2018
A Ser725Arg mutation in Band 3 abolishes transport function and leads to anemia and renal tubular acidosis
Yang E, Seo-Mayer P, Lezon-Geyda K, Badior KE, Li J, Casey JR, Reithmeier RAF, Gallagher PG. A Ser725Arg mutation in Band 3 abolishes transport function and leads to anemia and renal tubular acidosis. Blood 2018, 131: 1759-1763. PMID: 29483102, PMCID: PMC5897869, DOI: 10.1182/blood-2018-01-827725.Peer-Reviewed Original ResearchAcidosis, Renal TubularAmino Acid SubstitutionAnemiaAnion Exchange Protein 1, ErythrocyteBiological Transport, ActiveHumansInfant, NewbornInfant, Newborn, DiseasesMaleMutation, Missense
2015
Disorders of erythrocyte volume homeostasis
Glogowska E, Gallagher PG. Disorders of erythrocyte volume homeostasis. International Journal Of Laboratory Hematology 2015, 37: 85-91. PMID: 25976965, PMCID: PMC4435826, DOI: 10.1111/ijlh.12357.Peer-Reviewed Original ResearchMeSH KeywordsAnion Exchange Protein 1, ErythrocyteErythrocyte VolumeErythrocytesGlucose Transporter Type 1Hematologic DiseasesHomeostasisHumansMutationWaterWater-Electrolyte ImbalanceConceptsErythrocyte volume homeostasis
2011
A de novo band 3 mutation in hereditary spherocytosis
Bogardus HH, Maksimova YD, Forget BG, Gallagher PG. A de novo band 3 mutation in hereditary spherocytosis. Pediatric Blood & Cancer 2011, 58: 1004-1004. PMID: 22170767, DOI: 10.1002/pbc.23400.Peer-Reviewed Original ResearchAdultAnion Exchange Protein 1, ErythrocyteChildElectrophoresis, Polyacrylamide GelFemaleHumansMaleMutationPedigreeSpherocytosis, Hereditary
2009
The GPA-dependent, spherostomatocytosis mutant AE1 E758K induces GPA-independent, endogenous cation transport in amphibian oocytes
Stewart AK, Vandorpe DH, Heneghan JF, Chebib F, Stolpe K, Akhavein A, Edelman EJ, Maksimova Y, Gallagher PG, Alper SL. The GPA-dependent, spherostomatocytosis mutant AE1 E758K induces GPA-independent, endogenous cation transport in amphibian oocytes. American Journal Of Physiology - Cell Physiology 2009, 298: c283-c297. PMID: 19907019, PMCID: PMC2822494, DOI: 10.1152/ajpcell.00444.2009.Peer-Reviewed Original Research4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAmbystoma mexicanumAmino Acid SequenceAmphibiansAnemia, Hemolytic, CongenitalAnimalsAnion Exchange Protein 1, ErythrocyteBicarbonatesBumetanideCell MembraneCell Membrane PermeabilityChloridesCloning, MolecularDNA Mutational AnalysisFemaleGlycophorinsHeterozygoteHumansHydrogen-Ion ConcentrationKineticsMaleMembrane PotentialsMiddle AgedMolecular Sequence DataMutation, MissenseOocytesOuabainOxalic AcidRubidium RadioisotopesSeverity of Illness IndexSodium Potassium Chloride Symporter InhibitorsSodium-Potassium-Exchanging ATPaseSulfatesXenopus laevisImaging of the diffusion of single band 3 molecules on normal and mutant erythrocytes
Kodippili GC, Spector J, Sullivan C, Kuypers FA, Labotka R, Gallagher PG, Ritchie K, Low PS. Imaging of the diffusion of single band 3 molecules on normal and mutant erythrocytes. Blood 2009, 113: 6237-6245. PMID: 19369229, PMCID: PMC2699255, DOI: 10.1182/blood-2009-02-205450.Peer-Reviewed Original ResearchMeSH KeywordsAnion Exchange Protein 1, ErythrocyteDiffusionElliptocytosis, HereditaryErythrocyte MembraneHumansSpherocytosis, HereditaryConceptsBand 3 moleculesBand 3Membrane componentsPeripheral membrane proteinsMembrane-spanning proteinsProtein-protein interactionsBand 3 populationMembrane proteinsSingle-particle trackingIntact human erythrocytesPlasma membraneIntact normal erythrocytesRed cell pathologyMotile propertiesDiseased cellsHuman erythrocyte membranesMutant erythrocytesCell pathologyProteinEntire complexHuman erythrocytesCompartment sizeErythrocyte membranesMembraneMembrane abnormalities
2007
An 11-amino acid β-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes
Stefanovic M, Markham NO, Parry EM, Garrett-Beal LJ, Cline AP, Gallagher PG, Low PS, Bodine DM. An 11-amino acid β-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 13972-13977. PMID: 17715300, PMCID: PMC1950715, DOI: 10.1073/pnas.0706266104.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBeta-hairpin loopSpectrin-actinPlasma membraneBand 3Transmembrane protein band 3Β-hairpin loopProtein band 3Uncharacterized interactionMembrane proteinsProtein ankyrinCytoskeletal networkMembrane cytoskeletonCytoskeletal systemAnkyrinCurrent structural modelsErythrocyte membranesSLC4A1 geneLoop deletionComplete deficiencyDeletionMembraneMouse erythrocytesStructural supportDomain
2004
Update on the clinical spectrum and genetics of red blood cell membrane disorders.
Gallagher PG. Update on the clinical spectrum and genetics of red blood cell membrane disorders. Current Hematology Reports 2004, 3: 85-91. PMID: 14965483.Peer-Reviewed Original ResearchConceptsStructure/function relationshipsSignificant genetic heterogeneityPrecise genetic defectGenetic lociMolecular biologyRed blood cell membrane disordersSplicing mutationGene deletionNonsense mutationCell membraneFunction relationshipsGenetic heterogeneityGenetic defectsHereditary elliptocytosisMembrane disordersRed blood cell membraneBlood cell membranesHereditary pyropoikilocytosisMutationsBetter understandingErythrocyte membranesMembraneLociGeneticsBiology
2003
Variegated Expression from the Murine Band 3 (AE1) Promoter in Transgenic Mice Is Associated with mRNA Transcript Initiation at Upstream Start Sites and Can Be Suppressed by the Addition of the Chicken β-Globin 5′ HS4 Insulator Element
Frazar TF, Weisbein JL, Anderson SM, Cline AP, Garrett LJ, Felsenfeld G, Gallagher PG, Bodine DM. Variegated Expression from the Murine Band 3 (AE1) Promoter in Transgenic Mice Is Associated with mRNA Transcript Initiation at Upstream Start Sites and Can Be Suppressed by the Addition of the Chicken β-Globin 5′ HS4 Insulator Element. Molecular And Cellular Biology 2003, 23: 4753-4763. PMID: 12832463, PMCID: PMC162203, DOI: 10.1128/mcb.23.14.4753-4763.2003.Peer-Reviewed Original ResearchConceptsStart siteGamma-globin mRNAUpstream start siteVariegated expressionInsulator elementsHuman gamma-globin geneGamma-globin proteinPosition-effect variegationGamma-globin geneErythroid-specific expressionHS4 insulator elementsBeta-globin clusterHigh steady-state levelsTransgenic mouse assaysErythrocyte membrane skeletonTransgenic miceTransgene copy numberTranscript initiationCytoplasmic domainTransmembrane proteinSteady-state levelsRNA transcriptionMembrane skeletonGene promoterBeta spectrin
1997
Hematologically Important Mutations: Band 3 and Protein 4.2 Variants in Hereditary Spherocytosis
Gallagher P, Forget B. Hematologically Important Mutations: Band 3 and Protein 4.2 Variants in Hereditary Spherocytosis. Blood Cells Molecules And Diseases 1997, 23: 417-421. PMID: 9446757, DOI: 10.1006/bcmd.1997.0160.Peer-Reviewed Original ResearchAnion Exchange Protein 1, ErythrocyteBlood ProteinsCytoskeletal ProteinsHumansMembrane ProteinsMutationSpherocytosis, Hereditary
1996
A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.
Jenkins PB, Abou-Alfa GK, Dhermy D, Bursaux E, Féo C, Scarpa AL, Lux SE, Garbarz M, Forget BG, Gallagher PG. A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis. Journal Of Clinical Investigation 1996, 97: 373-380. PMID: 8567957, PMCID: PMC507027, DOI: 10.1172/jci118425.Peer-Reviewed Original ResearchConceptsBand 3 geneCytoplasmic domainNonsense mutationGenomic DNABand 3 cytoplasmic domainErythrocyte band 3 geneErythrocyte membrane mechanical stabilityEntire transmembrane domainBand 3Membrane mechanical stabilityBand 3 proteinTransmembrane domainNucleotide sequenceRT-PCRFamily membersStudy of erythrocytesMRNA accumulationSequence analysisAnion transport studiesBand 3 defectsTypical hereditary spherocytosisHS mutationsReticulocyte RNAUnaffected family membersRNA
1993
Analysis of a Pst I polymorphism of the human erythrocyte band 3 gene (EPB3)
Jenkins P, Gallagher P, Forget B. Analysis of a Pst I polymorphism of the human erythrocyte band 3 gene (EPB3). British Journal Of Haematology 1993, 85: 816-818. PMID: 7918052, DOI: 10.1111/j.1365-2141.1993.tb03232.x.Peer-Reviewed Original Research