2025
Activity-Dependent Effects of ERK1/2 on Hepatic Ischemia-Reperfusion Injury
Kim J, Hong S, Lee A, Kumar S, Suchi M, Park J. Activity-Dependent Effects of ERK1/2 on Hepatic Ischemia-Reperfusion Injury. Transplantation Proceedings 2025 PMID: 40796392, DOI: 10.1016/j.transproceed.2025.07.005.Peer-Reviewed Original ResearchHepatic ischemia-reperfusion injuryIschemia-reperfusion injuryERK1/2 activationLiver injuryActivity-dependent effectsResponse to IRIEnd-stage liver diseaseDose of trametinibAnalysis of cell death pathwaysEffect of ERK1/2Extracellular signal-regulated kinaseExpression of ferroptosis markersSignal-regulated kinaseSerum markersModulation of ERK1/2 activityLiver transplantationMEK1/2 inhibitorReperfusion timeMolecular analysisRat modelIschemia-reperfusionLiver ischemiaCell death pathwaysHistological assessmentLiver disease
2021
Inflammatory conversion of quiescent osteoblasts by metastatic breast cancer cells through pERK1/2 aggravates cancer-induced bone destruction
Back J, Nguyen MN, Li L, Lee S, Lee I, Chen F, Gillinov L, Chung YH, Alder KD, Kwon HK, Yu KE, Dussik CM, Hao Z, Flores MJ, Kim Y, Ibe IK, Munger AM, Seo SW, Lee FY. Inflammatory conversion of quiescent osteoblasts by metastatic breast cancer cells through pERK1/2 aggravates cancer-induced bone destruction. Bone Research 2021, 9: 43. PMID: 34588427, PMCID: PMC8481290, DOI: 10.1038/s41413-021-00158-w.Peer-Reviewed Original ResearchCancer-induced bone destructionBreast cancer cellsOsteolytic breast cancerBone homeostasisCancer growthCancer cellsBone destructionInflammatory osteolysisBreast cancerBreast cancer-induced bone destructionOsteolytic breast cancer metastasesPromising adjuvant therapyERK1/2 activationMEK1 expressionBreast cancer metastasisMetastatic breast cancer cellsActivation of pERK1/2Inflammatory conversionAdjuvant therapyPathological fracturesHuman pathological specimensBone microenvironmentPathological specimensSkeletal diseasePathway inhibitor
2020
Slc20a1/Pit1 and Slc20a2/Pit2 are essential for normal skeletal myofiber function and survival
Chande S, Caballero D, Ho BB, Fetene J, Serna J, Pesta D, Nasiri A, Jurczak M, Chavkin NW, Hernando N, Giachelli CM, Wagner CA, Zeiss C, Shulman GI, Bergwitz C. Slc20a1/Pit1 and Slc20a2/Pit2 are essential for normal skeletal myofiber function and survival. Scientific Reports 2020, 10: 3069. PMID: 32080237, PMCID: PMC7033257, DOI: 10.1038/s41598-020-59430-4.Peer-Reviewed Original ResearchConceptsHyp miceMuscle functionSkeletal muscleMyofiber functionNormal body weightSkeletal muscle atrophyGene dose-dependent reductionConditional knockout miceReduced oxygen consumption rateStimulation of AMP kinaseKnockout miceHypophosphatemic disordersMuscle atrophyERK1/2 activationGrip strengthConditional deletionHormonal changesLow bloodBody weightC2C12 myoblastsMiceFurther evaluationBlood phosphateDependent reductionAMP kinase
2013
Pseudophosphatase STYX modulates cell-fate decisions and cell migration by spatiotemporal regulation of ERK1/2
Reiterer V, Fey D, Kolch W, Kholodenko BN, Farhan H. Pseudophosphatase STYX modulates cell-fate decisions and cell migration by spatiotemporal regulation of ERK1/2. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: e2934-e2943. PMID: 23847209, PMCID: PMC3732994, DOI: 10.1073/pnas.1301985110.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCell DifferentiationCell MovementCell NucleusDual-Specificity PhosphatasesEnzyme ActivationGene Knockdown TechniquesGolgi ApparatusHumansIntracellular Signaling Peptides and ProteinsMAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinase PhosphatasesNuclear ProteinsPC12 CellsRatsConceptsPC12 cell differentiationCell migrationCell differentiationDual-specificity phosphatase familyCell fate decisionsDirectional cell migrationNuclear anchorPhosphatase familySpatiotemporal regulationGolgi polarizationSpatial regulatorCellular signalingNuclear exportERK activityGolgi apparatusERK signalingERK1/2 activationImportant regulatorInactive membersSignalingRegulatorERK1/2StyxDifferentiationDUSPs
2012
Olive Oil Polyphenols Differentially Inhibit Smooth Muscle Cell Proliferation through a G1/S Cell Cycle Block Regulated by ERK1/2
Abe R, Beckett J, Abe R, Nixon A, Rochier A, Yamashita N, Sumpio B. Olive Oil Polyphenols Differentially Inhibit Smooth Muscle Cell Proliferation through a G1/S Cell Cycle Block Regulated by ERK1/2. International Journal Of Angiology 2012, 21: 069-076. PMID: 23730132, PMCID: PMC3444010, DOI: 10.1055/s-0032-1315630.Peer-Reviewed Original ResearchSmooth muscle cell proliferationMuscle cell proliferationCell cycle blockOlive oil polyphenolsCell cycle analysisDay 1SMC proliferationG1/S cell cycle blockCycle blockOil polyphenolsRisk of atherosclerosisCell proliferationOLE groupControl groupFlow cytometryVascular SMCsWestern blottingDays of exposureS phaseCycle analysisERK1/2 activationNumber of cellsCell populationsOlive oilG1 phaseAltered store operated calcium entry increases cyclic 3′,5′‐adenosine monophosphate production and extracellular signal‐regulated kinases 1 and 2 phosphorylation in polycystin‐2‐defective cholangiocytes
Spirli C, Locatelli L, Fiorotto R, Morell CM, Fabris L, Pozzan T, Strazzabosco M. Altered store operated calcium entry increases cyclic 3′,5′‐adenosine monophosphate production and extracellular signal‐regulated kinases 1 and 2 phosphorylation in polycystin‐2‐defective cholangiocytes. Hepatology 2012, 55: 856-868. PMID: 21987453, PMCID: PMC3272110, DOI: 10.1002/hep.24723.Peer-Reviewed Original ResearchMeSH KeywordsAdenylyl CyclasesAnimalsBile DuctsCalciumCalcium ChannelsCalcium SignalingCells, CulturedCyclic AMPCyclic AMP-Dependent Protein KinasesHomeostasisMembrane GlycoproteinsMiceMice, KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Models, AnimalPhosphorylationSignal TransductionStromal Interaction Molecule 1TRPP Cation ChannelsVascular Endothelial Growth Factor AConceptsSensor stromal interaction molecule 1Adenylyl cyclase type 6Extracellular signal-regulated kinases 1Signal-regulated kinases 1Overproduction of cAMPStromal interaction molecule 1Orai channelsWild-type miceSOCE activationCAMP productionRapamycin (mTOR) signalingKinase 1ERK pathwayERK1/2 activationHuman diseasesWT cellsMammalian targetDependent activationSTIM-1CAMP/Inappropriate activationCyst growthCystic cholangiocytesPolycystic liver diseaseActivation
2010
Anaplasma phagocytophilum AptA modulates Erk1/2 signalling
Sukumaran B, Mastronunzio JE, Narasimhan S, Fankhauser S, Uchil PD, Levy R, Graham M, Colpitts TM, Lesser CF, Fikrig E. Anaplasma phagocytophilum AptA modulates Erk1/2 signalling. Cellular Microbiology 2010, 13: 47-61. PMID: 20716207, PMCID: PMC3005019, DOI: 10.1111/j.1462-5822.2010.01516.x.Peer-Reviewed Original ResearchConceptsA. phagocytophilum infectionPhagocytophilum infectionCommon tick-borne diseasesHuman granulocytic anaplasmosisActivation of ERK1/2ERK1/2 mitogen-activated protein kinasesA. phagocytophilum survivalPolymorphonuclear leucocytesMitogen-activated protein kinaseHuman neutrophilsObligate intracellular pathogensGranulocytic anaplasmosisIntracellular pathogensTick-borne diseasesInfectionERK1/2 activationAnaplasma phagocytophilumVimentinSurvivalActivationBacterial inclusionsHost proteinsIntermediate filament protein vimentinVirulence proteinsProtein vimentinERK1/2-Akt1 crosstalk regulates arteriogenesis in mice and zebrafish
Ren B, Deng Y, Mukhopadhyay A, Lanahan AA, Zhuang ZW, Moodie KL, Mulligan-Kehoe MJ, Byzova TV, Peterson RT, Simons M. ERK1/2-Akt1 crosstalk regulates arteriogenesis in mice and zebrafish. Journal Of Clinical Investigation 2010, 120: 1217-1228. PMID: 20237411, PMCID: PMC2846043, DOI: 10.1172/jci39837.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsArteriesCarrier ProteinsMaleMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MorphogenesisNeovascularization, PhysiologicNeuropeptidesPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktSignal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2ZebrafishZebrafish Proteins
2009
Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP
Xu J, Kurup P, Zhang Y, Goebel-Goody SM, Wu PH, Hawasli AH, Baum ML, Bibb JA, Lombroso PJ. Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP. Journal Of Neuroscience 2009, 29: 9330-9343. PMID: 19625523, PMCID: PMC2737362, DOI: 10.1523/jneurosci.2212-09.2009.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsBrainCalpainCell DeathCells, CulturedCyclin-Dependent Kinase 5EndocytosisGlutamic AcidIn Vitro TechniquesMiceMice, KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Neuronsp38 Mitogen-Activated Protein KinasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateSynapsesConceptsStriatal-enriched protein tyrosine phosphataseCalpain cleavage sitesP38 activationCell deathCleavage siteExtracellular signal-regulated kinase 1/2Protein tyrosine phosphataseSignal-regulated kinase 1/2Promotes cell survivalActivation of p38Tyrosine phosphataseSubstrate bindingKinase 1/2ERK1/2 activationCalpain cleavageCell survivalNovel mechanismCalpain-mediated proteolysisReceptors coupleP38NMDAR stimulationPostsynaptic terminalsValid targetCleavage productsSTEP substrates
2008
Cyst formation and activation of the extracellular regulated kinase pathway after kidney specific inactivation of Pkd1
Shibazaki S, Yu Z, Nishio S, Tian X, Thomson RB, Mitobe M, Louvi A, Velazquez H, Ishibe S, Cantley LG, Igarashi P, Somlo S. Cyst formation and activation of the extracellular regulated kinase pathway after kidney specific inactivation of Pkd1. Human Molecular Genetics 2008, 17: 1505-1516. PMID: 18263604, PMCID: PMC2902289, DOI: 10.1093/hmg/ddn039.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisButadienesCell ProliferationCystsDisease Models, AnimalEnzyme ActivationKidneyMAP Kinase Kinase 1MAP Kinase Kinase 2MiceMice, Mutant StrainsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NitrilesPolycystic Kidney, Autosomal DominantProtein Kinase InhibitorsTRPP Cation ChannelsConceptsCyst formationERK1/2 activationPostnatal day 21Renal cystic diseaseWeeks of birthCyst cell proliferationPolycystic kidney diseaseKinase pathwayKidney tubule cellsKidney-specific inactivationRenal failureMEK1/2 inhibitor U0126Kidney diseaseCystic diseaseMAPK/ERKMAPK/ERK activationPresence of ciliaProliferative indexCyst growthCyst expansionDay 21Tubule cellsBrdU uptakeCystic kidneysBromodeoxyuridine incorporation
2006
The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala
Paul S, Olausson P, Venkitaramani DV, Ruchkina I, Moran TD, Tronson N, Mills E, Hakim S, Salter MW, Taylor JR, Lombroso PJ. The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala. Biological Psychiatry 2006, 61: 1049-1061. PMID: 17081505, PMCID: PMC1853327, DOI: 10.1016/j.biopsych.2006.08.005.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAminoacetonitrileAmygdalaAnimalsBehavior, AnimalCells, CulturedConditioning, ClassicalCycloheximideElectric StimulationEnzyme InhibitorsFearFemaleImmunohistochemistryIn Vitro TechniquesLong-Term PotentiationMemoryMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NeostriatumPatch-Clamp TechniquesPoint MutationPregnancyProtein Synthesis InhibitorsProtein Tyrosine PhosphatasesRatsRats, Sprague-DawleyTranslocation, GeneticConceptsStriatal-enriched protein tyrosine phosphataseERK1/2 activationMitogen-activated protein kinaseProtein tyrosine phosphataseDe novo translationActivation of ERK1/2Tyrosine phosphataseProtein bindsKinase signalingProtein kinaseSequential recruitmentAmygdala-dependent memory formationERK pathwayMemory formationPrimary cell culturesNuclear translocationBiphasic activationLong-term potentiationTranslation blockTAT-STEPERKCell culturesERK1/2ActivationPathway
2005
ERK1/2 mitogen-activated protein kinase selectively mediates IL-13–induced lung inflammation and remodeling in vivo
Lee PJ, Zhang X, Shan P, Ma B, Lee CG, Homer RJ, Zhu Z, Rincon M, Mossman BT, Elias JA. ERK1/2 mitogen-activated protein kinase selectively mediates IL-13–induced lung inflammation and remodeling in vivo. Journal Of Clinical Investigation 2005, 116: 163-173. PMID: 16374521, PMCID: PMC1319220, DOI: 10.1172/jci25711.Peer-Reviewed Original ResearchConceptsIL-13-induced inflammationIL-13IL-13 expressionSTAT6-independent mannerIL-13 stimulationLung inflammationSpecific chemokinesTg miceEffector responsesSystemic administrationMMP-2Alveolar remodelingInflammationLungCritical rolePotent activationTissue effectsERK1/2 activationSTAT6ChemokinesInhibitor PD98059ERK1/2ERK1/2 mitogenRemodelingDisease
1999
Thrombospondin-1 regulation of smooth muscle cell chemotaxis is extracellular signal-regulated protein kinases 1/2 dependent
Gahtan V, Wang X, Willis A, Tuszynski G, Sumpio B. Thrombospondin-1 regulation of smooth muscle cell chemotaxis is extracellular signal-regulated protein kinases 1/2 dependent. Surgery 1999, 126: 203-207. PMID: 10455885, DOI: 10.1016/s0039-6060(99)70156-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCattleCell Adhesion MoleculesCells, CulturedChemotaxisDose-Response Relationship, DrugFocal Adhesion Protein-Tyrosine KinasesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesMuscle, Smooth, VascularProtein-Tyrosine KinasesThrombospondin 1ConceptsSmooth muscle cell chemotaxisTSP-1-induced chemotaxisThrombospondin-1Protein kinase familyExtracellular signal-regulated proteinExtracellular signal-regulated protein kinase 1/2Vascular smooth muscle cell chemotaxisProtein kinase 1/2Extracellular matrix proteinsCell chemotaxisSerum-free mediumPlatelet-derived growth factorKinase familyKinase 1/2Top chambersFunctional importanceMatrix proteinsERK1/2 activationWestern blot analysisERK1/2 inhibitorBlot analysisERK1/2VSMCPD98059VSMCsPhosphatidylinositol-3 Kinase Dependent MAP Kinase Activation via p21ras in Endothelial Cells Exposed to Cyclic Strain
Ikeda M, Kito H, Sumpio B. Phosphatidylinositol-3 Kinase Dependent MAP Kinase Activation via p21ras in Endothelial Cells Exposed to Cyclic Strain. Biochemical And Biophysical Research Communications 1999, 257: 668-671. PMID: 10208841, DOI: 10.1006/bbrc.1999.0532.Peer-Reviewed Original ResearchMeSH KeywordsAndrostadienesAnimalsAortaCalcium-Calmodulin-Dependent Protein KinasesCattleCells, CulturedChromonesEndothelium, VascularEnzyme ActivationGuanosine TriphosphateHemodynamicsMorpholinesOncogene Protein p21(ras)Phosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationSignal TransductionStress, MechanicalTime FactorsWortmanninConceptsERK1/2 activationPhosphatidylinositol-3 kinase inhibitorMAP kinase activationExtracellular signal-regulated protein kinases 1Endothelial cellsMechanical stretchKinase inhibitorsERK1/2 phosphorylationEffect of wortmanninPossible involvementHemodynamic forcesProtein kinase 1ActivationKinase 1Upstream pathwaysRapid activationKinase activationSignal transduction pathwaysP21ras activationLY294002ERK1 activationERK2 activation
1998
Calcium-Independent Activation of Extracellular Signal-Regulated Kinases 1 and 2 by Cyclic Strain
Ikeda M, Takei T, Mills I, Sumpio B. Calcium-Independent Activation of Extracellular Signal-Regulated Kinases 1 and 2 by Cyclic Strain. Biochemical And Biophysical Research Communications 1998, 247: 462-465. PMID: 9642151, DOI: 10.1006/bbrc.1998.8811.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium Channel BlockersCalcium-Calmodulin-Dependent Protein KinasesCattleCells, CulturedChelating AgentsEgtazic AcidEndothelium, VascularEnzyme ActivationExtracellular SpaceGadoliniumHydroquinonesIntracellular FluidMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPhosphorylationStress, MechanicalConceptsEndothelial cellsActivation of ERK1/2Baseline phosphorylationExtracellular Ca2Normal extracellular Ca2Aortic endothelial cellsKinase 1Bovine aortic endothelial cellsStrain-induced activationCycles/minChannel blockersExtracellular signal-regulated kinases 1Signal-regulated kinases 1Calcium-independent activationBenzohydroquinoneERK1/2 activationERK1/2Free mediumEffect of Ca2ActivationCa2EGTA
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply