2016
G protein-coupled receptors (GPCRs) That Signal via Protein Kinase A (PKA) Cross-talk at Insulin Receptor Substrate 1 (IRS1) to Activate the phosphatidylinositol 3-kinase (PI3K)/AKT Pathway*
Law N, White M, Hunzicker-Dunn M. G protein-coupled receptors (GPCRs) That Signal via Protein Kinase A (PKA) Cross-talk at Insulin Receptor Substrate 1 (IRS1) to Activate the phosphatidylinositol 3-kinase (PI3K)/AKT Pathway*. Journal Of Biological Chemistry 2016, 291: 27160-27169. PMID: 27856640, PMCID: PMC5207145, DOI: 10.1074/jbc.m116.763235.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBreast NeoplasmsCells, CulturedCyclic AMP-Dependent Protein KinasesFemaleGranulosa CellsHumansInsulin Receptor Substrate ProteinsOvarian FolliclePhosphatidylinositol 3-KinasePhosphorylationProto-Oncogene Proteins c-aktRatsRats, Sprague-DawleyReceptors, G-Protein-CoupledSignal TransductionThyroid NeoplasmsConceptsG protein-coupled receptorsInsulin receptor substrate-1PI3K/Akt cascadeProtein-coupled receptorsAkt cascadeSer/ThrReceptor substrate-1PI3K/Akt activationInsulin-like growth factor-1PI3K/Akt pathwayGranulosa cellsConserved mechanismPI3K/AktCellular functionsProtein kinaseSer residuesSubstrate-1Myosin phosphataseSubunit 1Akt activationCell survivalAutocrine/paracrine mannerViral oncoproteinsAkt pathwayPreantral granulosa cells
2012
Pulsatile Portal Vein Insulin Delivery Enhances Hepatic Insulin Action and Signaling
Matveyenko A, Liuwantara D, Gurlo T, Kirakossian D, Man C, Cobelli C, White M, Copps K, Volpi E, Fujita S, Butler P. Pulsatile Portal Vein Insulin Delivery Enhances Hepatic Insulin Action and Signaling. Diabetes 2012, 61: 2269-2279. PMID: 22688333, PMCID: PMC3425431, DOI: 10.2337/db11-1462.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlood GlucoseDiabetes Mellitus, ExperimentalDiabetes Mellitus, Type 2DogsForkhead Transcription FactorsGlucokinaseInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceInsulin SecretionLiverMaleNerve Tissue ProteinsPortal VeinProto-Oncogene Proteins c-aktRatsRats, Sprague-DawleySignal TransductionConceptsPulsatile insulin secretionHepatic insulin actionInsulin secretionHepatic insulinPortal veinInsulin deliveryPulsatile patternInsulin actionDiscrete insulin secretory burstsHepatic insulin receptor substrateImpaired activationType 2 diabetes mellitusSequential liver biopsiesIntraportal insulin infusionInsulin secretory burstsHepatic insulin resistanceHepatic portal veinExpression of glucokinaseGlycemic controlDiabetes mellitusLiver biopsyInsulin resistanceInsulin infusionSecretory burstsRat model
2004
Insulin resistance in thermally-injured rats is associated with post-receptor alterations in skeletal muscle, liver and adipose tissue.
Carter E, Burks D, Fischman A, White M, Tompkins R. Insulin resistance in thermally-injured rats is associated with post-receptor alterations in skeletal muscle, liver and adipose tissue. International Journal Of Molecular Medicine 2004, 14: 653-8. PMID: 15375597, DOI: 10.3892/ijmm.14.4.653.Peer-Reviewed Original ResearchConceptsUrinary C-peptide excretionC-peptide excretionPost-receptor alterationsInsulin resistanceInsulin receptor bindingSkeletal muscleInsulin infusionBurn injuryAdipose tissueFull-thickness scald injuryGlucose productionSham-treated control animalsReceptor bindingHepatic glucose productionIRS-1 expressionWestern blot methodBinding of insulinAbsence of changesScald injuryBolus injectionRat modelPossible molecular mechanismsControl animalsInjuryThermal injury
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 resistance
1997
The 60 kDa Insulin Receptor Substrate Functions Like an IRS Protein (pp60IRS3) in Adipose Cells †
Smith-Hall J, Pons S, Patti M, Burks D, Yenush L, Sun X, Kahn C, White M. The 60 kDa Insulin Receptor Substrate Functions Like an IRS Protein (pp60IRS3) in Adipose Cells †. Biochemistry 1997, 36: 8304-8310. PMID: 9204876, DOI: 10.1021/bi9630974.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAnimalsImmunosorbent TechniquesInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsMaleMiceMolecular WeightPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineRatsRats, Sprague-DawleyReceptor, InsulinTestisConceptsIRS-1IRS proteinsInsulin receptor substrates functionIRS-2IRS protein familyTyrosine phosphorylated proteinsInsulin receptor signalsInsulin receptor substratePTB domainNPXY motifSH2 domainProtein familyPhosphorylated proteinsReceptor substrateInsulin stimulationReceptor signalsSubstrate functionP85New memberProteinRat adipocytesAdipose cellsAlternate pathwayFunctional characteristicsSynthetic peptides