1999
Cloning and Characterization of the Murine Histone Deacetylase (HDAC3)
Mahlknecht U, Hoelzer D, Bucala R, Verdin E. Cloning and Characterization of the Murine Histone Deacetylase (HDAC3). Biochemical And Biophysical Research Communications 1999, 263: 482-490. PMID: 10491319, DOI: 10.1006/bbrc.1999.1389.Peer-Reviewed Original ResearchConceptsHistone deacetylasesCore histone proteinsHuman chromosome 5q31Potential tumor suppressor geneHistone acetylation modifiersMalignant myeloid diseasesTumor suppressor geneHistone proteinsTranscriptional complexHistone acetylationDevelopment of cancerHistone deacetylaseSuppressor geneHDAC3Chromosome 5q31Cellular proliferationEnzymatic activityAcetylationMyeloid diseasesImportant insightsOrthologsHistonesCloningDeacetylasesGenesAn inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: Role in tumor cell glycolysis and the Warburg effect
Chesney J, Mitchell R, Benigni F, Bacher M, Spiegel L, Al-Abed Y, Han J, Metz C, Bucala R. An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: Role in tumor cell glycolysis and the Warburg effect. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 3047-3052. PMID: 10077634, PMCID: PMC15892, DOI: 10.1073/pnas.96.6.3047.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsAllosteric RegulationAmino Acid SequenceBase SequenceCell DivisionCell Transformation, NeoplasticCloning, MolecularGene Expression Regulation, NeoplasticGlycolysisHumansMolecular Sequence DataNeoplasmsPhosphofructokinase-2Phosphotransferases (Alcohol Group Acceptor)RNA, MessengerSequence AlignmentTumor Cells, CulturedConceptsGene productsWarburg effectAU-rich instability elementsMRNA instability motifsInducible gene productsTissue-specific isoformsImportant control pointPentose phosphate pathwayNucleic acid biosynthesisHigh glycolytic rateAcid biosynthesisInducible genesInstability motifsTumor cell glycolysisAllosteric regulatorsPhosphate pathwayPFK-2Tumor cell growthInstability elementMultiple copiesCell growthCancer cell linesEnhanced glycolysisCell glycolysisHuman cancer cell lines
1998
Filarial Nematode Parasites Secrete a Homologue of the Human Cytokine Macrophage Migration Inhibitory Factor
Pastrana D, Raghavan N, FitzGerald P, Eisinger S, Metz C, Bucala R, Schleimer R, Bickel C, Scott A. Filarial Nematode Parasites Secrete a Homologue of the Human Cytokine Macrophage Migration Inhibitory Factor. Infection And Immunity 1998, 66: 5955-5963. PMID: 9826378, PMCID: PMC108754, DOI: 10.1128/iai.66.12.5955-5963.1998.Peer-Reviewed Original ResearchConceptsMacrophage migration inhibitory factorCytokine macrophage migration inhibitory factorMonocytes/macrophagesMigration inhibitory factorHuman monocytes/macrophagesExcretory-secretory productsInhibitory factorProinflammatory cytokine macrophage migration inhibitory factorParasite excretory-secretory productsMurine macrophage migration inhibitory factorLong-term chronic infectionsMonocyte/macrophage migrationHost immune responseHuman macrophage migration inhibitory factorFilarial nematode parasitesTh2 responsesTh2 biasAntiparasite immunityChronic infectionImmunological environmentFilarial antigenImmune responseUterine wallCytokine homologuesMacrophage migration
1997
Biochemical and Mutational Investigations of the Enzymatic Activity of Macrophage Migration Inhibitory Factor †
Bendrat K, Al-Abed Y, Callaway D, Peng T, Calandra T, Metz C, Bucala R. Biochemical and Mutational Investigations of the Enzymatic Activity of Macrophage Migration Inhibitory Factor †. Biochemistry 1997, 36: 15356-15362. PMID: 9398265, DOI: 10.1021/bi971153a.Peer-Reviewed Original ResearchConceptsEnzymatic activityL-dopachrome methyl esterN-terminal proline residueSite-directed mutagenesisAmino acid residuesDopachrome tautomerase activityNative solution conditionsMutant proteinsProtein domainsStable trimer formationCarboxy terminusBasic residuesN-terminusProline residuesSDS-PAGE analysisBacterial enzymesHomotrimeric structureAcid residuesCatalytic functionEnzymatic mechanismMutational investigationTrimer formationLow protein concentrationsBiochemical analysisInternal histidineMacrophage Migration Inhibitory Factor (MIF): A Glucocorticoid Counter-Regulator within the Immune System
Calandra T, Bucala R. Macrophage Migration Inhibitory Factor (MIF): A Glucocorticoid Counter-Regulator within the Immune System. Critical Reviews In Immunology 1997, 17: 77-88. PMID: 9034724, DOI: 10.1615/critrevimmunol.v17.i1.30.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCattleChickensGene Expression RegulationGlucocorticoidsHumansInterferon-gammaInterleukinsLipopolysaccharidesMacrophage Migration-Inhibitory FactorsMacrophagesMiceMolecular Sequence DataMolecular StructurePituitary GlandRatsSequence Homology, Amino AcidShock, SepticT-LymphocytesTumor Necrosis Factor-alphaConceptsMacrophage migration inhibitory factorMigration inhibitory factorImmune responseImmune systemT lymphocyte-derived factorInhibitory factorInhibitory effectLymphocyte-derived factorRecombinant MIF proteinIFN-gamma productionIL-1 betaIL-8 productionT cell proliferationAnterior pituitary glandEnigmatic cytokineLethal endotoxemiaIL-6MIF proteinIL-2TNF-alphaCounter regulatorT lymphocytesProtective effectGlucocorticoid inhibitionPituitary glandRole of Macrophage Migration Inhibitory Factor in the Regulation of the Immune Response
Metz C, Bucala R. Role of Macrophage Migration Inhibitory Factor in the Regulation of the Immune Response. Advances In Immunology 1997, 66: 197-223. PMID: 9328642, DOI: 10.1016/s0065-2776(08)60598-2.Peer-Reviewed Original ResearchConceptsMacrophage migration inhibitory factorMigration inhibitory factorT cellsImmune responseInhibitory factorAnti-inflammatory effectsInflammatory disease statesAnterior pituitary glandSeptic shockMIF actionMIF proteinInflammatory responseGlucocorticoid actionImmune systemPituitary glandCorticotrophic cellsGlucocorticoidsInhibitory effectDisease statesBaseline statePotential roleMacrophagesCellsResponseArthritis
1996
NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF)
Mühlhahn P, Czisch M, Georgescu J, Renner C, Ross A, Holak T, Bernhagen J, Bucala R. NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF). Protein Science 1996, 5: 2095-2103. PMID: 8897610, PMCID: PMC2143260, DOI: 10.1002/pro.5560051016.Peer-Reviewed Original ResearchSite-specific modification of apolipoprotein B by advanced glycosylation end-products: implications for lipoprotein clearance and atherogenesis
Bucala R. Site-specific modification of apolipoprotein B by advanced glycosylation end-products: implications for lipoprotein clearance and atherogenesis. Nephrology Dialysis Transplantation 1996, 11: 17-19. PMID: 9044301, DOI: 10.1093/ndt/11.supp5.17.Peer-Reviewed Original ResearchConceptsLDL receptorAGE modificationApolipoprotein BAdvanced glycosylationHuman fibroblast LDL receptorsAGE-modified formAGE-specific antibodiesRegion of apoBNon-diabetic individualsFibroblast LDL receptorLDL receptor binding siteRenal insufficiencyDiabetes mellitusDiabetic patientsElevated LDLAGE-LDLLipoprotein clearanceReceptor binding sitesHuman LDL receptorGeneral populationPlasma clearance kineticsTransgenic miceLDLAGE formationClearance kineticsThe Immunoregulatory Mediator Macrophage Migration Inhibitory Factor (MIF) Catalyzes a Tautomerization Reaction
Rosengren E, Bucala R, Åman P, Jacobsson L, Odh G, Metz C, Rorsman H. The Immunoregulatory Mediator Macrophage Migration Inhibitory Factor (MIF) Catalyzes a Tautomerization Reaction. Molecular Medicine 1996, 2: 143-149. PMID: 8900542, PMCID: PMC2230029, DOI: 10.1007/bf03402210.Peer-Reviewed Original Research
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 siteA Role for DNA Mutations in Diabetes-Associated Teratogenesis in Transgenic Embryos
Lee A, Plump A, DeSimone C, Cerami A, Bucala R. A Role for DNA Mutations in Diabetes-Associated Teratogenesis in Transgenic Embryos. Diabetes 1995, 44: 20-24. PMID: 7813809, DOI: 10.2337/diab.44.1.20.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBlood GlucoseCongenital AbnormalitiesDiabetes Mellitus, ExperimentalDNAEmbryo, MammalianEmbryonic and Fetal DevelopmentFemaleHyperglycemiaLac OperonMaleMiceMice, TransgenicMolecular Sequence DataPolymerase Chain ReactionPregnancyPregnancy in DiabeticsConceptsDNA mutationsDiabetic environmentInsulin-dependent diabetic mothersMaternal diabetic environmentTransgenic mouse model systemCause of deathMouse model systemTransgenic embryosEmbryonic developmentTarget genesDiabetic mothersFetal malformationsGestational periodNormoglycemic conditionsCongenital malformationsHyperglycemic environmentDiabetic embryopathyFirst direct evidenceMutation frequencyModel systemGenotoxic effectsDiabetesMutant frequencyMalformationsTwofold increase
1994
Identification of MIF as a new pituitary hormone and macrophage cytokine and its role in endotoxic shock
Bucala R. Identification of MIF as a new pituitary hormone and macrophage cytokine and its role in endotoxic shock. Immunology Letters 1994, 43: 23-26. PMID: 7737686, DOI: 10.1016/0165-2478(94)00152-9.Peer-Reviewed Original ResearchConceptsPituitary hormonesMacrophage migration inhibitory factorSystemic inflammatory responseMacrophage-derived cytokinesMigration inhibitory factorNovel pituitary hormoneEndotoxic shockMacrophage cytokinesInflammatory responseHost responseInhibitory factorProtein mediatorsHormoneCytokinesMIFPivotal roleEndotoxicResponse