2018
KLF1 E325K-associated Congenital Dyserythropoietic Anemia Type IV
Ravindranath Y, Johnson RM, Goyette G, Buck S, Gadgeel M, Gallagher PG. KLF1 E325K-associated Congenital Dyserythropoietic Anemia Type IV. Journal Of Pediatric Hematology/Oncology 2018, 40: e405-e409. PMID: 29300242, PMCID: PMC6092092, DOI: 10.1097/mph.0000000000001056.Peer-Reviewed Original ResearchConceptsCongenital dyserythropoietic anemia type IVClinical courseSevere clinical courseType IVSevere clinical phenotypeIV patientsFetal anemiaTransfusion dependenceFunctional abnormalitiesClinical phenotypePatientsHematologic phenotypeChildrenErythrocyte membranesPhenotypeSplenectomyAnemiaComplete sex reversalFetalisAbnormalities
2013
Abnormalities of the Erythrocyte Membrane
Gallagher PG. Abnormalities of the Erythrocyte Membrane. Pediatric Clinics Of North America 2013, 60: 1349-1362. PMID: 24237975, PMCID: PMC4155395, DOI: 10.1016/j.pcl.2013.09.001.Peer-Reviewed Original ResearchConceptsCommon primary disordersRole of splenectomyHealth care providersLong-term riskMost patientsSymptomatic anemiaPrimary disorderCare providersPrimary abnormalitySplenectomyPatientsManagement guidelinesHereditary spherocytosisHereditary spherocytosis patientsErythrocyte membranesAbnormalitiesGenetic heterogeneityAnemiaSyndromeTherapyThe common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation
Harper SL, Sriswasdi S, Tang HY, Gaetani M, Gallagher PG, Speicher DW. The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. Blood 2013, 122: 3045-3053. PMID: 23974198, PMCID: PMC3811177, DOI: 10.1182/blood-2013-02-487702.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCross-Linking ReagentsElliptocytosis, HereditaryErythrocyte MembraneHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSpectrinConceptsHereditary elliptocytosisMembrane destabilizationLarge conformational rearrangementsGel filtration analysisMembrane proteinsTetramer assemblyHereditary pyropoikilocytosisBiophysical analysisCommon hereditary elliptocytosisConformational rearrangementsDimer conformationHelical contentTetramerization siteFiltration analysisSpectrin tetramersNovel mechanismUnknown mechanismMutationsBinding assaysSpectrinChemical crosslinkingErythrocyte shapeTetramerErythrocyte membranesMembrane
2011
Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum
Bouyer G, Cueff A, Egée S, Kmiecik J, Maksimova Y, Glogowska E, Gallagher PG, Thomas SL. Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum. Blood 2011, 118: 2305-2312. PMID: 21795748, DOI: 10.1182/blood-2011-01-329300.Peer-Reviewed Original ResearchConceptsPeripheral-type benzodiazepine receptorBenzodiazepine receptorsNew permeability pathwaysP falciparumPlasmodium falciparumFalciparum-infected erythrocytesAnti-malarial therapyP falciparum-infected erythrocytesErythrocyte membranesInfected erythrocytesAnion channelIntraerythrocytic growthFalciparumReceptorsSelective inhibitionEndogenous channelsVoltage-dependent anion channelPharmacologic applicationsPermeability pathwaysErythrocytesMolecular identityObvious targetTherapy
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
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
2005
Molecular mechanisms in the inherited red cell membrane disorders
Liem R, Gallagher P. Molecular mechanisms in the inherited red cell membrane disorders. Drug Discovery Today Disease Mechanisms 2005, 2: 539-545. DOI: 10.1016/j.ddmec.2005.11.004.Peer-Reviewed Original ResearchRed cell membrane disordersSingle molecular defectEpigenetic controlMRNA processingProtein functionGene expressionMolecular mechanismsMolecular defectsErythrocyte membrane structureRed cell membrane abnormalitiesMembrane structureMolecular medicineMutationsMembrane disordersDiverse groupCurrent knowledgeGenesRegion mutationsMolecular heterogeneityPromoter mutationsCell membrane abnormalitiesErythrocyte membranesInherited disorderMembrane abnormalitiesProtein
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 membranesMembraneLociGeneticsBiologyMutation of a highly conserved isoleucine disrupts hydrophobic interactions in the αβ spectrin self-association binding site
Gallagher PG, Zhang Z, Morrow JS, Forget BG. Mutation of a highly conserved isoleucine disrupts hydrophobic interactions in the αβ spectrin self-association binding site. Laboratory Investigation 2004, 84: 229-234. PMID: 14661034, DOI: 10.1038/labinvest.3700029.Peer-Reviewed Original ResearchConceptsBinding sitesAlpha-spectrin mutationsEvolutionary conservationSpectrin functionSpectrin repeatsTriple helical modelAlpha-spectrinGenetic studiesHydrophobic isoleucineHydrophobic interactionsLow-expression alleleMolecular modelingExpression alleleSpectrinFunctional defectsTriple helixMutationsHelical modelIsoleucineErythrocyte membranesDrosophilaClinical phenotypeNeonatal hemolytic anemiaRepeatsHelix
1997
Spectrin St Claude, a Splicing Mutation of the Human α-Spectrin Gene Associated With Severe Poikilocytic Anemia
Fournier C, Nicolas G, Gallagher P, Dhermy D, Grandchamp B, Lecomte M. Spectrin St Claude, a Splicing Mutation of the Human α-Spectrin Gene Associated With Severe Poikilocytic Anemia. Blood 1997, 89: 4584-4590. PMID: 9192783, DOI: 10.1182/blood.v89.12.4584.Peer-Reviewed Original ResearchConceptsAlpha-spectrin chainAcceptor splice siteSplice siteSplicing mutationAlpha-spectrin geneΑ-spectrin geneExon 20New acceptor splice siteMolecular basisTermination codonNovel mRNAInsertion upstreamTract mutationsTryptic digestionMutationsG mutationGenesMRNAHeterozygous parentsErythrocyte membranesMembraneFrame skippingCodonSitesVariantsMutation of a highly conserved residue of betaI spectrin associated with fatal and near-fatal neonatal hemolytic anemia.
Gallagher PG, Petruzzi MJ, Weed SA, Zhang Z, Marchesi SL, Mohandas N, Morrow JS, Forget BG. Mutation of a highly conserved residue of betaI spectrin associated with fatal and near-fatal neonatal hemolytic anemia. Journal Of Clinical Investigation 1997, 99: 267-277. PMID: 9005995, PMCID: PMC507794, DOI: 10.1172/jci119155.Peer-Reviewed Original ResearchMeSH KeywordsAnemia, Hemolytic, CongenitalArginineBase SequenceConserved SequenceErythrocyte MembraneFemaleHomozygoteHumansHydrops FetalisLaosLeucineMaleMembrane ProteinsModels, MolecularMuscle, SkeletalPedigreePeptide MappingPoint MutationPolymerase Chain ReactionProtein ConformationSequence Analysis, DNASpectrinConceptsImportance of leucineEvolutionary conservationSpectrin functionSpectrin repeatsBeta spectrinBetaI spectrinTriple helical modelGenetic studiesSpectrinMutationsSkeletal muscleMolecular modelingTriple helixNormal functionHelical modelLeucineErythrocyte membranesDrosophilaHydrophobic interactionsNeonatal hemolytic anemiaRepeatsHelixConservationResiduesMembrane
1996
Genomic Organization and 5′-Flanking DNA Sequence of the Murine Stomatin Gene (Epb72)
Gallagher P, Turetsky T, Mentzer W. Genomic Organization and 5′-Flanking DNA Sequence of the Murine Stomatin Gene (Epb72). Genomics 1996, 34: 410-412. PMID: 8786142, DOI: 10.1006/geno.1996.0304.Peer-Reviewed Original ResearchConceptsStomatin geneDNA sequencesPotential DNA-binding proteinsIntegral membrane proteinsDNA-binding proteinsGenomic DNA sequencesHousekeeping gene promoterGenomic organizationExon structureGenomic structureChromosomal genesMembrane proteinsGene promoterConsensus sequenceGenomic DNAProtein structureGenesHereditary stomatocytosisSequenceProteinErythrocyte membranesStomatinCloningExonsPromoter
1995
cDNA Structure, Tissue-Specific Expression, and Chromosomal Localization of the Murine Band 7.2b Gene
Gallagher P, Romana M, Lieman J, Ward D. cDNA Structure, Tissue-Specific Expression, and Chromosomal Localization of the Murine Band 7.2b Gene. Blood 1995, 86: 359-365. PMID: 7540886, DOI: 10.1182/blood.v86.1.359.bloodjournal861359.Peer-Reviewed Original ResearchConceptsTissue-specific expressionSingle membrane-spanning domainMembrane-spanning domainsBp of cDNAOpen reading frameChromosomal localizationSignificant homologyReading frameCDNA structureHuman homologueAlpha-helixProtein structureBeta sheetAmino acidsErythrocyte membranesGenesProximal regionDatabase searchingProteinSitu hybridizationCDNADistal regionWider patternsSkeletal muscleExpressionRecurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene.
Gallagher PG, Weed SA, Tse WT, Benoit L, Morrow JS, Marchesi SL, Mohandas N, Forget BG. Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene. Journal Of Clinical Investigation 1995, 95: 1174-1182. PMID: 7883966, PMCID: PMC441455, DOI: 10.1172/jci117766.Peer-Reviewed Original ResearchConceptsBeta-spectrin geneErythrocyte membrane mechanical stabilityPrincipal structural proteinMembrane mechanical stabilitySpectrin functionBeta spectrinErythrocyte membranesNucleotide substitutionsStudy of erythrocytesStructural proteinsAlpha-spectrinGenetic studiesMolecular defectsPoint mutationsSpectrinHydrops fetalisRecombinant peptideMutationsGenesSevere Coomb's negative hemolytic anemiaThird-trimester fetal loss
1993
Poikilocytic hereditary elliptocytosis associated with spectrin Alexandria: an alpha I/50b Kd variant that is caused by a single amino acid deletion
Gallagher P, Roberts W, Benoit L, Speicher D, Marchesi S, Forget B. Poikilocytic hereditary elliptocytosis associated with spectrin Alexandria: an alpha I/50b Kd variant that is caused by a single amino acid deletion. Blood 1993, 82: 2210-2215. DOI: 10.1182/blood.v82.7.2210.bloodjournal8272210.Peer-Reviewed Original ResearchRed blood cellsHereditary elliptocytosisPolymerase chain reactionHeterogeneous disorderBlood cellsSingle amino acid deletionImpaired abilityDifferent severityChain reactionKD variantAffected individualsAlpha iAbnormal peptideAmino acid deletionSpectrin dimer self-associationProteolytic cleavage sitesResidues 470KD peptidePosition 470Limited tryptic digestionAcid deletionProteolytic cleavageErythrocyte membranesAmino acid sequence analysisIndividualsPoikilocytic Hereditary Elliptocytosis Associated With Spectrin Alexandria: An al/50b Kd Variant That Is Caused by a Single Amino Acid Deletion
Gallagher P, Roberts W, Benoit L, Speicher D, Marchesi S, Forget B. Poikilocytic Hereditary Elliptocytosis Associated With Spectrin Alexandria: An al/50b Kd Variant That Is Caused by a Single Amino Acid Deletion. Blood 1993, 82: 2210-2215. PMID: 8400271, DOI: 10.1182/blood.v82.7.2210.2210.Peer-Reviewed Original ResearchConceptsRed blood cellsHereditary elliptocytosisPolymerase chain reactionHeterogeneous disorderBlood cellsSingle amino acid deletionImpaired abilityDifferent severityChain reactionKD variantAffected individualsAlpha iAbnormal peptideAmino acid deletionSpectrin dimer self-associationProteolytic cleavage sitesResidues 470KD peptidePosition 470Limited tryptic digestionAcid deletionProteolytic cleavageErythrocyte membranesAmino acid sequence analysisIndividuals