2022
BRD4 inhibitor suppresses melanoma metastasis via the SPINK6/EGFR-EphA2 pathway
Hu R, Li Y, Guo Y, Li X, Du S, Liao M, Hou H, Sun H, Zhao S, Su J, Chen X, Yin M. BRD4 inhibitor suppresses melanoma metastasis via the SPINK6/EGFR-EphA2 pathway. Pharmacological Research 2022, 187: 106609. PMID: 36516883, DOI: 10.1016/j.phrs.2022.106609.Peer-Reviewed Original ResearchRegulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis
An S, Anneken A, Xi Z, Choi C, Schlessinger J, Toomre D. Regulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2208947119. PMID: 36417441, PMCID: PMC9860279, DOI: 10.1073/pnas.2208947119.Peer-Reviewed Original ResearchConceptsPI-3K/Akt pathwayAkt pathwayAkt activationDocking protein Gab1EGF-stimulated activationEpithelial cellsLive-cell imagingPhosphoinositide-3 kinaseCell survival pathwaysExocyst complexExocyst functionSmall molecule inhibitorsVesicle tethersExocytic fusionProtein Gab1EGF stimulationExocystSurvival pathwaysExocytosisInhibitors resultsPathwayImportant pathwayEGFR inhibitionMinute time scaleVesicles
2020
Differential effects of the Akt pathway on the internalization of Klebsiella by lung epithelium and macrophages
Chang D, Feng J, Liu H, Liu W, Sharma L, Dela Cruz CS. Differential effects of the Akt pathway on the internalization of Klebsiella by lung epithelium and macrophages. Innate Immunity 2020, 26: 618-626. PMID: 32762278, PMCID: PMC7556185, DOI: 10.1177/1753425920942582.Peer-Reviewed Original ResearchConceptsAkt pathwayEpithelial cellsCell typesKey cellular pathwaysLung epitheliumActivation of AktPhagocytic abilityMultiple cell typesAkt inhibitor MK2206Particular bacterial infectionsCellular pathwaysLung epithelial cellsMacrophage cell lineHost cellsBacterial infectionsRespiratory epithelial cellsCell proliferationType of infectionCell linesPathwayHost defenseDifferential rolesAktSC-79Cells
2019
TIGIT signaling restores suppressor function of Th1 Tregs
Lucca LE, Axisa PP, Singer ER, Nolan NM, Dominguez-Villar M, Hafler DA. TIGIT signaling restores suppressor function of Th1 Tregs. JCI Insight 2019, 4: e124427. PMID: 30728325, PMCID: PMC6413794, DOI: 10.1172/jci.insight.124427.Peer-Reviewed Original ResearchIL-12Multiple sclerosisHuman autoimmune disordersT-bet expressionProinflammatory cytokine secretionProduction of IFNType 1 diabetesReduced suppressor activitySuppressor functionRepression of AktFOXO1 nuclear localizationTh1 programTIGIT pathwayCoinhibitory receptorsImmunomodulatory therapyTh17 responsesAutoimmune disordersAutoimmune diseasesSuppressor defectCytokine secretionTregsTIGITProtective effectFunctional inhibitionAkt pathway
2018
Regulation and Role of Chitotriosidase during Lung Infection with Klebsiella pneumoniae
Sharma L, Amick AK, Vasudevan S, Lee SW, Marion CR, Liu W, Brady V, Losier A, Bermejo SD, Britto CJ, Lee CG, Elias JA, Dela Cruz CS. Regulation and Role of Chitotriosidase during Lung Infection with Klebsiella pneumoniae. The Journal Of Immunology 2018, 201: 615-626. PMID: 29891554, PMCID: PMC6291403, DOI: 10.4049/jimmunol.1701782.Peer-Reviewed Original ResearchConceptsLung infectionMouse modelRole of chitotriosidaseBronchoalveolar lavage fluidNumber of neutrophilsSimilar inflammatory responseRole of CHIT1Antibiotic therapyImproved survivalInflammatory changesLavage fluidInflammatory responseNeutrophil proteasesBacterial disseminationTrue chitinasesInfectionBeneficial effectsDetrimental roleAkt pathwayKlebsiella pneumoniaeAkt inhibitorCHIT1Chitinase-like proteinsMiceAkt activation
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
2014
Genetic modifiers of EGFR dependence in non-small cell lung cancer
Sharifnia T, Rusu V, Piccioni F, Bagul M, Imielinski M, Cherniack AD, Pedamallu CS, Wong B, Wilson FH, Garraway LA, Altshuler D, Golub TR, Root DE, Subramanian A, Meyerson M. Genetic modifiers of EGFR dependence in non-small cell lung cancer. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 18661-18666. PMID: 25512530, PMCID: PMC4284598, DOI: 10.1073/pnas.1412228112.Peer-Reviewed Original ResearchMeSH KeywordsCarcinoma, Non-Small-Cell LungCell Line, TumorErbB ReceptorsGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticHumansLung NeoplasmsMAP Kinase Signaling SystemMembrane GlycoproteinsProtein-Tyrosine KinasesProto-Oncogene Proteins c-mosProto-Oncogene Proteins c-rafReceptor Protein-Tyrosine KinasesReceptor, Fibroblast Growth Factor, Type 1Receptor, Fibroblast Growth Factor, Type 2Receptor, trkAReceptor, trkBConceptsEpidermal growth factor receptorEGFR dependenceMEK-ERKUnbiased gene expression profilingGenetic modifiersEGFR-independent activationKinase-related genesGene expression profilingEGFR-mutant NSCLC cellsGrowth factor receptorGenetic basisKinase geneEGFR activityGenesPI3K-AktAkt pathwayPC9 cellsPI3K-mTORFactor receptorKinaseNSCLC cellsKinase inhibitorsCombined inhibitionMutationsCellsNAP Reduces Murine Microvascular Endothelial Cells Proliferation Induced by Hyperglycemia
D’Amico A, Scuderi S, Maugeri G, Cavallaro S, Drago F, D’Agata V. NAP Reduces Murine Microvascular Endothelial Cells Proliferation Induced by Hyperglycemia. Journal Of Molecular Neuroscience 2014, 54: 405-413. PMID: 24874579, DOI: 10.1007/s12031-014-0335-2.Peer-Reviewed Original ResearchConceptsProtein kinase/extracellular signal-regulated protein kinaseExtracellular signal-regulated protein kinaseMitogen-activated protein kinase/extracellular signal-regulated protein kinaseSignal-regulated protein kinaseKinase/Akt pathwayEndothelial cell proliferationPhosphatidylinositol-3-kinase/Akt pathwayCell proliferationProtein expression analysisProtein kinaseExpression analysisBiological roleAkt pathwayPhosphorylation levelsTime-dependent mannerHigh glucoseMurine microvascular endothelial cellsMicrovascular endothelial cell proliferationMicrovascular endothelial cellsEndothelial cellsProliferationMTT assayCellsEpigenetic regulation of OPA1 sensitizes hepatocellular carcinoma to sorafenib‐induced apoptosis (59.1)
Puszyk W, Dong H, Zhao F, Shisgal P, Cabrera R, Neslon D, Liu C. Epigenetic regulation of OPA1 sensitizes hepatocellular carcinoma to sorafenib‐induced apoptosis (59.1). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.59.1.Peer-Reviewed Original ResearchDNA methylationHepatocellular carcinomaEpigenetic regulationProtein OPA1HCC cellsMitochondrial fragmentationGene promoterC releaseEpigenetic analysisXenograft tumor growthEpigenetic markersSorafenib-induced apoptosisAkt pathwayOPA1HCC xenograft tumor growthHepatocellular carcinoma cellsNovel therapeutic targetExpression levelsTumorigenesis of HCCIdentification of patientsPathogenesis of HCCOPA1 knockdownApoptosisPrimary hepatocytesSensitivity of HCCFGF2 and Insulin Signaling Converge to Regulate Cyclin D Expression in Multipotent Neural Stem Cells
Adepoju A, Micali N, Ogawa K, Hoeppner DJ, McKay RD. FGF2 and Insulin Signaling Converge to Regulate Cyclin D Expression in Multipotent Neural Stem Cells. Stem Cells 2014, 32: 770-778. PMID: 24155149, DOI: 10.1002/stem.1575.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell ProliferationCyclin DDNAFemaleFibroblast Growth Factor 2InsulinIntracellular SpaceMiceMice, Inbred C57BLModels, BiologicalMultipotent Stem CellsNeural Stem CellsProtein BiosynthesisProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junSignal TransductionTranscription, GeneticConceptsNeural stem cellsMultipotent neural stem cellsStem cellsPost-transcriptional levelPI3K/Akt pathwayTyrosine kinase receptorsPhosphorylation of ERK1/2Cell statesInsulin signalProliferation controlCell lineagesFibroblast growth factorBasic fibroblast growth factorCyclin D expressionMultipotent cellsC-JunD mRNA levelsKinase receptorsNeural precursorsAkt pathwayCell expansionMultipotent natureCentral nervous systemDisease mechanismsC-fos
2012
Cyclooxygenase‐2 and Akt mediate multiple growth‐factor‐induced epithelial‐mesenchymal transition in human hepatocellular carcinoma
Ogunwobi O, Wang T, Zhang L, Liu C. Cyclooxygenase‐2 and Akt mediate multiple growth‐factor‐induced epithelial‐mesenchymal transition in human hepatocellular carcinoma. Journal Of Gastroenterology And Hepatology 2012, 27: 566-578. PMID: 22097969, PMCID: PMC3288221, DOI: 10.1111/j.1440-1746.2011.06980.x.Peer-Reviewed Original ResearchMeSH KeywordsAlbuminsalpha 1-AntitrypsinAnimalsCadherinsCarcinoma, HepatocellularCell MovementCell TransplantationCollagen Type ICyclooxygenase 2DinoprostoneEpidermal Growth FactorEpithelial-Mesenchymal TransitionFibroblast Growth Factor 2FibronectinsGene ExpressionHepatocyte Growth FactorHumansMiceOncogene Protein v-aktRNA, Small InterferingSignal TransductionTransforming Growth Factor beta1Tumor Cells, CulturedVimentinConceptsEpithelial-mesenchymal transitionCyclooxygenase-2Hepatocellular carcinomaBasic fibroblast growth factorGrowth factorProstaglandin E2Metastatic hepatocellular carcinomaProgression of HCCEffective therapeutic strategyExpression of vimentinHepatocyte growth factorGrowth factor βHuman hepatocellular carcinomaFibroblast growth factorAssociated hepatitisChemopreventive strategiesEpidermal growth factorMultiple growth factorsTherapeutic strategiesMesenchymal changesSignificant mortalityAkt pathwayMolecular targetingCancer invasionAkt
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-86SignalingIRS1In Vivo Identification of Tumor- Suppressive PTEN ceRNAs in an Oncogenic BRAF-Induced Mouse Model of Melanoma
Karreth FA, Tay Y, Perna D, Ala U, Tan SM, Rust AG, DeNicola G, Webster KA, Weiss D, Perez-Mancera PA, Krauthammer M, Halaban R, Provero P, Adams DJ, Tuveson DA, Pandolfi PP. In Vivo Identification of Tumor- Suppressive PTEN ceRNAs in an Oncogenic BRAF-Induced Mouse Model of Melanoma. Cell 2011, 147: 382-395. PMID: 22000016, PMCID: PMC3236086, DOI: 10.1016/j.cell.2011.09.032.Peer-Reviewed Original ResearchConceptsMicroRNA recognition elementsLow PTEN levelsPTEN protein levelsZEB2 expressionBeauty insertional mutagenesisMicroRNA decoysPI3K/Akt pathwayLoss of PTENCeRNA activityInsertional mutagenesisZeb2 transcriptTumor suppressorCell transformationCeRNAsPTEN levelsAkt pathwayFunctional roleMRNA transcriptsSignificant enrichmentZEB2 mRNAProtein levelsMouse modelCeRNATranscriptsPTEN
2010
Dlxin-1, a MAGE family protein, induces accelerated neurite outgrowth and cell survival by enhanced and early activation of MEK and Akt signalling pathways in PC12 cells
Reddy E, Chettiar S, Kaur N, Shepal V, Shiras A. Dlxin-1, a MAGE family protein, induces accelerated neurite outgrowth and cell survival by enhanced and early activation of MEK and Akt signalling pathways in PC12 cells. Experimental Cell Research 2010, 316: 2220-2236. PMID: 20595047, DOI: 10.1016/j.yexcr.2010.05.030.Peer-Reviewed Original ResearchConceptsDlxin-1MAGE homology domainCell survivalPC12 cellsPresence of NGFNeuronal differentiationDiverse cellular functionsMAGE family proteinsCell cycle progressionTranscriptional regulationHomology domainCellular functionsFamily proteinsNeuronal survivalDevelopmental apoptosisEnhanced neuritogenesisCycle progressionSignaling pathwaysMEK pathwayPharmacological inhibitorsCell deathAkt pathwayUnique regionAmino acidsEarly activation
2009
Phase I evaluation of lapatinib and everolimus in patients with advanced malignancies: Southwest Oncology Group trial S0528
Hoban C, Hoering A, Synold T, Chung V, Gandara D, Schott A, Kingsbury L, Lew D, LoRusso P, Gadgeel S. Phase I evaluation of lapatinib and everolimus in patients with advanced malignancies: Southwest Oncology Group trial S0528. Journal Of Clinical Oncology 2009, 27: 3553-3553. DOI: 10.1200/jco.2009.27.15_suppl.3553.Peer-Reviewed Original ResearchLapatinib 1250Oral inhibitorCombination of lapatinibMedian age 63Phase I evaluationPre-clinical studiesPI3/Akt pathwayAnti-tumor activityEligible ptsStable diseaseAdvanced malignanciesAdvanced tumorsLung cancerCommon tumorsEffective therapyPharmacokinetic analysisI evaluationEverolimusAge 63Drug pharmacokineticsPharmacokineticsMTDPhase ILapatinibAkt pathwayAcidic Mammalian Chitinase Regulates Epithelial Cell Apoptosis via a Chitinolytic-Independent Mechanism
Hartl D, He CH, Koller B, Da Silva CA, Kobayashi Y, Lee CG, Flavell RA, Elias JA. Acidic Mammalian Chitinase Regulates Epithelial Cell Apoptosis via a Chitinolytic-Independent Mechanism. The Journal Of Immunology 2009, 182: 5098-5106. PMID: 19342690, PMCID: PMC2666938, DOI: 10.4049/jimmunol.0803446.Peer-Reviewed Original ResearchConceptsAcidic mammalian chitinaseTh2-mediated diseasesEpithelial cellsMammalian chitinasePI3K/Akt pathwayPulmonary epithelial cellsEpithelial cell apoptosisApoptosis-inhibiting effectsComparable cytoprotectionGrowth factor withdrawal-induced apoptosisChitinolytic activityEffector responsesParacrine mannerFas ligand-induced apoptosisAntiparasite responsesGrowth factor withdrawalWithdrawal-induced apoptosisLigand-induced apoptosisFas ligandAkt pathwayCell apoptosisAkt phosphorylationAMCaseBiologic propertiesCytoprotection
2008
Dual roles of IL‐15 in maintaining IL‐7 receptor alpha low CCR7− memory CD8+ T cells in humans via recovering the PI3K/AKT pathway
Kang I, Kim H, Hwang K. Dual roles of IL‐15 in maintaining IL‐7 receptor alpha low CCR7− memory CD8+ T cells in humans via recovering the PI3K/AKT pathway. The FASEB Journal 2008, 22: 846.18-846.18. DOI: 10.1096/fasebj.22.1_supplement.846.18.Peer-Reviewed Original ResearchPI3K/Akt pathwayMemory CD8Lower CCR7IL-15T cellsAkt pathwayIL-7 receptor alphaMemory T cell survivalIL-7 receptor alpha chainHuman peripheral bloodT cell survivalReceptor alpha chainHigher CCR7Peripheral CD8T cell receptor triggeringPeripheral bloodReceptor beta chainT-betCD8IL-7CCR7Effector functionsReceptor alphaEnhanced gene expressionProliferative function
2007
Dual Roles of IL-15 in Maintaining IL-7RαlowCCR7− Memory CD8+ T Cells in Humans via Recovering the Phosphatidylinositol 3-Kinase/AKT Pathway
Kim HR, Hwang KA, Kang I. Dual Roles of IL-15 in Maintaining IL-7RαlowCCR7− Memory CD8+ T Cells in Humans via Recovering the Phosphatidylinositol 3-Kinase/AKT Pathway. The Journal Of Immunology 2007, 179: 6734-6740. PMID: 17982063, DOI: 10.4049/jimmunol.179.10.6734.Peer-Reviewed Original ResearchMeSH KeywordsCD8-Positive T-LymphocytesCell ProliferationCell SurvivalEnzyme ActivationGene Expression RegulationHumansImmunologic MemoryInfectionsInterleukin-15Interleukin-2 Receptor beta SubunitInterleukin-7NeoplasmsPerforinPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReceptors, Antigen, T-CellReceptors, CCR7Receptors, Interleukin-17Signal TransductionConceptsIL-15T cellsPI3K/Akt pathwayAkt pathwayIL-7Memory T cell survivalProliferation of ILIL-15 signalingHuman peripheral bloodT cell survivalEffector cytokinesMemory CD8Peripheral bloodEffector functionsIL-7REnhanced gene expressionProliferative functionIndependent mechanismsILTCR triggeringCell survivalSuch cellsSurvivalTranscriptional factorsDual roleEnzastaurin, a Protein Kinase Cβ–Selective Inhibitor, and Its Potential Application as an Anticancer Agent in Lung Cancer
Herbst RS, Oh Y, Wagle A, Lahn M. Enzastaurin, a Protein Kinase Cβ–Selective Inhibitor, and Its Potential Application as an Anticancer Agent in Lung Cancer. Clinical Cancer Research 2007, 13: 4641s-4646s. PMID: 17671157, DOI: 10.1158/1078-0432.ccr-07-0538.Peer-Reviewed Original ResearchConceptsSerine/threonine kinase inhibitorLung cancerOral serine/threonine kinase inhibitorProtein kinase CFavorable safety profileCurrent phase IKinase CTumor cell apoptosisAkt pathwayClinical findingsSafety profilePKC inhibitorTumor-induced angiogenesisPreclinical experienceCell apoptosisEnzastaurinKinase inhibitorsPhase ICancerIGF‐1 stimulates de novo fatty acid biosynthesis by Schwann cells during myelination
Liang G, Cline GW, Macica CM. IGF‐1 stimulates de novo fatty acid biosynthesis by Schwann cells during myelination. Glia 2007, 55: 632-641. PMID: 17299765, DOI: 10.1002/glia.20496.Peer-Reviewed Original ResearchMeSH KeywordsAcetatesAnimalsCell CommunicationCells, CulturedCoculture TechniquesFatty AcidsGanglia, SpinalInsulin-Like Growth Factor IMembrane LipidsMyelin SheathNeurons, AfferentPeripheral Nervous SystemPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktRatsRats, Sprague-DawleySchwann CellsSignal TransductionConceptsInsulin-like growth factor-1Fatty acid synthesizing enzymesSynthesizing enzymesIGF-1 treatmentMyelin membrane formationGrowth factor-1PI3K/Akt pathwaySchwann cell differentiationPI3K/AktWestern blot analysisSciatic nerveIGF-1Schwann cellsElectrospray mass spectroscopy analysisCell coculturesMyelin-specific proteinsGrowth factorAkt pathwayMyelinationFactor 1Fatty acid synthesisCocultureBlot analysisEarly eventsMyelin membrane
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