Search results for "PROTEIN KINASE"

showing 10 items of 1188 documents

Phorbol Esters and Muscarinic Receptor Agonists Activate Phospholipase D in Heart and Brain

1991

Phospholipase D (PLD) hydrolyzes phosphatidylcholine and thereby seems to play a key role in a novel pathway of signal transduction. PLD activity in rat hippocampal slices and atria of rat, guinea pig and chicken hearts was determined by measuring the catalytic products choline (Ch), phosphatidic acid (PA) and, in the presence of a primary alcohol, phosphatidylpropanol or phosphatidylethanol. It was found that the PLD activity was high, even under resting conditions, in both tissues, especially in the hippocampus, and that the enzyme activity could be enhanced by activation of protein kinase C and by muscarinic receptor stimulation.

chemistry.chemical_compoundchemistryBiochemistryPhospholipase DMuscarinic acetylcholine receptor M4Muscarinic acetylcholine receptor M3lipids (amino acids peptides and proteins)Muscarinic acetylcholine receptor M2PhosphatidylethanolPhosphatidic acidMuscarinic acetylcholine receptor M1Protein kinase C
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Integrin α2β1 Mediates Isoform-Specific Activation of p38 and Upregulation of Collagen Gene Transcription by a Mechanism Involving the α2 Cytoplasmic…

1999

Two collagen receptors, integrins alpha1beta1 and alpha2beta1, can regulate distinct functions in cells. Ligation of alpha1beta1, unlike alpha2beta1, has been shown to result in recruitment of Shc and activation of the Ras/ERK pathway. To identify the downstream signaling molecules activated by alpha2beta1 integrin, we have overexpressed wild-type alpha2, or chimeric alpha2 subunit with alpha1 integrin cytoplasmic domain in human osteosarcoma cells (Saos-2) lacking endogenous alpha2beta1. The chimeric alpha2/alpha1 chain formed a functional heterodimer with beta1. In contrast to alpha2/alpha1 chimera, forced expression of alpha2 integrin resulted in upregulation of alpha1 (I) collagen gene …

collagenIntegrinsReceptors CollagenTranscription GeneticintegrinIntegrincytoplasmic domainCDC42Biologyp38 MAPKTransfectionCD49cp38 Mitogen-Activated Protein KinasesCollagen receptorTumor Cells CulturedHumansProtein IsoformsCell BiologyMolecular biologyCell biologyUp-RegulationEnzyme ActivationIntegrin alpha Mbiology.proteinIntegrin beta 6Original ArticleSignal transductionMitogen-Activated Protein KinasesITGA6Signal TransductionThe Journal of Cell Biology
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Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity

2002

Mismatch repair (MMR) is involved in the removal of mispaired bases from DNA and thus plays an important role in the maintenance of genomic stability and the prevention of mutations and cancer. Moreover, MMR triggers genotoxicity and apoptosis upon processing of DNA lesions such as O6-methylguanine. Whereas the enzymology of MMR has been elucidated in great detail, only limited data are available concerning its regulation. Here we show that the major mismatch-binding proteins MSH2 and MSH6, forming the MutSalpha complex, are phosphorylated in vitro by protein kinase C and casein kinase II, but not by protein kinase A. Phosphorylation of MSH2 and MSH6 was also found within the cell, with MSH…

congenital hereditary and neonatal diseases and abnormalitiesDNA RepairDNA repairBase Pair MismatchMacromolecular SubstancesActive Transport Cell NucleusBiologyProtein Serine-Threonine KinasesArticleProto-Oncogene ProteinsGeneticsHumansProtein phosphorylationPhosphorylationProtein kinase ACasein Kinase IIneoplasmsProtein kinase CProtein Kinase CCell Nucleusnutritional and metabolic diseasesdigestive system diseasesDNA-Binding ProteinsMutS Homolog 2 ProteinBiochemistryMSH2PhosphorylationDNA mismatch repairCasein kinase 2HeLa Cells
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In vivo discovery of a peptide that prevents CUG-RNA hairpin formation and reverses RNA toxicity in myotonic dystrophy models

2011

6 pages, 5 figures. PMID:21730182[PubMed] PMCID: PMC3141925[Available on 2012/1/19]

congenital hereditary and neonatal diseases and abnormalitiesProtein ConformationRNA-binding proteinProtein Serine-Threonine KinasesBiologyMyotonic dystrophyMyotonin-Protein Kinasedrug discoveryMicechemistry.chemical_compoundnon-coding RNA diseasePeptide Librarymedicinal chemistryDrug DiscoveryGene expressionmedicineAnimalsMyotonic DystrophyMBNL1MultidisciplinaryMusclesdisease modelAlternative splicingRNA-Binding ProteinsRNADystrophyBiological Sciencesmedicine.diseaseRNA secondary structureMolecular biologyDNA-Binding ProteinschemistryRNA splicingDrosophilaTrinucleotide Repeat ExpansionOligopeptides
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Infectious Entry Pathway of Enterovirus B Species

2015

Enterovirus B species (EV-B) are responsible for a vast number of mild and serious acute infections. They are also suspected of remaining in the body, where they cause persistent infections contributing to chronic diseases such as type I diabetes. Recent studies of the infectious entry pathway of these viruses revealed remarkable similarities, including non-clathrin entry of large endosomes originating from the plasma membrane invaginations. Many cellular factors regulating the efficient entry have recently been associated with macropinocytic uptake, such as Rac1, serine/threonine p21-activated kinase (Pak1), actin, Na/H exchanger, phospholipace C (PLC) and protein kinase Cα (PKCα). Another…

coxsackievirus A9EchovirusEndosomelcsh:QR1-502Virus AttachmentEndosomesReviewCoxsackievirusEndocytosismedicine.disease_causelcsh:Microbiology03 medical and health sciencesVirologymedicineReceptorProtein kinase A030304 developmental biology0303 health sciencesbiologyKinase030302 biochemistry & molecular biologyechovirusVirus Internalizationbiology.organism_classificationVirologyEndocytosisEnterovirus B Human3. Good healthCell biologyInfectious DiseasesHost-Pathogen InteractionsEnterovirusentrycoxsackievirus B3signalingViruses
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Targeting DNA double strand break repair with hyperthermia and DNA-PKcs inhibition to enhance the effect of radiation treatment

2016

// Bregje van Oorschot 1 , Giovanna Granata 1 , Simone Di Franco 2 , Rosemarie ten Cate 1 , Hans M. Rodermond 1 , Matilde Todaro 3 , Jan Paul Medema 1 , Nicolaas A.P. Franken 1 1 Laboratory for Experimental Oncology and Radiobiology (LEXOR), Center for Experimental Molecular Medicine, Department of Radiation Oncology, Academic Medical Center, Cancer Genomics Center, Amsterdam, The Netherlands 2 Department of Surgical, Oncological and Stomatological Sciences (DICHIRONS), Cellular and Molecular Pathophysiology Laboratory, University of Palermo, Palermo, Italy 3 Biomedical Department of Internal and Specialistic Medicine (DIBIMIS), University of Palermo, Palermo, Italy Correspondence to: Nicol…

double-strand break0301 basic medicineRadiation-Sensitizing AgentsPathologymedicine.medical_specialtyDNA End-Joining RepairRadiobiologyDNA repairDNA damageMorpholinesmedicine.medical_treatmentMice NudeUterine Cervical NeoplasmsDNA repairBreast NeoplasmsDNA-Activated Protein KinaseRadiation ToleranceMice03 medical and health sciences0302 clinical medicineCancer stem cellTumor Cells CulturedAnimalsHumansMedicineDNA Breaks Double-StrandedHomologous RecombinationDNA-PKcsdouble-strand breaksRadiotherapybusiness.industryCancerradiation oncologyHyperthermia Inducedhyperthermiamedicine.diseaseRadiation therapyradiation oncology.030104 developmental biologyOncologyChromones030220 oncology & carcinogenesisCancer cellNeoplastic Stem CellsCancer researchFemalebusinessResearch PaperDNA DamageOncotarget
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The endopolygalacturonase 1 from botrytis cinerea activates grapevine defense reactions unrelated to its enzyumatic activity

2003

A purified glycoprotein from Botrytis cinerea(strain T4), identified as endopolygalacturonase 1 (T4BcPG1) by mass spectrometry analysis, has been shown to activate defense reactions in grapevine (Vitis vinifera cv. Gamay). These reactions include calcium influx, production of active oxygen species, activation of two mitogen-activated protein kinases, defense gene transcript accumulation, and phytoalexin production. Most of these defense reactions were also activated in grapevine in response to purified oligogalacturonides (OGA) with a degree of polymerization of 9 to 20. In vivo, these active OGA might be a part of the released products resulting from endopolygalacturonase activity on plan…

elicitor; endopolygalacturonase 1; Botrytis cinerea; plant defenceplant defencePhysiologyMolecular Sequence DataOligosaccharidesBiologyCell wallBotrytis cinereaGene Expression Regulation PlantSequence Homology Nucleic Acid[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyVitisAmino Acid SequencePectinaseendopolygalacturonase 1ComputingMilieux_MISCELLANEOUSBotrytis cinereachemistry.chemical_classificationelicitorBase SequenceSequence Homology Amino AcidKinasePhytoalexinfood and beveragesGeneral MedicineHydrogen Peroxidebiology.organism_classificationImmunity InnateElicitorEnzyme ActivationEnzymePolygalacturonasechemistryBiochemistryCalciumBotrytisMitogen-Activated Protein KinasesGlycoproteinAgronomy and Crop Science
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Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases.

2008

The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced up-regulation of RAGE is involved in various pathophysiological processes, including late diabetic complications and Alzheimer disease. Application of recombinant soluble RAGE has been shown to block RAGE-mediated pathophysiological conditions. After expression of full-length RAGE in HEK cells we identified a 48-kDa soluble RAGE form (sRAGE) in the culture medium. This variant of RAGE is smaller than a 51-kDa soluble version derived from alternative splicing. The release of sRAGE can be induced by the phorbol ester PMA and the calcium ionophore c…

endocrine system diseasesADAM10Receptor for Advanced Glycation End ProductsMatrix Metalloproteinase InhibitorsHydroxamic AcidsBiochemistryProtein biotinylationCell LineDiabetes ComplicationsADAM10 ProteinGlycationAlzheimer DiseaseHumansProtein IsoformsProtease Inhibitorscardiovascular diseasesRNA Small InterferingReceptors ImmunologicReceptorMolecular BiologyProtein kinase CCalcimycinIonophoresChemistryHEK 293 cellsCell Membranenutritional and metabolic diseasesMembrane ProteinsCell BiologyProtein Structure TertiaryADAM ProteinsAlternative SplicingEctodomainBiochemistryMatrix Metalloproteinase 9cardiovascular systemCarcinogensImmunoglobulin superfamilyTetradecanoylphorbol AcetateAmyloid Precursor Protein Secretaseshuman activitiesThe Journal of biological chemistry
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Resveratrol post-transcriptionally regulates pro-inflammatory gene expression via regulation of KSRP RNA binding activity

2014

Resveratrol shows beneficial effects in inflammation-based diseases like cancer, cardiovascular and chronic inflammatory diseases. Therefore, the molecular mechanisms of the anti-inflammatory resveratrol effects deserve more attention. In human epithelial DLD-1 and monocytic Mono Mac 6 cells resveratrol decreased the expression of iNOS, IL-8 and TNF-α by reducing mRNA stability without inhibition of the promoter activity. Shown by pharmacological and siRNA-mediated inhibition, the observed effects are SIRT1-independent. Target-fishing and drug responsive target stability experiments showed selective binding of resveratrol to the RNA-binding protein KSRP, a central post-transcriptional regul…

endocrine system diseasesMRNA destabilizationRNA Stabilityp38 mitogen-activated protein kinasesGene ExpressionRNA-binding proteinResveratrolBiologyp38 Mitogen-Activated Protein KinasesMicechemistry.chemical_compoundCell Line TumorStilbenesGene expressionGeneticsAnimalsHumansddc:610RNA Messengerskin and connective tissue diseasesMice KnockoutMessenger RNAGene knockdownExosome Multienzyme Ribonuclease Complexorganic chemicalsAnti-Inflammatory Agents Non-SteroidalGene regulation Chromatin and EpigeneticsRNA-Binding Proteinsfood and beveragesMolecular biology3. Good healthCell biologychemistryResveratrolMutationTrans-ActivatorsPhosphorylationInflammation Mediatorshormones hormone substitutes and hormone antagonistsNucleic Acids Research
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Mechanisms involved in lipid accumulation and apoptosis induced by 1-nitropyrene in Hepa1c1c7 cells

2011

International audience; 1-Nitropyrene (1-NP) is a nitro-polycyclic aromatic hydrocarbon (nitro-PAH) present in diesel exhaust and bound to particular matter in urban air. We show that 1-NP and the referent PAH benzo(a)pyrene (BP) induce apoptosis and a lipid accumulation dependent on cytochrome P450 1A1-metabolites in mouse hepatoma cells, whereas 1-amino-pyrene had no effect. The caspase inhibitor, N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone (Z-VAD-fmk), inhibits 1-NP-induced apoptosis, but failed to alter 1-NP-triggered lipid accumulation determined by Nile red staining. We further show that cholesterol and fatty acid contents are modified after nitro-PAH exposure and that 1…

endoplasmic-reticulum stressMESH: PyrenesHepatoma cellsliver-cellsactivated protein-kinaseApoptosisAMP-Activated Protein KinasesToxicologyMESH: Liver Neoplasms ExperimentalMicechemistry.chemical_compoundMESH: CholesterolLiver Neoplasms ExperimentalMESH: AnimalsMESH: AMP-Activated Protein KinasesStearoyl-CoA desaturase 1CaspaseMESH: Lipid Metabolismchemistry.chemical_classificationhuman macrophages0303 health sciencesPyrenesbiology8-tetrachlorodibenzo-p-dioxin tcdd030302 biochemistry & molecular biologyGeneral Medicineinhibition[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]CholesterolBiochemistry[SDV.TOX]Life Sciences [q-bio]/ToxicologyCaspaseslipids (amino acids peptides and proteins)stearoyl-coaStearoyl-CoA DesaturaseMESH: Cell Line Tumor[SDV.BC]Life Sciences [q-bio]/Cellular Biology03 medical and health sciencesMESH: Benzo(a)pyreneCell Line Tumor1-NitropyreneBenzo(a)pyreneAnimalsFatty acidsProtein kinase AMESH: Mice030304 developmental biologyaromatic-hydrocarbonsMESH: CaspasesCholesterolMESH: Apoptosisc-srcFatty acidAMPKCytochrome P450Lipid MetabolismMolecular biologychemistryApoptosisMESH: Stearoyl-CoA Desaturasebiology.proteinStearoyl-CoA desaturase-1desaturaseToxicology Letters
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