2020
Decline of RhoA/Rho-kinase 1 expression and myosin light chain phosphorylation facilitate the formation of aortic dissection
Zhang W, Liu F, Shu X, Wang E, Wang L, Fu W. Decline of RhoA/Rho-kinase 1 expression and myosin light chain phosphorylation facilitate the formation of aortic dissection. Chinese Journal Of Experimental Surgery 2020, 37: 828-831. DOI: 10.3760/cma.j.cn421213-20191209-00869.Peer-Reviewed Original ResearchSmooth muscle cellsMyosin light chainPhosphorylation of myosin light chainMyosin light chain phosphorylationAortic dissectionFormation of aortic dissectionExpression of RhoAFormation of ADPhosphorylated myosin light chainPrimary smooth muscle cellsLight chain phosphorylationMLC phosphorylationRhoA/Rho-kinaseMuscle cellsFasudilAD groupInhibitors of ROCK1Light chainPhosphorylationQuantitative variationDissectionRhoAROCK1ImmunofluorescenceBAPN
2018
Endothelial cell‐secreted MIF reduces pericyte contractility and enhances neutrophil extravasation
Pellowe AS, Sauler M, Hou Y, Merola J, Liu R, Calderon B, Lauridsen HM, Harris MR, Leng L, Zhang Y, Tilstam PV, Pober JS, Bucala R, Lee PJ, Gonzalez AL. Endothelial cell‐secreted MIF reduces pericyte contractility and enhances neutrophil extravasation. The FASEB Journal 2018, 33: 2171-2186. PMID: 30252532, PMCID: PMC6338650, DOI: 10.1096/fj.201800480r.Peer-Reviewed Original ResearchConceptsMacrophage migration inhibitory factorNeutrophil transmigrationNeutrophil extravasationPericyte contractilitySelective deletionMIF knockout miceAcute lung injuryMigration inhibitory factorHuman neutrophil transmigrationMyosin light chain phosphorylationLung injuryNeutrophil infiltrationBronchoalveolar lavageInflammatory disordersKnockout miceInhibitory factorMicro-ELISAContractilityLight chain phosphorylationPhosphorylated myosin light chainEndothelial cellsBarrier functionExtravasationPericytesParacrine signalsHypercapnia increases airway smooth muscle contractility via caspase-7–mediated miR-133a–RhoA signaling
Shigemura M, Lecuona E, Angulo M, Homma T, Rodríguez DA, Gonzalez-Gonzalez FJ, Welch LC, Amarelle L, Kim SJ, Kaminski N, Budinger GRS, Solway J, Sznajder JI. Hypercapnia increases airway smooth muscle contractility via caspase-7–mediated miR-133a–RhoA signaling. Science Translational Medicine 2018, 10 PMID: 30185650, PMCID: PMC6889079, DOI: 10.1126/scitranslmed.aat1662.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAgedAged, 80 and overAirway ResistanceAnimalsCalciumCalpainCarbon DioxideCaspase 7Chronic DiseaseDown-RegulationEnzyme ActivationFemaleHumansHypercapniaMaleMEF2 Transcription FactorsMice, Inbred C57BLMicroRNAsMiddle AgedMuscle ContractionMuscle, SmoothMyocytes, Smooth MusclePulmonary Disease, Chronic ObstructiverhoA GTP-Binding ProteinSignal TransductionConceptsChronic obstructive pulmonary diseaseAirway smooth muscle cellsSmooth muscle cellsMouse airway smooth muscle cellsSevere chronic obstructive pulmonary diseaseHuman airway smooth muscle cellsAirway smooth muscle contractilityMuscle cellsCorrection of hypercapniaSmooth muscle cell contractionCohort of patientsObstructive pulmonary diseaseHigh airway resistanceSevere lung diseaseDevelopment of hypercapniaSmooth muscle contractilityMuscle cell contractionRas homolog family member AMyosin light chain phosphorylationAirway contractilityAirway contractionHypercapnic patientsCOPD severityPulmonary diseaseAirway resistance
2016
Leukaemia-associated Rho guanine nucleotide exchange factor (LARG) plays an agonist specific role in platelet function through RhoA activation
Zou S, Teixeira AM, Yin M, Xiang Y, Xavier-Ferrucio J, Zhang PX, Hwa J, Min W, Krause DS. Leukaemia-associated Rho guanine nucleotide exchange factor (LARG) plays an agonist specific role in platelet function through RhoA activation. Thrombosis And Haemostasis 2016, 116: 506-516. PMID: 27345948, PMCID: PMC5845781, DOI: 10.1160/th15-11-0848.Peer-Reviewed Original ResearchConceptsMegakaryocyte maturationPlatelet functionRhoA activationKO plateletsLeukemia-associated Rho guanineΑ-granule releasePlatelet signal transductionSmall molecule-mediated inhibitionExchange factorSignal transductionMyosin light chain phosphorylationRho guanineKO miceBleeding timeHuman megakaryocytesInternal bleedingPlatelet aggregationNormal haemostasisLight chain phosphorylationHuman plateletsVivo assaysPlateletsSpecific roleMiceChain phosphorylation
2013
CXCL12 induces hepatic stellate cell contraction through a calcium-independent pathway
Saiman Y, Agarwal R, Hickman DA, Fausther M, El-Shamy A, Dranoff JA, Friedman SL, Bansal MB. CXCL12 induces hepatic stellate cell contraction through a calcium-independent pathway. AJP Gastrointestinal And Liver Physiology 2013, 305: g375-g382. PMID: 23812037, PMCID: PMC3761245, DOI: 10.1152/ajpgi.00185.2012.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCalciumCell LineCell ShapeChelating AgentsChemokine CXCL12CollagenDose-Response Relationship, DrugGelsHepatic Stellate CellsHumansMiceMyosin Light ChainsPhenotypePhosphorylationProtein Kinase InhibitorsReceptors, CXCR4Recombinant Proteinsrho-Associated KinasesRNA InterferenceSignal TransductionTransfectionConceptsHepatic stellate cellsChronic liver diseaseStellate cell contractionPortal hypertensionLiver diseaseLiver fibrosisSmall molecule inhibitorsStimulation of HSCsHepatic stellate cell contractionEnd-stage liver diseaseGel contractionActivated hepatic stellate cellsAddition of AMD3100Functional chemokine receptorsIntrahepatic blood flowCXCR4-dependent mannerCell contractionDeath of patientsRho-kinase pathwayMolecule inhibitorsCollagen gel latticeRho-kinase inhibitorCalcium-independent fashionCalcium-independent pathwayMyosin light chain phosphorylation
2012
Statin pleiotropy prevents rho kinase‐mediated intestinal epithelial barrier compromise induced by Blastocystis cysteine proteases
Mirza H, Wu Z, Teo JD, Tan KS. Statin pleiotropy prevents rho kinase‐mediated intestinal epithelial barrier compromise induced by Blastocystis cysteine proteases. Cellular Microbiology 2012, 14: 1474-1484. PMID: 22587300, DOI: 10.1111/j.1462-5822.2012.01814.x.Peer-Reviewed Original ResearchConceptsZonula occludens-1Intestinal epithelial barrier functionEpithelial barrier functionEpithelial permeabilityIntestinal infectionsFluorescein isothiocyanate-dextran fluxHuman colonic epithelial monolayersTherapeutic potentialHMG-CoA reductaseHMG-CoA reductase inhibitor simvastatinBarrier functionChronic intestinal infectionCytoskeletal F-actinIntestinal epithelial permeabilityReductase inhibitor simvastatinColonic epithelial monolayersIntestinal epithelial barrierTransepithelial resistanceTight junctional ZO-1Myosin light chain phosphorylationParasite cysteine proteasesSymptomatic patientsIntestinal pathologyCysteine proteasesBlastocystis infection
2007
Induction of Vascular Permeability: βPIX and GIT1 Scaffold the Activation of Extracellular Signal-regulated Kinase by PAK
Stockton R, Reutershan J, Scott D, Sanders J, Ley K, Schwartz MA. Induction of Vascular Permeability: βPIX and GIT1 Scaffold the Activation of Extracellular Signal-regulated Kinase by PAK. Molecular Biology Of The Cell 2007, 18: 2346-2355. PMID: 17429073, PMCID: PMC1877103, DOI: 10.1091/mbc.e06-07-0584.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCapillary PermeabilityCattleCell Cycle ProteinsCells, CulturedEndothelial CellsEnzyme ActivationExtracellular Signal-Regulated MAP KinasesGuanine Nucleotide Exchange FactorsHumansInflammationLipopolysaccharidesLungMicep21-Activated KinasesPeptidesProtein Serine-Threonine KinasesRho Guanine Nucleotide Exchange FactorsConceptsP21-activated kinaseMitogen-activated protein kinase kinaseEndothelial cell-cell junctionsExtracellular signal-regulated kinaseCell-cell junctionsProtein kinase kinaseMyosin light chain phosphorylationLight chain phosphorylationSignal-regulated kinaseCell-permeant peptideActivation of ERKKinase kinaseExtracellular signalsPAK functionChain phosphorylationCritical regulatorKinaseCell contractilityCell typesCultured endothelial cellsPhosphorylationMouse lung injury modelMyosin phosphorylationEndothelial cellsGIT1
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