2001
Lysozyme Enhances Renal Excretion of Advanced Glycation Endproducts In Vivo and Suppresses Adverse AGE-mediated Cellular Effects In Vitro: A Potential AGE Sequestration Therapy for Diabetic Nephropathy?
Zheng F, Cai W, Mitsuhashi T, Vlassara H, Bucala R. Lysozyme Enhances Renal Excretion of Advanced Glycation Endproducts In Vivo and Suppresses Adverse AGE-mediated Cellular Effects In Vitro: A Potential AGE Sequestration Therapy for Diabetic Nephropathy? Molecular Medicine 2001, 7: 737-747. PMID: 11788787, PMCID: PMC1950004, DOI: 10.1007/bf03401963.Peer-Reviewed Original ResearchConceptsAdvanced glycation endproductsSerum advanced glycation endproductsDb/db miceNon-obese diabeticSerum AGEsMesangial cellsDb miceAGE-BSAGlycation endproductsIGF-I productionDiabetic renal damageSprague-Dawley ratsAGE clearanceSuppress macrophagesNOD miceDiabetic nephropathyRenal damageRenal excretionNormal ratsMMP-9Type IV collagenHost defense proteinsExcretionMRNA levelsMiceMacrophage migration inhibitory factor is an important mediator in the pathogenesis of gastric inflammation in rats
Huang X, Hui C, Chen Y, Chun B, Wong Y, Fung P, Metz C, Cho C, Hui W, Bucala R, Lam S, Lan H. Macrophage migration inhibitory factor is an important mediator in the pathogenesis of gastric inflammation in rats. Gastroenterology 2001, 121: 619-630. PMID: 11522746, DOI: 10.1053/gast.2001.27205.Peer-Reviewed Original ResearchMeSH KeywordsAcetic AcidAcute DiseaseAnimalsAntibodies, MonoclonalDisease Models, AnimalGastritisGene ExpressionIn Situ HybridizationIn Vitro TechniquesIntercellular Adhesion Molecule-1Macrophage Migration-Inhibitory FactorsMacrophagesMaleNeutrophilsNitric Oxide SynthaseNitric Oxide Synthase Type IIRatsRats, Sprague-DawleyRNA, MessengerStomach UlcerTumor Necrosis Factor-alphaWound HealingConceptsAcute gastric ulcerMigration inhibitory factorInducible nitric oxide synthaseGastric ulcerNitric oxide synthaseGastric inflammationMIF antibodyOxide synthaseRole of MIFRat gastric ulcer modelsInhibitory factorMacrophage migration inhibitory factorIntercellular adhesion molecule-1Tumor necrosis factor alphaGastric ulcer modelImmune-mediated diseasesKey inflammatory mediatorsMajor inflammatory cellsAccumulation of macrophagesNecrosis factor alphaAdhesion molecule-1Sites of inflammationNeutrophil accumulationMIF productionUlcer size
1999
Interaction of Borrelia burgdorferi with Peripheral Blood Fibrocytes, Antigen-Presenting Cells with the Potential for Connective Tissue Targeting
Grab D, Lanners H, Martin L, Chesney J, Cai C, Adkisson H, Bucala R. Interaction of Borrelia burgdorferi with Peripheral Blood Fibrocytes, Antigen-Presenting Cells with the Potential for Connective Tissue Targeting. Molecular Medicine 1999, 5: 46-54. PMID: 10072447, PMCID: PMC2230375, DOI: 10.1007/bf03402138.Peer-Reviewed Original ResearchConceptsPeripheral blood fibrocytesBlood fibrocytesDifferent cell typesB. burgdorferiB. burgdorferi bindsInteraction of BorreliaMolecular mechanismsOspB proteinsAntigen presenting cellsCell typesFibroblast-like cellsCellular interactionsCell membraneJoint connective tissuesCollagen type ILyme arthritisPresent antigensInflammatory processT cellsFunctional capacityCellular collagenImmune systemFlow cytometryFibrocytesConnective tissue
1997
Tobacco smoke is a source of toxic reactive glycation products
Cerami C, Founds H, Nicholl I, Mitsuhashi T, Giordano D, Vanpatten S, Lee A, Al-Abed Y, Vlassara H, Bucala R, Cerami A. Tobacco smoke is a source of toxic reactive glycation products. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 13915-13920. PMID: 9391127, PMCID: PMC28407, DOI: 10.1073/pnas.94.25.13915.Peer-Reviewed Original ResearchConceptsAdvanced glycation end productsTobacco smokeGlycation productsAGE formationSerum AGE levelsIncidence of atherosclerosisPlasma of patientsGlycation end productsRenal insufficiencyCerebrovascular diseaseCigarette smokersHuman smokersHigh prevalenceHigh riskSmokersNonsmokersGlycotoxinsPatientsSpecific fluorescenceSerum proteinsDiseaseCuring of tobaccoAqueous extractSmokeTobaccoInsulin secretion is regulated by the glucose-dependent production of islet β cell macrophage migration inhibitory factor
Waeber G, Calandra T, Roduit R, Haefliger J, Bonny C, Thompson N, Thorens B, Temler E, Meinhardt A, Bacher M, Metz C, Nicod P, Bucala R. Insulin secretion is regulated by the glucose-dependent production of islet β cell macrophage migration inhibitory factor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 4782-4787. PMID: 9114069, PMCID: PMC20802, DOI: 10.1073/pnas.94.9.4782.Peer-Reviewed Original ResearchConceptsMacrophage migration inhibitory factorMigration inhibitory factorInsulin releaseInsulin secretionBeta cellsRecombinant macrophage migration inhibitory factorInhibitory factorGlucose-induced insulin releasePancreatic islet beta cellsInsulin-secreting beta cellsINS-1 cell lineIslet beta cellsIsolated rat isletsInsulin secretion responseIslets of LangerhansConcentration-dependent mannerIslet cell productsImmune cellsT lymphocytesPituitary hormonesPerifusion studiesAutocrine fashionRat isletsSecretion responseGlucocorticoid stimulation
1995
Identification of the Major Site of Apolipoprotein B Modification by Advanced Glycosylation End Products Blocking Uptake by the Low Density Lipoprotein Receptor *
Bucala R, Mitchell R, Arnold K, Innerarity T, Vlassara H, Cerami A. Identification of the Major Site of Apolipoprotein B Modification by Advanced Glycosylation End Products Blocking Uptake by the Low Density Lipoprotein Receptor *. Journal Of Biological Chemistry 1995, 270: 10828-10832. PMID: 7738020, DOI: 10.1074/jbc.270.18.10828.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceApolipoproteins BGlycation End Products, AdvancedIn Vitro TechniquesMolecular Sequence DataPeptide MappingReceptors, LDLConceptsLow-density lipoproteinAGE-modified formAdvanced glycosylation end productsLDL receptorApolipoprotein BHuman fibroblast LDL receptorsAGE-specific antibodiesApolipoprotein B modificationDiabetic vascular diseaseLow-density lipoprotein receptorGlycosylation end productsDensity lipoprotein receptorFibroblast LDL receptorMajor siteAGE immunoreactivityRenal insufficiencyGlucose-derived Amadori productsVascular diseasePlasma clearance kineticsDensity lipoproteinLipoprotein receptorAGE formationClearance kineticsAGE modificationPredominant site
1985
Nonenzymatic modification of lens crystallins by prednisolone induces sulfhydryl oxidation and aggregate formation: In vitro and in vivo studies
Bucala R, Manabe S, Urban R, Cerami A. Nonenzymatic modification of lens crystallins by prednisolone induces sulfhydryl oxidation and aggregate formation: In vitro and in vivo studies. Experimental Eye Research 1985, 41: 353-363. PMID: 4065253, DOI: 10.1016/s0014-4835(85)80026-9.Peer-Reviewed Original ResearchConceptsSteroid-induced cataractPossible pharmacological strategiesSteroid therapyLens crystallinsPharmacological strategiesLens opacitiesNonenzymatic modificationGlucocorticoid prednisoloneToxic manifestationsTherapeutic levelsPrednisoloneCataractogenic effectVivo studiesGlucocorticoidsCataractLens proteinsSulfhydryl oxidationGel filtration chromatographyPrevious studiesAddition of dithiothreitol
1984
The reaction of 16α‐hydroxyestrone with erythrocytes in vitro and in vivo
BUCALA R, FISHMAN J, CERAMI A. The reaction of 16α‐hydroxyestrone with erythrocytes in vitro and in vivo. The FEBS Journal 1984, 140: 593-598. PMID: 6723653, DOI: 10.1111/j.1432-1033.1984.tb08143.x.Peer-Reviewed Original ResearchConceptsMembrane proteinsCellular proteinsCell lifeRed cell lifeLysine residuesProteinCovalent adductsHydrophobic chromatographyAcid-precipitable radioactivityRate of incorporationStable covalent adductCellsReverse-phase high-pressure liquid chromatographyElevated levelsResiduesAdduct formationRed cellsElectrophoresisVitro