2009
Imaging 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 ResearchConceptsBand 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
Regulators of Erythrocyte Volume as Modifiers in Sickle Cell Disease: The Gardos Channel.
Tian C, Okam M, Alper S, Steinberg M, Brugnara C, Gallagher P. Regulators of Erythrocyte Volume as Modifiers in Sickle Cell Disease: The Gardos Channel. Blood 2007, 110: 3387. DOI: 10.1182/blood.v110.11.3387.3387.Peer-Reviewed Original ResearchModifier genesMissense mutationsChannel genesSequence analysisErythrocyte hydrationSmaller mRNA speciesGenetic variantsReverse transcription-PCR analysisNucleotide sequence analysisBand 3Disease-associated mutationsCore promoter regionFunction of transportersBand 3 geneAquaporin-1 geneAberrant mRNAsSmaller transcriptMRNA speciesIdentification of targetsAquaporin 3 genePromoter regionSplice junctionsChannel proteinsChannel mRNARegion exonsAn 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
2005
Genetic Evidence That an 11 Amino Acid β-Hairpin Loop in the Cytoplasmic Domain of Band 3 Is Responsible for at Least 50% of Ankyrin Binding in Mouse Erythrocytes.
Markham N, Parry E, Stefanovic M, Gallagher P, Low P, Bodine D. Genetic Evidence That an 11 Amino Acid β-Hairpin Loop in the Cytoplasmic Domain of Band 3 Is Responsible for at Least 50% of Ankyrin Binding in Mouse Erythrocytes. Blood 2005, 106: 1659. DOI: 10.1182/blood.v106.11.1659.1659.Peer-Reviewed Original ResearchΒ-hairpin loopCytoplasmic domainWild typeHuman band 3Neomycin resistance geneMembrane proteinsBand 3Mutant allelesBand 3 cytoplasmic domainResistance genesLevels of mRNARed cell membrane proteinsIntegral erythrocyte membrane proteinsSpectrin-actin cytoskeletonCre recombinase proteinDomain 3Embryonic stem cellsQuantitative RT-PCR analysisCell membrane proteinsNormal Mendelian ratioBand 3 mRNATransgenic miceAnion exchange proteinMutant erythrocytesBand 3 geneAdducin Forms a Bridge between the Spectrin-Actin Junctional Complex and Band 3.
Anong W, Mohandas N, An X, Bodine D, Markham N, Gallagher P, Low P. Adducin Forms a Bridge between the Spectrin-Actin Junctional Complex and Band 3. Blood 2005, 106: 808. DOI: 10.1182/blood.v106.11.808.808.Peer-Reviewed Original Research
2004
Multiple Defects in Erythroid Gene Expression in Erythroid Krupple-Like Factor (EKLF) Target Genes in EKLF-Deficient Mice.
Gallagher P, Pilon A, Arcasoy M, Bodine D. Multiple Defects in Erythroid Gene Expression in Erythroid Krupple-Like Factor (EKLF) Target Genes in EKLF-Deficient Mice. Blood 2004, 104: 1602. DOI: 10.1182/blood.v104.11.1602.1602.Peer-Reviewed Original ResearchDNaseI hypersensitive sitesSubtractive hybridizationHypersensitive sitesΒ-globin geneHistone H3Transcription factorsTarget genesFetal liver cellsΒ-spectrinGene expressionΒ-globinErythroid gene expressionMouse Genome 430 2.0 ArrayAffymetrix GeneChip Mouse Genome 430 2.0 ArrayFactor target genesAHSP gene expressionChromatin immunoprecipitation analysisBand 3Mature erythroid progenitorsAHSP promoterRBC membrane proteinsErythroid genesChromatin upstreamChromatin modulatorsRegulated genes
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