2012
Inhibition of TNF-α Improves the Bladder Dysfunction That Is Associated With Type 2 Diabetes
Wang Z, Cheng Z, Cristofaro V, Li J, Xiao X, Gomez P, Ge R, Gong E, Strle K, Sullivan M, Adam R, White M, Olumi A. Inhibition of TNF-α Improves the Bladder Dysfunction That Is Associated With Type 2 Diabetes. Diabetes 2012, 61: 2134-2145. PMID: 22688336, PMCID: PMC3402324, DOI: 10.2337/db11-1763.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDiabetes Mellitus, Type 2Disease Models, AnimalInsulin Receptor Substrate ProteinsMetforminMiceMice, KnockoutMuscle ContractionMyosin Light ChainsReceptors, Tumor Necrosis Factor, Type IRho-Associated KinasesTumor Necrosis Factor-alphaUp-RegulationUrinary BladderUrinary Bladder DiseasesUrinary Bladder, OveractiveConceptsDiabetic bladder dysfunctionTumor necrosis factorType 2 diabetesBladder dysfunctionDKO animalsPrimary cultured bladder smooth muscle cellsSoluble TNF receptor 1Bladder smooth muscle tissueInhibition of TNFCultured bladder smooth muscle cellsAppropriate animal modelsBladder smooth muscle cellsTNF receptor 1Smooth muscle cellsRho-kinase activitySmooth muscle tissueInsulin receptor substrate-1Detrusor hypoactivityUrologic complicationsDetrusor overactivitySystemic treatmentDiabetic patientsClinical featuresBladder fillingVoided volume
2001
Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action*
Aguirre V, Werner E, Giraud J, Lee Y, Shoelson S, White M. Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action*. Journal Of Biological Chemistry 2001, 277: 1531-1537. PMID: 11606564, DOI: 10.1074/jbc.m101521200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnisomycinAnti-Bacterial AgentsCell LineHumansInsulinInsulin Receptor Substrate ProteinsMitogen-Activated Protein Kinase 8Mitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationRatsReceptor, InsulinRecombinant Fusion ProteinsSignal TransductionTumor Necrosis Factor-alphaTwo-Hybrid System TechniquesConceptsInsulin receptor substrate-1Phosphotyrosine-binding (PTB) domainInsulin receptorPotential phosphorylation sitesPhosphorylation of Ser307Stress-activated kinasesInsulin-stimulated kinasesReceptor substrate-1Insulin signal transductionPTB domainMAPK cascadePhosphorylation sitesMyeloid progenitor cellsSignal transductionSerine residuesCatalytic domainSerine phosphorylationDomain functionsSubstrate-1Insulin stimulationCell backgroundPhosphorylationProgenitor cellsGeneral mechanismMechanism of inhibitionInsulin/IGF-1 and TNF-α stimulate phosphorylation of IRS-1 at inhibitory Ser307 via distinct pathways
Rui L, Aguirre V, Kim J, Shulman G, Lee A, Corbould A, Dunaif A, White M. Insulin/IGF-1 and TNF-α stimulate phosphorylation of IRS-1 at inhibitory Ser307 via distinct pathways. Journal Of Clinical Investigation 2001, 107: 181-189. PMID: 11160134, PMCID: PMC199174, DOI: 10.1172/jci10934.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnisomycinCHO CellsCricetinaeInsulinInsulin AntagonistsInsulin ResistanceInsulin-Like Growth Factor IMAP Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesPhosphatidylinositol 3-KinasesPhosphorylationProtein Serine-Threonine KinasesReceptor, InsulinSerineSignal TransductionTumor Necrosis Factor-alphaTyrosineConceptsPhosphorylation of Ser307IRS-1Serine/threonine phosphorylationTNF-alpha-stimulated phosphorylationInsulin-stimulated tyrosine phosphorylationRelevant phosphorylation sitesDistinct kinase pathwaysInsulin/IGFInsulin-stimulated phosphorylationThreonine phosphorylationStimulates PhosphorylationPhosphorylation sitesJun kinaseTyrosine phosphorylationKinase pathwaySer307PhosphorylationCultured cellsDistinct pathwaysHeterologous inhibitionPolyclonal antibodiesPreadipocytesPathwayAdipocytesCells
2000
The c-Jun NH2-terminal Kinase Promotes Insulin Resistance during Association with Insulin Receptor Substrate-1 and Phosphorylation of Ser307 *
Davis R, Aguirre V, Uchida T, Yenush L, White M. The c-Jun NH2-terminal Kinase Promotes Insulin Resistance during Association with Insulin Receptor Substrate-1 and Phosphorylation of Ser307 *. Journal Of Biological Chemistry 2000, 275: 9047-9054. PMID: 10722755, DOI: 10.1074/jbc.275.12.9047.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnisomycinCHO CellsCricetinaeHumansInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceJNK Mitogen-Activated Protein KinasesMiceMitogen-Activated Protein KinasesMolecular Sequence DataPhosphoproteinsPhosphorylationProtein BindingReceptor, InsulinRecombinant ProteinsSerineSignal TransductionTumor Necrosis Factor-alphaConceptsInsulin-stimulated tyrosine phosphorylationIRS-1Serine 307Tyrosine phosphorylationInsulin receptor substrate-1IRS-1 functionSignal transduction cascadePhosphorylation of Ser307Receptor substrate-1Chinese hamster ovary cellsIRS proteinsActivity of JNKJNK associatesPhosphorylation sitesHamster ovary cellsTransduction cascadeSerine phosphorylationTerminal kinaseSubstrate-1PhosphorylationStrong activatorPromotes Insulin ResistanceJNK phosphorylationOvary cellsJNK
1996
Tumor Necrosis Factor (TNF)-α Inhibits Insulin Signaling through Stimulation of the p55 TNF Receptor and Activation of Sphingomyelinase*
Peraldi P, Hotamisligil G, Buurman W, White M, Spiegelman B. Tumor Necrosis Factor (TNF)-α Inhibits Insulin Signaling through Stimulation of the p55 TNF Receptor and Activation of Sphingomyelinase*. Journal Of Biological Chemistry 1996, 271: 13018-13022. PMID: 8662983, DOI: 10.1074/jbc.271.22.13018.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdipocytesAnimalsAntigens, CDCell LineCeramidesEnzyme ActivationHumansInsulinInsulin Receptor Substrate ProteinsMicePhosphoproteinsPhosphorylationReceptor, InsulinReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISignal TransductionSphingomyelin PhosphodiesteraseTumor Necrosis Factor-alphaTyrosineConceptsInsulin receptor substrate-1Myeloid 32D cellsInsulin receptorP55 TNF receptorP75 TNF receptorTyrosine phosphorylationInhibits InsulinIRS-2Insulin-dependent tyrosine phosphorylationTNF receptorIRS-1 tyrosine phosphorylationTNF-alphaIR tyrosine kinaseReceptor substrate-1Tyrosine kinase activityNecrosis factorActivation of sphingomyelinaseSerine phosphorylationBiological functionsKinase activitySubstrate-1Tyrosine kinaseExogenous sphingomyelinaseMurine TNF-alphaTumor necrosis factor