Search results for "ASK1"

showing 10 items of 18 documents

Activation of a nuclear-localized SIPK in tobacco cells challenged by cryptogein, an elicitor of plant defence reactions.

2009

When a plant cell is challenged by a well-defined stimulus, complex signal transduction pathways are activated to promote the modulation of specific sets of genes and eventually to develop adaptive responses. In this context, protein phosphorylation plays a fundamental role through the activation of multiple protein kinase families. Although the involvement of protein kinases at the plasma membrane and cytosolic levels are now well-documented, their nuclear counterparts are still poorly investigated. In the field of plant defence reactions, no known study has yet reported the activation of a nuclear protein kinase and/or its nuclear activity in plant cells, although some protein kinases, e.…

0106 biological sciencesMAPK/ERK pathwayMolecular Sequence DataActive Transport Cell NucleusBiology01 natural sciencesBiochemistryMAP2K703 medical and health sciencesCytosolTobaccoASK1Protein phosphorylation[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceNuclear proteinProtein kinase AMolecular BiologyConserved Sequence030304 developmental biologyPlant ProteinsCell Nucleus0303 health sciencesKinasePlant ExtractsAlgal ProteinsLife SciencesCell BiologyCell biologyEnzyme ActivationBiochemistrySignal transductionMitogen-Activated Protein KinasesSequence Alignment010606 plant biology & botanySignal TransductionThe Biochemical journal
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Regulation of Nicotiana tabacum osmotic stress-activated protein kinase and its cellular partner GAPDH by nitric oxide in response to salinity

2010

Several studies focusing on elucidating the mechanism of NO (nitric oxide) signalling in plant cells have highlighted that its biological effects are partly mediated by protein kinases. The identity of these kinases and details of how NO modulates their activities, however, remain poorly investigated. In the present study, we have attempted to clarify the mechanisms underlying NO action in the regulation of NtOSAK (Nicotiana tabacum osmotic stress-activated protein kinase), a member of the SNF1 (sucrose non-fermenting 1)-related protein kinase 2 family. We found that in tobacco BY-2 (bright-yellow 2) cells exposed to salt stress, NtOSAK is rapidly activated, partly through a NO-dependent pr…

0106 biological sciencesOsmosisSalinityNicotiana tabacumMolecular Sequence DataNitric Oxide01 natural sciencesBiochemistry03 medical and health sciencesEnzyme activatorStress PhysiologicalTobaccoASK1[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceProtein kinase AMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseCells Cultured030304 developmental biologyPlant Proteins0303 health sciencesbiologyKinaseGlyceraldehyde-3-Phosphate DehydrogenasesLife SciencesCell BiologyS-Nitrosylationbiology.organism_classification3. Good healthBiochemistrybiology.proteinPhosphorylationProtein Kinases010606 plant biology & botany
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Loss of cellular FLICE-inhibitory protein promotes acute cholestatic liver injury and inflammation from bile duct ligation.

2017

Cholestatic liver injury results from impaired bile flow or metabolism and promotes hepatic inflammation and fibrogenesis. Toxic bile acids that accumulate in cholestasis induce apoptosis and contribute to early cholestatic liver injury, which is amplified by accompanying inflammation. The aim of the current study was to evaluate the role of the antiapoptotic caspase 8-homolog cellular FLICE-inhibitory (cFLIP) protein during acute cholestatic liver injury. Transgenic mice exhibiting hepatocyte-specific deletion of cFLIP (cFLIP−/−) were used for in vivo and in vitro analysis of cholestatic liver injury using bile duct ligation (BDL) and the addition of bile acids ex vivo. Loss of cFLIP in h…

0301 basic medicineLiver CirrhosisTime FactorsPhysiologyCASP8 and FADD-Like Apoptosis Regulating ProteinInflammationApoptosisp38 Mitogen-Activated Protein KinasesHepatitisBile Acids and Salts03 medical and health sciencesNecrosisCholestasisPhysiology (medical)medicineHepatic Stellate CellsAnimalsASK1Genetic Predisposition to DiseaseLigationCells CulturedTumor Necrosis Factor alpha-Induced Protein 3chemistry.chemical_classificationLiver injuryCommon Bile DuctMice KnockoutReactive oxygen speciesHepatologyBile duct ligationGastroenterologyTranscription Factor RelAmedicine.diseaseOxidative Stress030104 developmental biologyCholedocholithiasisPhenotypechemistryLiverNeutrophil InfiltrationApoptosisFLICE Inhibitory ProteinCancer researchHepatocytesCytokinesmedicine.symptomInflammation MediatorsSignal TransductionAmerican journal of physiology. Gastrointestinal and liver physiology
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Diverse stress signals activate the C1 subgroup MAP kinases ofArabidopsis

2007

AbstractMitogen-activated protein kinase (MAPK) cascades play an important role in mediating stress responses in plants. In Arabidopsis, 20 MAPKs have been identified and classified into four major groups (A–D). Little is known about the role of group C MAPKs. We have studied the activation of Arabidopsis subgroup C1 MAPKs (AtMPK1/AtMPK2) in response to mechanical injury. An increase in their kinase activity was detected in response to wounding that was blocked by cycloheximide. Jasmonic acid (JA) activated AtMPK1/AtMPK2 in the absence of wounding. Wound and JA-induction of AtMPK1/2 kinase activity was not prevented in the JA-insensitive coi1 mutant. Other stress signals, such as abscisic a…

AcclimatizationArabidopsisBiophysicsBiochemistryGene Expression Regulation Enzymologicchemistry.chemical_compoundGene Expression Regulation PlantStructural BiologyArabidopsisGeneticsASK1Kinase activityProtein kinase AMolecular BiologyJasmonic acidMAP kinase kinase kinasebiologyArabidopsis ProteinsKinaseJasmonic acidWoundHydrogen PeroxideCell Biologybiology.organism_classificationBiochemistrychemistryMitogen-activated protein kinasebiology.proteinMAP kinaseStress MechanicalMitogen-Activated Protein KinasesAbscisic AcidSignal TransductionFEBS Letters
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Different Genetic Expression Profiles of Oxidative Stress and Apoptosis-Related Genes in Crohn's Disease.

2018

<b><i>Background/Aims:</i></b> Increased oxidative stress and decreased immune cell apoptosis have been reported to be important factors in the pathogenesis of Crohn’s disease (CD). Our aim was to characterize the genetic expression of molecules implicated in the regulation of oxidative stress and apoptosis in peripheral white mononuclear cells of 18 healthy volunteers (controls) and 20 patients at the onset of CD (active CD [aCD]): 10 who achieved remission (inactive CD [iCD]) and 10 who did not present a complete and deep response to treatment (aCD-T). <b><i>Methods:</i></b> mRNA expression was measured by the Agena MassARRAY quantitative ge…

AdultMalePeptidylprolyl isomerase DDown-RegulationApoptosismedicine.disease_causeFas ligandPathogenesis03 medical and health sciencesYoung Adult0302 clinical medicineCrohn DiseaseGene expressionMedicineHumansASK1RNA Messengerbusiness.industryKinaseGene Expression ProfilingGastroenterologyCatalaseHealthy VolunteersUp-RegulationCrohn's diseaseOxidative StressApoptosisOxidative stress030220 oncology & carcinogenesisCase-Control StudiesCancer researchLeukocytes Mononuclear030211 gastroenterology & hepatologyFemalebusinessReactive oxygen speciesTranscriptomeOxidative stressBiomarkersDigestion
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Protein kinase activities associated with ribosomes of developing rat brain. Identification of eukaryotic initiation factor 2 kinases.

1986

Protein kinases associated with ribosomes in the brains of suckling (4-10 days) and adult (2 months) rats were extracted from ribosomal fraction with 0.5 M KCl. The different protein kinase activities were characterized by their ability to phosphorylate three exogenous substrates: casein, histone IIs and histone IIIs in the presence of different modulators. Ribosomal salt wash fractions contain a high casein kinase activity which was partially inhibited by heparin and stimulated by calmodulin in the presence of Ca2+, indicating the presence of casein kinase I and II and calcium/calmodulin-dependent kinases. Cyclic AMP and cyclic GMP-dependent kinases and protein kinase C (calcium/phospholip…

AgingbiologyCyclin-dependent kinase 2BrainCaseinsRats Inbred StrainsMitogen-activated protein kinase kinaseRatseIF-2 KinaseDevelopmental NeuroscienceBiochemistryCasein Kinase ICasein kinase 2 alpha 1biology.proteinAnimalsASK1Cyclin-dependent kinase 9Casein kinase 1Casein kinase 2PhosphorylationProtein KinasesRibosomesDevelopmental BiologySubcellular FractionsInternational journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience
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Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O.

2006

Following the observation that cells are able to recover from membrane lesions incurred by Staphylococcus aureus alpha-toxin and streptolysin O (SLO), we investigated the role of p38 in this process. p38 phosphorylation occurred in response to attack by both toxins, commencing within minutes after toxin treatment and waning after several hours. While SLO reportedly activates p38 via ASK1 and ROS, we show that this pathway does not play a major role for p38 induction in alpha-toxin-treated cells. Strikingly divergent effects of p38 blockade were noted depending on the toxin employed. In the case of alpha-toxin, inhibition of p38 within the time frame of its activation led to disruption of th…

KeratinocytesProgrammed cell deathStaphylococcus aureusCell Membrane Permeabilityp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologymedicine.disease_causeMAP Kinase Kinase Kinase 5Biochemistryp38 Mitogen-Activated Protein KinasesMicrobiologyHemolysin ProteinsAdenosine TriphosphateBacterial ProteinsProto-Oncogene ProteinsmedicineHumansASK1PhosphorylationMolecular BiologyCells CulturedPore-forming toxinToxinCell MembraneCell BiologyProtein-Tyrosine KinasesBlockadeCell biologyEnzyme ActivationStreptolysinsPhosphorylationStreptolysinBiochemical and biophysical research communications
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Tumor Necrosis Factor (TNF) Receptor 1 Signaling Downstream of TNF Receptor-associated Factor 2

1997

Like other members of the tumor necrosis factor (TNF) receptor family, p55 TNF receptor 1 (TNF-R1) lacks intrinsic signaling capacity and transduces signals by recruiting associating molecules. The TNF-R1 associated death domain protein interacts with the p55 TNF-R1 cytoplasmic domain and recruits the Fas-associated death domain protein (which directly activates the apoptotic proteases), the protein kinase receptor interacting protein, and TNF receptor-associated factor 2 (TRAF2). TRAF2 has previously been demonstrated to activate both transcription factor nuclear factor kappaB (NFkappaB) and the c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) pathway, which in turn stimu…

MAP kinase kinase kinasebiologyChemistryCyclin-dependent kinase 2Cell BiologyMitogen-activated protein kinase kinaseBiochemistryProtein kinase RMAP2K7Cancer researchbiology.proteinCyclin-dependent kinase 9ASK1c-RafMolecular BiologyJournal of Biological Chemistry
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The neuropeptide PACAP promotes ?‐secretase pathway for processing Alzheimer amyloid precursor protein

2006

SPECIFIC AIMSProteolytic cleavage of the amyloid precursor protein (APP) by α-secretase within the Aβ sequence precludes formation of amyloidogenic peptides and leads to a release of soluble APPsα,...

MAP kinase kinase kinasebiologyNeuropeptideMitogen-activated protein kinase kinaseCleavage (embryo)BiochemistryAlpha secretaseBiochemistrymental disordersGeneticsAmyloid precursor proteinbiology.proteinASK1Molecular BiologyBiotechnologyG protein-coupled receptorThe FASEB Journal
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Activation of Cardiac c-Jun NH 2 -Terminal Kinases and p38-Mitogen–Activated Protein Kinases With Abrupt Changes in Hemodynamic Load

2001

Abstract —The role of mitogen-activated protein kinase (MAPK) pathways as signal transduction intermediates of hemodynamic stress leading to cardiac hypertrophy in the adult heart is not fully established. In a rat model of pressure-overload hypertrophy, we examined whether activation of MAPK pathways, namely, the extracellular signal–regulated protein kinase (ERK), c-Jun NH 2 -terminal kinase (JNK), and the p38-MAPK pathways, occurs during rapid changes in hemodynamic load in vivo. A slight activation of ERK2 and marked increases in JNK1 and p38-MAPK activities were observed 30 minutes after aortic banding. The increase in p38-MAPK activity was accompanied by an increase in the phosphoryl…

MAPK/ERK pathwaymedicine.medical_specialtyProto-Oncogene Proteins c-junp38 mitogen-activated protein kinasesp38 Mitogen-Activated Protein KinasesVentricular Function LeftStress PhysiologicalInternal medicineInternal MedicinemedicineAnimalsASK1PhosphorylationRats WistarCyclic AMP Response Element-Binding ProteinProtein kinase AProtein kinase CMAPK14Activating Transcription Factor 2biologyKinaseMyocardiumJNK Mitogen-Activated Protein KinasesRatsCell biologyEnzyme ActivationTranscription Factor AP-1Disease Models AnimalEndocrinologyMitogen-activated protein kinasebiology.proteinFemaleMitogen-Activated Protein KinasesTranscription FactorsHypertension
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