Search results for "Calmodulin"

showing 10 items of 83 documents

Proteomic signature of the Dravet syndrome in the genetic Scn1a-A1783V mouse model.

2021

Abstract Background Dravet syndrome is a rare, severe pediatric epileptic encephalopathy associated with intellectual and motor disabilities. Proteomic profiling in a mouse model of Dravet syndrome can provide information about the molecular consequences of the genetic deficiency and about pathophysiological mechanisms developing during the disease course. Methods A knock-in mouse model of Dravet syndrome with Scn1a haploinsufficiency was used for whole proteome, seizure, and behavioral analysis. Hippocampal tissue was dissected from two- (prior to epilepsy manifestation) and four- (following epilepsy manifestation) week-old male mice and analyzed using LC-MS/MS with label-free quantificati…

MaleProteomics0301 basic medicineProteomeHippocampusEpilepsies MyoclonicHaploinsufficiencyScn1aHippocampusSynaptic TransmissionElevated Plus Maze TestEpilepsyMice0302 clinical medicineTandem Mass Spectrometry11-beta-Hydroxysteroid Dehydrogenase Type 1Genetic epilepsyCarbon-Nitrogen LigasesGene Knock-In TechniquesGliosisNeuronal PlasticityBehavior AnimalEpileptic encephalopathyImmunohistochemistryAstrogliosisNeurologyProteomeDisease ProgressionFemaleHaploinsufficiencySignal TransductionRC321-571Dopamine and cAMP-Regulated Phosphoprotein 32Neovascularization PhysiologicNeurosciences. Biological psychiatry. NeuropsychiatryBiologyNitric Oxide03 medical and health sciencesDravet syndromemedicineAnimalsHyperthermiaSocial Behaviorras-GRF1Proteomic Profilingmedicine.diseaseVascular Endothelial Growth Factor Receptor-2NAV1.1 Voltage-Gated Sodium ChannelDisease Models Animal030104 developmental biologyRotarod Performance TestSynaptic plasticityEpileptic Encephalopathy ; Genetic Epilepsy ; Mice ; Proteome ; Scn1aCalcium-Calmodulin-Dependent Protein Kinase Type 2Open Field TestNeuroscience030217 neurology & neurosurgeryChromatography Liquid
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Constitutive Promoter Occupancy by the MBF-1 Activator and Chromatin Modification of the Developmental Regulated Sea Urchin α-H2A Histone Gene

2007

The tandemly repeated sea urchin alpha-histone genes are developmentally regulated. These genes are transcribed up to the early blastula stage and permanently silenced as the embryos approach gastrulation. As previously described, expression of the alpha-H2A gene depends on the binding of the MBF-1 activator to the 5' enhancer, while down-regulation relies on the functional interaction between the 3' sns 5 insulator and the GA repeats located upstream of the enhancer. As persistent MBF-1 binding and enhancer activity are detected in gastrula embryos, we have studied the molecular mechanisms that prevent the bound MBF-1 from trans-activating the H2A promoter at this stage of development. Her…

Embryo Nonmammaliananimal structuresRestriction MappingMBF-1Down-RegulationEnhancer RNAschromatin immunoprecipitationBiologyHistone DeacetylasesactivatorHistonesHistone H3Histone H1Structural BiologyHistone H2AHistone methylationAnimalsNucleosomeHistone codenucleosome phasingPromoter Regions GeneticEnhancerBase PairingMolecular Biologyhistone modificationsGene Expression Regulation DevelopmentalGastrulaMolecular biologyChromatinNucleosomesRepressor ProteinsMutagenesis InsertionalEnhancer Elements GeneticSea Urchinsembryonic structuresTrans-ActivatorsCalmodulin-Binding ProteinsInsulator Elementssea urchin histone geneProtein Processing Post-TranslationalProtein BindingJournal of Molecular Biology
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Angiotensin-Converting Enzyme Inhibitor Ramiprilat Interferes With the Sequestration of the B 2 Kinin Receptor Within the Plasma Membrane of Native E…

1999

Background —ACE (kininase II) inhibitors have been shown to exert their beneficial cardiovascular effects via the inhibition of both angiotensin II formation and bradykinin breakdown. Because recent evidence suggests that ACE inhibitors may also interfere with B 2 kinin receptor signaling and thus enhance the vascular response to bradykinin, we examined whether the distribution of B 2 kinin receptors within the plasma membrane of native endothelial cells is affected by an ACE inhibitor. Methods and Results —Localization of the B 2 kinin receptor in membranes prepared from native porcine aortic endothelial cells was evaluated by means of specific [ 3 H]bradykinin binding and immunoprecipita…

medicine.medical_specialtyReceptor Bradykinin B2SwineBradykininAngiotensin-Converting Enzyme InhibitorsPharmacologyBradykininchemistry.chemical_compoundRamiprilPhysiology (medical)Internal medicinemedicineAnimalsCalcium SignalingBradykinin receptorReceptorAortaMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyReceptors BradykininMembrane ProteinsBiological TransportAngiotensin-converting enzymeKininAngiotensin IIEndothelial stem cellEndocrinologychemistryCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinEndothelium VascularMitogen-Activated Protein KinasesCardiology and Cardiovascular MedicineRamiprilatSignal TransductionCirculation
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Characterization of a Ryanodine Receptor inPeriplaneta Americana

1997

Specific binding sites for the alkaloid ryanodine were characterized in membrane preparations from sarcoplasmatic reticulum of Periplaneta americana skeletal muscle. Binding of [3H]ryanodine was optimal at pH 8 and at CaCl2 concentration of about 300 mumol l-1. The Ca-chelating agents EGTA (100 mumol l-1) and EDTA (100 mumol l-1) abolished 95% and 90% of the [3H]ryanodine binding respectively. Preincubation with Ca2+ (100 mumol l-1) restored the ryanodine binding in presence of up to 300 mumol l-1 EGTA. Radioligand binding experiments showed one class of high affinity binding sites for ryanodine. Determination of rate constants revealed 7.05 x 10(6) l mol-1 min-1 for associating and 3.77 x …

Maleanimal structuresMuscle ProteinsBiochemistrymedicineAnimalsPeriplanetaheterocyclic compoundsBinding siteEgtazic AcidMolecular BiologyEdetic AcidbiologyRyanodineRyanodine receptorChemistryMusclesAlkaloidSodiumfungiSkeletal muscleRyanodine Receptor Calcium Release ChannelCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationmedicine.anatomical_structureBiochemistryPotassiumCalciumCalmodulin-Binding ProteinsFemaleCalcium ChannelsReticulumPeriplanetaJournal of Receptors and Signal Transduction
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Calcium/calmodulin-dependent protein kinases in the carotid body: an immunohistochemical study

2012

We determined the presence of Ca(2+)/calmodulin-dependent protein kinases (CaMKs), a family of multifunctional proteins engaged in Ca(2+)-linked signaling, in carotid body chemoreceptor cells which are critical for the hypoxia-sensing. Carotid bodies were dissected from anesthetized normoxic adult Wistar rats and were double stained for individual CaMKs and for tyrosine hydroxylase (TH), a marker of chemoreceptor cells. Immunofluorescence was examined by confocal laser scanning microscopy. We found that CaMKI and CaMKII were expressed in chemoreceptor cells, but their distribution and intensity varied. CaMKI immunoreactivity was distributed throughout the cytoplasm, whereas that of CaMKII w…

Calcium-Calmodulin-Dependent Protein KinasesPathologymedicine.medical_specialtyMultidisciplinarymedicine.diagnostic_testTyrosine hydroxylaseKinaseResearchBiologyImmunofluorescenceChemoreceptor cellsCell biologyCarotid bodymedicine.anatomical_structurenervous systemCytoplasmCa2+/calmodulin-dependent protein kinaseCa2+/calmodulin-dependent protein kinasecardiovascular systemmedicineImmunohistochemistryCarotid bodyhuman activitiescirculatory and respiratory physiologySpringerPlus
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The structural plasticity of the C terminus of p21Cip1 is a determinant for target protein recognition.

2003

The cyclin-dependent kinase inhibitory protein p21(Cip1) might play multiple roles in cell-cycle regulation through interaction of its C-terminal domain with a defined set of cellular proteins such as proliferating cell nuclear antigen (PCNA), calmodulin (CaM), and the oncoprotein SET. p21(Cip1) could be described as an intrinsically unstructured protein in solution although the C-terminal domain adopts a well-defined extended conformation when bound to PCNA. However, the molecular mechanism of the interaction with CaM and the oncoprotein SET is not well understood, partly because of the lack of structural information. In this work, a peptide derived from the C-terminal domain of p21(Cip1) …

Cyclin-Dependent Kinase Inhibitor p21Models MolecularMagnetic Resonance SpectroscopyCalmodulinChromosomal Proteins Non-HistoneProtein ConformationPeptideBiologyLigandsBiochemistryBinding CompetitiveDomain (software engineering)Molecular recognitionCalmodulinCyclinsProliferating Cell Nuclear AntigenEscherichia coliHumansHistone ChaperonesMolecular Biologychemistry.chemical_classificationC-terminusCircular DichroismOrganic ChemistryCell CycleProteinsPeptide FragmentsCell biologyDNA-Binding ProteinschemistryBiochemistrybiology.proteinMolecular MedicineTarget proteinAlpha helixBinding domainTranscription FactorsChembiochem : a European journal of chemical biology
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NO signaling in cryptogein-induced immune responses in tobacco

2014

SPEIPM; International audience

CalmodulinTobacco[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyCryptogeinCalciumNitric oxidePAMPplant immunityNO
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p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
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A role for the MAP kinase gene MKC1 in cell wall construction and morphological transitions in Candida albicans.

1998

The Candida albicans MKC1 gene encodes a mitogen-activated protein (MAP) kinase, which has been cloned by complementation of the lytic phenotype associated with Saccharomyces cerevisiae slt2 (mpk1) mutants. In this work, the physiological role of this MAP kinase in the pathogenic fungus C. albicans was characterized and a role for MKC1 in the biogenesis of the cell wall suggested based on the following criteria. First, C. albicans mkc1Δ/mkc1Δ strains displayed alterations in their cell surfaces under specific conditions as evidenced by scanning electron microscopy. Second, an increase in specific cell wall epitopes (O-glycosylated mannoprotein) was shown by confocal microscopy in mkc1Δ/mkc1…

Antifungal AgentsTranscription GeneticSaccharomyces cerevisiaeMutantMAP Kinase Kinase 2MAP Kinase Kinase 1ChitinSaccharomyces cerevisiaeProtein Serine-Threonine KinasesMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsPseudohyphal growthCell WallGene Expression Regulation FungalCandida albicansCandida albicansDNA FungalFluorescent Antibody Technique IndirectGlucansProtein Kinase CMitogen-Activated Protein Kinase KinasesRecombination GeneticMembrane GlycoproteinsMicroscopy ConfocalbiologyKinaseProtein-Tyrosine Kinasesbiology.organism_classificationFlow Cytometrybeta-GalactosidaseCorpus albicansComplementationMicroscopy ElectronBiochemistryMitogen-activated protein kinaseCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMicroscopy Electron ScanningMitogen-Activated Protein KinasesPlasmidsMicrobiology (Reading, England)
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rhoB encoding a UV-inducible Ras-related small GTP-binding protein is regulated by GTPases of the Rho family and independent of JNK, ERK, and p38 MAP…

1998

The small GTPase RhoB is immediate-early inducible by DNA damaging treatments and thus part of the early response of eukaryotic cells to genotoxic stress. To investigate the regulation of this cellular response, we isolated the gene for rhoB from a mouse genomic library. Sequence analysis of the rhoB gene showed that its coding region does not contain introns. The promoter region of rhoB harbors regulatory elements such as TATA, CAAT, and Sp1 boxes but not consensus sequences for AP-1, Elk-1, or c-Jun/ATF-2. The rhoB promoter was activated by UV irradiation, but not by 12-O-tetradecanoylphorbol-13-acetate treatment. rhoB promoter deletion constructs revealed a fragment of 0.17 kilobases in …

Ultraviolet RaysRHOBMolecular Sequence DataMAP Kinase Kinase Kinase 1BiologyProtein Serine-Threonine KinasesBiochemistryp38 Mitogen-Activated Protein KinasesGTP PhosphohydrolasesWortmanninchemistry.chemical_compoundMiceGTP-Binding ProteinsRhoB GTP-Binding ProteinAnimalsCloning MolecularEnzyme InhibitorsPromoter Regions GeneticrhoB GTP-Binding ProteinMolecular BiologyPhosphoinositide-3 Kinase InhibitorsMAP kinase kinase kinaseBase SequenceKinaseMEK inhibitorJNK Mitogen-Activated Protein KinasesMembrane ProteinsCell BiologyMolecular biologychemistryMitogen-activated protein kinaseCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinras ProteinsSignal transductionMitogen-Activated Protein KinasesThe Journal of biological chemistry
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