2023
Plant MDL proteins synergize with the cytokine MIF at CXCR2 and CXCR4 receptors in human cells
Spiller L, Manjula R, Leissing F, Basquin J, Bourilhon P, Sinitski D, Brandhofer M, Levecque S, Gerra S, Sabelleck B, Zhang L, Feederle R, Flatley A, Hoffmann A, Panstruga R, Bernhagen J, Lolis E. Plant MDL proteins synergize with the cytokine MIF at CXCR2 and CXCR4 receptors in human cells. Science Signaling 2023, 16: eadg2621. PMID: 37988455, DOI: 10.1126/scisignal.adg2621.Peer-Reviewed Original ResearchConceptsMammalian macrophage migration inhibitory factorHetero-oligomeric complexesHigh structural similarityMultifunctional inflammatory cytokineHuman lung epithelial cellsYeast reporter systemReporter systemLung epithelial cellsPlant leavesFunctional similarityCellular responsesHuman cellsPharmacological inhibitorsDopachrome tautomeraseFunctional implicationsX-ray crystallographyMacrophage migration inhibitory factorStructural similarityEpithelial cellsMigration inhibitory factorCXCR4 receptorProteinTautomerase activityCellsMIF receptor
2010
AV411 (Ibudilast) and AV1013 are non-competitive inhibitors of macrophage migration inhibitory factor: a novel induced-fit allosteric inhibition mechanism (133.11)
Cho Y, Crichlow G, Vermeire J, Leng L, Du X, Hodsdon M, Bucala R, Cappello M, Gross M, Gaeta F, Johnson K, Lolis E. AV411 (Ibudilast) and AV1013 are non-competitive inhibitors of macrophage migration inhibitory factor: a novel induced-fit allosteric inhibition mechanism (133.11). The Journal Of Immunology 2010, 184: 133.11-133.11. DOI: 10.4049/jimmunol.184.supp.133.11.Peer-Reviewed Original ResearchMacrophage migration inhibitory factorMigration inhibitory factorInhibitory factorPro-inflammatory proteinsAnti-inflammatory activityAnti-inflammatory drugsNon-selective inhibitorPDE inhibitor rolipramNeuropathic painOpioid withdrawalBronchial asthmaOcular indicationsGlial cellsNon-competitive inhibitorPossible therapeuticsInhibitor rolipramChemotactic functionAV411Tautomerase activityInhibitorsAllosteric binding siteIsobutylmethylxanthineTreatmentAsthmaPain
1999
Pro-1 of Macrophage Migration Inhibitory Factor Functions as a Catalytic Base in the Phenylpyruvate Tautomerase Activity † , ‡
Lubetsky J, Swope M, Dealwis C, Blake P, Lolis E. Pro-1 of Macrophage Migration Inhibitory Factor Functions as a Catalytic Base in the Phenylpyruvate Tautomerase Activity † , ‡. Biochemistry 1999, 38: 7346-7354. PMID: 10353846, DOI: 10.1021/bi990306m.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsBinding SitesCatalysisCrystallography, X-RayEnzyme ActivationGlycineHumansHydrogen-Ion ConcentrationIntramolecular OxidoreductasesMacromolecular SubstancesMacrophage Migration-Inhibitory FactorsMethionineMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhenylpyruvic AcidsProlineRecombinant ProteinsConceptsMacrophage migration inhibitory factorMacrophage migration inhibitory factor (MIF) functionsAnti-inflammatory effectsMigration inhibitory factorImportant immunoregulatory moleculeTautomerase activityImmunoregulatory moleculesPhenylpyruvate tautomerase activityInhibitory factorP-hydroxyphenylpyruvateGlucocorticoidsPro-1CytokinesActivity