DOI: 10.1002/jbmr.4003.Peer-Reviewed Original ResearchConceptsChronic kidney diseaseOnset of CKDEarly chronic kidney diseaseFGF-23 expressionFGF-23Renal dysfunctionParathyroid hormoneIL-1βCongenital chronic kidney diseaseFGF-23 levelsSerum parathyroid hormoneGlomerular capillary tuftCongenital modelSerum phosphateIron bioavailabilitySystemic elevationVitamin DInflammatory cytokinesKidney diseaseEarly biomarkersIron statusMouse modelPhosphate imbalanceInitial upregulationCapillary tuftNCOA4 is regulated by HIF and mediates mobilization of murine hepatic iron stores after blood loss
Li X, Lozovatsky L, Sukumaran A, Gonzalez L, Jain A, Liu D, Ayala-Lopez N, Finberg KE. NCOA4 is regulated by HIF and mediates mobilization of murine hepatic iron stores after blood loss. Blood 2020, 136: 2691-2702. PMID: 32659785, PMCID: PMC7735158, DOI: 10.1182/blood.2020006321.Peer-Reviewed Original ResearchConceptsHepatic iron storesHypoxia-inducible factorNonheme iron concentrationsIron storesBlood lossNCOA4 expressionSubunit levelsHIF-2α knockdownMurine hepatoma cell lineMessenger RNA inductionDietary ironHepatic responseHepatoma cell lineHIF-1αHepatic originIron deficiencyInducible factorMiceCell linesNCOA4PhlebotomyModest effectRNA inductionIron concentrationProlyl hydroxylasesLow iron promotes megakaryocytic commitment of megakaryocytic-erythroid progenitors in humans and mice
Xavier-Ferrucio J, Scanlon V, Li X, Zhang PX, Lozovatsky L, Ayala-Lopez N, Tebaldi T, Halene S, Cao C, Fleming MD, Finberg KE, Krause DS. Low iron promotes megakaryocytic commitment of megakaryocytic-erythroid progenitors in humans and mice. Blood 2019, 134: 1547-1557. PMID: 31439541, PMCID: PMC6839952, DOI: 10.1182/blood.2019002039.Peer-Reviewed Original ResearchConceptsMK lineage commitmentExtracellular signal-regulated kinase (ERK) pathwaySignal-regulated kinase pathwayMegakaryocytic-erythroid progenitorsBone marrow transplantation assaysSignal transduction analysisIron-deficient conditionsGene expression analysisMegakaryocytic commitmentLineage commitmentTransferrin receptor 2MK lineageTmprss6-/- miceIron sensorExpression analysisKinase pathwayTransduction analysisTransplantation assaysErythroid progenitorsMarrow environmentHematopoietic cellsMessenger RNAPhospho-ERK1/2Systemic iron deficiencyLow ironTmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice
Finberg KE, Whittlesey RL, Andrews NC. Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice. Blood 2011, 117: 4590-4599. PMID: 21355094, PMCID: PMC3099575, DOI: 10.1182/blood-2010-10-315507.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimicrobial Cationic PeptidesFemaleGenotypeHemochromatosisHemochromatosis ProteinHepcidinsHeterozygoteHistocompatibility Antigens Class IHomozygoteHumansIronLiverMaleMembrane ProteinsMiceMice, Inbred C57BLMice, TransgenicPhenotypeSerine EndopeptidasesSignal TransductionUp-RegulationConceptsBMP/SmadBone morphogenetic proteinSystemic iron deficiencyGenetic lossHereditary hemochromatosis protein HFENatural genetic variationHemochromatosis protein HFEIron deficiencySmad target genesIron deficiency anemiaSystemic iron overloadElevated hepatic expressionExpression of hepcidinIron-refractory iron deficiency anemiaTransmembrane serine proteaseDietary iron absorptionSystemic iron homeostasisGenetic variationGenetic approachesTarget genesMacrophage iron releaseHepcidin elevationMorphogenetic proteinsDeficiency anemiaHepcidin productionDown-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis
Finberg KE, Whittlesey RL, Fleming MD, Andrews NC. Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis. Blood 2010, 115: 3817-3826. PMID: 20200349, PMCID: PMC2865872, DOI: 10.1182/blood-2009-05-224808.Peer-Reviewed Original ResearchMeSH KeywordsAnemia, Iron-DeficiencyAnimalsAntimicrobial Cationic PeptidesBlotting, WesternBone Morphogenetic ProteinsDown-RegulationFemaleGPI-Linked ProteinsHemochromatosis ProteinHepatocytesHepcidinsHomeostasisInhibitor of Differentiation Protein 1IronLiverMembrane ProteinsMiceMice, Inbred C57BLMice, KnockoutReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSerine EndopeptidasesSignal TransductionSmad ProteinsConceptsIron deficiency anemiaSystemic iron homeostasisHepcidin expressionSmad signalingIntravenous iron therapyOral iron treatmentSystemic iron overloadIron regulatory hormone hepcidinBMP/Smad signalingBmp6 mRNA levelsSmad Signaling PathwayIron homeostasisIron therapyIron storesDeficiency anemiaIron overloadHepatic levelsType II transmembrane serine proteaseIRIDA patientsTransmembrane serine proteaseFamilial disorderHormone hepcidinIron treatmentHepcidin transcriptionMiceGenetic loss of Tmprss6 alters terminal erythroid differentiation in a mouse model of β-thalassemia intermedia
Stagg DB, Whittlesey RL, Li X, Lozovatsky L, Gardenghi S, Rivella S, Finberg KE. Genetic loss of Tmprss6 alters terminal erythroid differentiation in a mouse model of β-thalassemia intermedia. Haematologica 2019, 104: e442-e446. PMID: 30819909, PMCID: PMC6886429, DOI: 10.3324/haematol.2018.213371.Peer-Reviewed Original Research
2019
Going solo in iron transport
Finberg KE. Going solo in iron transport. Blood 2019, 134: 1363-1364. PMID: 31698431, DOI: 10.1182/blood.2019003019.Commentaries, Editorials and Letters
2015
Ironing out the role of Toll-like receptors
Finberg KE. Ironing out the role of Toll-like receptors. Blood 2015, 125: 2183-2184. PMID: 25838278, DOI: 10.1182/blood-2015-02-628412.Commentaries, Editorials and Letters
2013
Striking the target in iron overload disorders
Finberg KE. Striking the target in iron overload disorders. Journal Of Clinical Investigation 2013, 123: 1424-1427. PMID: 23524962, PMCID: PMC3613936, DOI: 10.1172/jci68889.Commentaries, Editorials and LettersConceptsIron overload disordersOverload disordersBody iron storesAdministration of antisenseSystemic iron homeostasisIron storesClinical conditionsMouse modelIron balanceHereditary hemochromatosisDisease severityHepatic proteinsΒ-thalassemiaIron homeostasisMajor siteDisordersTMPRSS6TherapyHemochromatosisLiverAdministrationSeverity
2012
Altered V-ATPase expression in renal intercalated cells isolated from B1 subunit-deficient mice by fluorescence-activated cell sorting
Vedovelli L, Rothermel JT, Finberg KE, Wagner CA, Azroyan A, Hill E, Breton S, Brown D, Păunescu T. Altered V-ATPase expression in renal intercalated cells isolated from B1 subunit-deficient mice by fluorescence-activated cell sorting. American Journal Of Physiology. Renal Physiology 2012, 304: f522-f532. PMID: 23269648, PMCID: PMC3602708, DOI: 10.1152/ajprenal.00394.2012.Peer-Reviewed Original ResearchConceptsV-ATPase expressionVacuolar proton-pumping ATPaseProtein levelsV-ATPase subunitsFluorescence-assisted cellProton-pumping ATPaseV-ATPase AWestern blotFluorescence-activated cell sortingV-ATPasesSubunit protein levelsE1 subunitSubunit promoterQuantitative Western blotApical membraneEGFP expressionH subunitAcid-base homeostasisEGFPSubunitsCell sortingExpressionCytosol fractionCellsMembrane
2006
The connecting tubule is the main site of the furosemide-induced urinary acidification by the vacuolar H+-ATPase
Kovacikova J, Winter C, Loffing-Cueni D, Loffing J, Finberg K, Lifton R, Hummler E, Rossier B, Wagner C. The connecting tubule is the main site of the furosemide-induced urinary acidification by the vacuolar H+-ATPase. Kidney International 2006, 70: 1706-1716. PMID: 16985514, DOI: 10.1038/sj.ki.5001851.Peer-Reviewed Original ResearchMeSH KeywordsAcid-Base EquilibriumAmilorideAnimalsDiureticsEpithelial Sodium ChannelsFurosemideGene Expression RegulationGene Expression Regulation, EnzymologicHydrochlorothiazideHydrogen-Ion ConcentrationKidney Tubules, CollectingKidney Tubules, DistalMetabolic Clearance RateMiceMice, KnockoutNephronsProton-Translocating ATPasesWater-Electrolyte BalanceConceptsUrinary acidificationRenal clearance experimentsEffect of furosemideNormal urinary acidificationLumen-negative voltageNet acid excretionThick ascending limbFinal urinary acidificationKidney-specific inactivationENaC channelsClearance experimentsAcid excretionMouse modelAscending limbFurosemideDuct cellsProton secretionMiceExact localizationReabsorptionMain siteB1 subunitAlpha subunitTubulesFunctional expression
2005
The B1-subunit of the H+ ATPase is required for maximal urinary acidification
Finberg KE, Wagner CA, Bailey MA, Păunescu T, Breton S, Brown D, Giebisch G, Geibel JP, Lifton RP. The B1-subunit of the H+ ATPase is required for maximal urinary acidification. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 13616-13621. PMID: 16174750, PMCID: PMC1224669, DOI: 10.1073/pnas.0506769102.Peer-Reviewed Original ResearchConceptsMaximal urinary acidificationNormal urinary acidificationMetabolic acidosisUrinary acidificationDistal renal tubular acidosisAcid challengeRenal tubular acidosisAcute intracellular acidificationB1 subunitLumen-negative potentialFurosemide infusionTubular acidosisAlkaline urineDistal nephronGreater severityAcidosisMiceLoss of B1Intracellular acidificationApical expressionUrineDuctFurther decreaseIsoformsPlasma membrane
2004
Renal Vacuolar H+-ATPase
Wagner CA, Finberg KE, Breton S, Marshansky V, Brown D, Geibel JP. Renal Vacuolar H+-ATPase. Physiological Reviews 2004, 84: 1263-1314. PMID: 15383652, DOI: 10.1152/physrev.00045.2003.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsProximal tubular bicarbonate reabsorptionDistal renal tubular acidosisTubular bicarbonate reabsorptionRenal tubular acidosisFinal urinary acidificationTubular acidosisElectrolyte statusBicarbonate reabsorptionMonogenic defectsProximal tubulesUrinary acidificationKidneyATP-dependent transportVariety of factorsHigher numberPatientsIntracellular organellesAcidosisRegulatory proteinsLocalization patterns
2003
Localization and Regulation of the ATP6V0A4 (a4) Vacuolar H+-ATPase Subunit Defective in an Inherited Form of Distal Renal Tubular Acidosis
Stehberger PA, Schulz N, Finberg KE, Karet FE, Giebisch G, Lifton RP, Geibel JP, Wagner CA. Localization and Regulation of the ATP6V0A4 (a4) Vacuolar H+-ATPase Subunit Defective in an Inherited Form of Distal Renal Tubular Acidosis. Journal Of The American Society Of Nephrology 2003, 14: 3027-3038. PMID: 14638902, DOI: 10.1097/01.asn.0000099375.74789.ab.Peer-Reviewed Original ResearchConceptsDistal renal tubular acidosisRenal tubular acidosisLoop of HenleProximal tubulesTubular acidosisMouse kidneyA4 expressionDistal tubulesDistal convoluted tubuleProtein expression levelsElectrolyte intakeA4 proteinConvoluted tubulesMouse nephron segmentsNephron segmentsApical stainingWestern blottingAcidosisProtein expressionKidneyATPase activityDistal portionHenleExpression levelsTubulesMolecular cloning and characterization of Atp6v1b1, the murine vacuolar H+-ATPase B1-subunit
Finberg KE, Wagner CA, Stehberger PA, Geibel JP, Lifton RP. Molecular cloning and characterization of Atp6v1b1, the murine vacuolar H+-ATPase B1-subunit. Gene 2003, 318: 25-34. PMID: 14585495, DOI: 10.1016/s0378-1119(03)00790-x.Peer-Reviewed Original ResearchMeSH Keywords5' Flanking RegionAmino Acid SequenceAnimalsAntibody SpecificityBase SequenceCloning, MolecularDNADNA, ComplementaryEpididymisGene Expression Regulation, EnzymologicHumansImmune SeraImmunohistochemistryIsoenzymesKidneyMaleMiceMice, Inbred StrainsMolecular Sequence DataPhylogenyProtein SubunitsRNA, MessengerSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidSequence Homology, Nucleic AcidVacuolar Proton-Translocating ATPasesConceptsDistal renal tubular acidosisRenal tubular acidosisMouse renal cortexProton-translocating ATPasesTubular acidosisRenal cortexSubset of tissuesAnimal modelsATP6V1B1Major organsGenomic organizationGenomic lociMouse kidneyProtein levelsMolecular cloningAcid proteinPlasma membraneMurine orthologIntracellular organellesB1 isoformKidneyNorthern blottingMice lacking the B1 subunit of H+-ATPase have normal hearing
Dou H, Finberg K, Cardell EL, Lifton R, Choo D. Mice lacking the B1 subunit of H+-ATPase have normal hearing. Hearing Research 2003, 180: 76-84. PMID: 12782355, DOI: 10.1016/s0378-5955(03)00108-4.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAnimalsAnimals, NewbornAuditory ThresholdCochleaEar, InnerEmbryo, MammalianEmbryonic and Fetal DevelopmentEvoked Potentials, Auditory, Brain StemFemaleHearingIn Situ HybridizationMaleMiceMice, KnockoutProtein SubunitsTissue DistributionVacuolar Proton-Translocating ATPasesConceptsNormal inner ear functionInner ear functionMouse inner earInner earEar functionNormal hearingAuditory brainstem response testAutosomal recessive distal renal tubular acidosisSubunit null mutant miceDistal renal tubular acidosisInner ear developmentNormal inner ear developmentRecessive distal renal tubular acidosisRenal tubular acidosisSensorineural hearing lossB1 subunitNull mutant miceAcid-base homeostasisPhysiologic assessmentTubular acidosisClinical dataHearing lossPhysiologic effectsDuct epitheliumATPase B1 subunit
2002
Regulation of the expression of the Cl-/anion exchanger pendrin in mouse kidney by acid-base status
Wagner CA, Finberg KE, Stehberger PA, Lifton RP, Giebisch GH, Aronson PS, Geibel JP. Regulation of the expression of the Cl-/anion exchanger pendrin in mouse kidney by acid-base status. Kidney International 2002, 62: 2109-2117. PMID: 12427135, DOI: 10.1046/j.1523-1755.2002.00671.x.Peer-Reviewed Original ResearchConceptsPendrin-positive cellsAcid-base statusPositive cellsBicarbonate secretionMouse kidneyAcid-base transportKnockout mouse modelProtein expression levelsMetabolic alkalosisDeficient dietExchanger pendrinPendrin expressionMouse modelSensorineural deafnessThyroid glandBicarbonate loadPendred syndromeWestern blottingApical membraneInner earPendrin proteinControl levelsKidneyPendrinProtein levels
2001
Molecular Cloning and Characterization of Atp6n1b A NOVEL FOURTH MURINE VACUOLAR H+-ATPase a-SUBUNIT GENE*
Smith A, Finberg K, Wagner C, Lifton R, Devonald M, Su Y, Karet F. Molecular Cloning and Characterization of Atp6n1b A NOVEL FOURTH MURINE VACUOLAR H+-ATPase a-SUBUNIT GENE*. Journal Of Biological Chemistry 2001, 276: 42382-42388. PMID: 11495928, DOI: 10.1074/jbc.m107267200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAquaporin 2Aquaporin 6AquaporinsChromosome MappingCloning, MolecularMiceMolecular Sequence DataPhylogenyPolymorphism, GeneticPregnancy ProteinsProtein SubunitsProton PumpsProton-Translocating ATPasesReverse Transcriptase Polymerase Chain ReactionSuppressor Factors, ImmunologicVacuolar Proton-Translocating ATPasesConceptsAutosomal recessive distal renal tubular acidosisDistal renal tubular acidosisRecessive distal renal tubular acidosisMale genital tissuesRenal tubular acidosisReverse transcription-polymerase chain reactionTranscription-polymerase chain reactionPolymerase chain reactionTubular acidosisGenital tissues