2013
Serine Phosphorylation Sites on IRS2 Activated by Angiotensin II and Protein Kinase C To Induce Selective Insulin Resistance in Endothelial Cells
Park K, Li Q, Rask-Madsen C, Mima A, Mizutani K, Winnay J, Maeda Y, D'Aquino K, White M, Feener E, King G. Serine Phosphorylation Sites on IRS2 Activated by Angiotensin II and Protein Kinase C To Induce Selective Insulin Resistance in Endothelial Cells. Molecular And Cellular Biology 2013, 33: 3227-3241. PMID: 23775122, PMCID: PMC3753901, DOI: 10.1128/mcb.00506-13.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAnimalsCattleCell LineEndothelial CellsEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceMaleMiceMice, TransgenicPhosphatidylinositol 3-KinasesPhosphorylationProtein Kinase CProtein Kinase C betaRatsRats, ZuckerSerineTetradecanoylphorbol AcetateThreonineTyrosine
2011
Inhibition of Insulin Signaling in Endothelial Cells by Protein Kinase C-induced Phosphorylation of p85 Subunit of Phosphatidylinositol 3-Kinase (PI3K)*
Maeno Y, Li Q, Park K, Rask-Madsen C, Gao B, Matsumoto M, Liu Y, Wu I, White M, Feener E, King G. Inhibition of Insulin Signaling in Endothelial Cells by Protein Kinase C-induced Phosphorylation of p85 Subunit of Phosphatidylinositol 3-Kinase (PI3K)*. Journal Of Biological Chemistry 2011, 287: 4518-4530. PMID: 22158866, PMCID: PMC3281670, DOI: 10.1074/jbc.m111.286591.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCells, CulturedClass Ia Phosphatidylinositol 3-KinaseEndothelial CellsEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMetabolic DiseasesNitric Oxide Synthase Type IIIPhosphorylationProtein Kinase CProto-Oncogene Proteins c-aktSignal TransductionVascular Endothelial Growth Factor AConceptsP85/PI3KPI3KPKC activationInsulin receptor substrateProtein kinase C activationEndothelial nitric oxide synthaseProtein kinase CAkt/endothelial nitric oxide synthaseKinase C activationPI3K/Akt pathwayP85 subunitDeletion mutantsGeneral activatorTyrosine phosphorylationReceptor substrateEndothelial cellsInsulin signalingInsulin activationKinase CAkt pathwayPhosphorylationC activationThr-86SignalingIRS1
2009
Metformin and Insulin Meet in a Most Atypical Way
White M. Metformin and Insulin Meet in a Most Atypical Way. Cell Metabolism 2009, 9: 485-487. PMID: 19490902, DOI: 10.1016/j.cmet.2009.05.007.Peer-Reviewed Original Research
2003
Role of Insulin Receptor Substrates and Protein Kinase C-ζ in Vascular Permeability Factor/Vascular Endothelial Growth Factor Expression in Pancreatic Cancer Cells*
Neid M, Datta K, Stephan S, Khanna I, Pal S, Shaw L, White M, Mukhopadhyay D. Role of Insulin Receptor Substrates and Protein Kinase C-ζ in Vascular Permeability Factor/Vascular Endothelial Growth Factor Expression in Pancreatic Cancer Cells*. Journal Of Biological Chemistry 2003, 279: 3941-3948. PMID: 14604996, DOI: 10.1074/jbc.m303975200.Peer-Reviewed Original ResearchMeSH KeywordsAdenocarcinomaBase SequenceCell Line, TumorDNA, NeoplasmFeedbackGene Expression Regulation, NeoplasticHumansInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsNeovascularization, PathologicPancreatic NeoplasmsPhosphoproteinsProtein Kinase CSignal TransductionSp1 Transcription FactorVascular Endothelial Growth Factor AConceptsVPF/VEGF expressionIRS proteinsIRS-2Negative feedback loopVEGF transcriptionPKC-zetaVascular Permeability Factor/Vascular Endothelial Growth Factor ExpressionPancreatic cancer cellsProtein kinase C zetaCancer cellsInsulin receptor substrate-1IGF-1RReceptor substrate-1Insulin receptor substrateIRS-2 proteinProtein kinase CMajor downstream moleculesInsulin-like growth factor receptorRenal cancer cellsVascular permeability factor/vascular endothelial growth factorIGF-1R signalingGrowth factorRas pathwayGrowth factor receptorC zetaMolecular Mechanisms of Insulin Resistance in IRS-2-Deficient Hepatocytes
Valverde A, Burks D, Fabregat I, Fisher T, Carretero J, White M, Benito M. Molecular Mechanisms of Insulin Resistance in IRS-2-Deficient Hepatocytes. Diabetes 2003, 52: 2239-2248. PMID: 12941762, DOI: 10.2337/diabetes.52.9.2239.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsAnimals, NewbornAntigens, Polyomavirus TransformingCell Line, TransformedFemaleForkhead Box Protein O1Forkhead Transcription FactorsGluconeogenesisGlucose-6-PhosphataseGlycogen SynthaseGlycogen Synthase Kinase 3HepatocytesHypoglycemic AgentsInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceIntracellular Signaling Peptides and ProteinsIsoenzymesMaleMiceMice, Mutant StrainsPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphoenolpyruvate Carboxykinase (GTP)PhosphoproteinsPregnancyProtein Kinase CProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRetroviridaeSignal TransductionTranscription FactorsConceptsGluconeogenic gene expressionIRS-2Gene expressionPrimary hepatocytesAtypical protein kinase CIRS-1-associated phosphatidylinositolIRS-1 tyrosine phosphorylationInsulin-induced phosphatidylinositolTranslocation of phosphatidylinositolInsulin receptor substrateGlycogen synthase kinaseProtein kinase CActivation of AktDownstream phosphatidylinositolTyrosine phosphorylationPlasma membraneReceptor substrateGlycogen synthase activityMolecular mechanismsSynthase kinaseInsulin stimulationKinase CHepatocyte cell linePhosphatidylinositolFunctional insulinEssential role of protein kinase Cζ in the impairment of insulin‐induced glucose transport in IRS‐2‐deficient brown adipocytes
Arribas M, Valverde A, Burks D, Klein J, Farese R, White M, Benito M. Essential role of protein kinase Cζ in the impairment of insulin‐induced glucose transport in IRS‐2‐deficient brown adipocytes. FEBS Letters 2003, 536: 161-166. PMID: 12586357, DOI: 10.1016/s0014-5793(03)00049-8.Peer-Reviewed Original ResearchConceptsGLUT4 translocationIRS-2/PIBrown adipocytesInsulin-induced glucose transportProtein kinase C zetaIRS-2-associated phosphatidylinositolKinase-inactive mutantGlucose uptakeWild-type cellsProtein kinase CζEssential roleInsulin receptor substrate-2-deficient (IRS2(-/-)) miceC zetaPKC-zetaMolecular mechanismsIRS-2Impaired glucose uptakeGlucose transportAdipocytesTranslocationCellsUptakeMutantsPhosphatidylinositolCζ
1999
Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade.
Griffin ME, Marcucci MJ, Cline GW, Bell K, Barucci N, Lee D, Goodyear LJ, Kraegen EW, White MF, Shulman GI. Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade. Diabetes 1999, 48: 1270-1274. PMID: 10342815, DOI: 10.2337/diabetes.48.6.1270.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDeoxyglucoseEnzyme ActivationFatty Acids, NonesterifiedInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceIsoenzymesMagnetic Resonance SpectroscopyMaleMuscle, SkeletalPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein Kinase CProtein Kinase C-thetaRatsRats, Sprague-DawleySignal TransductionTyrosineZinc FingersConceptsProtein kinase C thetaGlucose transport activityInsulin resistanceMuscle glycogen synthesisFree fatty acidsC thetaInsulin-stimulated insulin receptor substrateInsulin-stimulated IRS-1 tyrosine phosphorylationTransport activityIRS-1 tyrosine phosphorylationReduced glucose transport activityInsulin-stimulated muscle glucose metabolismFatty acid-induced insulin resistanceEndothelin-1 modulates insulin signaling through phosphatidylinositol 3-kinase pathway in vascular smooth muscle cells.
Jiang Z, Zhou Q, Chatterjee A, Feener E, Myers M, White M, King G. Endothelin-1 modulates insulin signaling through phosphatidylinositol 3-kinase pathway in vascular smooth muscle cells. Diabetes 1999, 48: 1120-1130. PMID: 10331419, DOI: 10.2337/diabetes.48.5.1120.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEndothelin Receptor AntagonistsEndothelin-1Enzyme InhibitorsGTP-Binding ProteinsHumansInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsMaleMuscle, Smooth, VascularPeptides, CyclicPertussis ToxinPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsPhosphoserineProtein Kinase CRatsRats, ZuckerSignal TransductionTetradecanoylphorbol AcetateVirulence Factors, BordetellaConceptsInsulin-stimulated phosphatidylinositolProtein kinase CIRS-2P85 subunitSerine phosphorylationSmooth muscle cellsInsulin receptor beta subunitInsulin-induced phosphatidylinositolInsulin receptor substrateReceptor beta subunitMuscle cellsTreatment of cellsArterial smooth muscle cellsReceptor substratePretreatment of cellsVascular smooth muscle cellsBeta subunitKinase CPhosphatidylinositolIndependent pathwaysSpecific inhibitorET-1SubunitsPhosphorylationPathway
1997
Requirement of Protein Kinase Cζ for Stimulation of Protein Synthesis by Insulin
Mendez R, Kollmorgen G, White M, Rhoads R. Requirement of Protein Kinase Cζ for Stimulation of Protein Synthesis by Insulin. Molecular And Cellular Biology 1997, 17: 5184-5192. PMID: 9271396, PMCID: PMC232369, DOI: 10.1128/mcb.17.9.5184.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCalcium-Calmodulin-Dependent Protein KinasesEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMiceOligonucleotides, AntisensePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)Protein BiosynthesisProtein Kinase CProtein Serine-Threonine KinasesProto-Oncogene Proteins c-mycRibosomal Protein S6 KinasesConceptsGeneral protein synthesisPKC-zetaCell cycle progressionProtein synthesisIRS-1Insulin receptorCycle progressionGuanine nucleotide exchange factorsNucleotide exchange factorsInsulin-stimulated protein synthesisProto-oncogene AktTarget of rapamycinMitogen-activated protein kinaseInsulin-stimulated activationPKC zeta activationProtein kinase CζGrowth-regulating proteinsActive PKC-zetaPrevention of apoptosisExchange factorPhosphorylated substratesS6 kinaseProtein kinaseGab-1Ectopic expression