Search results for "Marck"

showing 9 items of 19 documents

Role of calcineurin in Ca2+-induced release of catecholamines and neuropeptides

1998

Neurotransmission requires rapid docking, fusion, and recycling of neurotransmitter vesicles. Several of the proteins involved in this complex Ca2+-regulated mechanism have been identified as substrates for protein kinases and phosphatases, e.g., the synapsins, synaptotagmin, rabphilin3A, synaptobrevin, munc18, MARCKS, dynamin I, and B-50/GAP-43. So far most attention has focused on the role of kinases in the release processes, but recent evidence indicates that phosphatases may be as important. Therefore, we investigated the role of the Ca2+/calmodulin-dependent protein phosphatase calcineurin in exocytosis and subsequent vesicle recycling. Calcineurin-neutralizing antibodies, which blocke…

MaleSynaptobrevinCYCLOSPORINE-APhosphataseCalcineurin InhibitorsB-50 GAP-43Biologydynamin IBiochemistryBRAIN NERVE-TERMINALSExocytosisSynaptotagmin 1SincalidephosphataseGeneeskundeCellular and Molecular NeuroscienceNorepinephrineBacterial ProteinsPERMEATED SYNAPTOSOMESAnimalsratNEUROTRANSMITTER RELEASEMARCKSEnzyme InhibitorsRats WistarPROTEIN-KINASE-CDynaminCalcineurinTRANSMITTER RELEASEDYNAMIN-ISynapsinPhosphoric Monoester HydrolasesRatsINDUCED NORADRENALINE RELEASECalcineurinBiochemistryImmunoglobulin GStreptolysinsCalciumexocytosisCALMODULIN-BINDINGSynaptosomes
researchProduct

PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

1996

AbstractThe 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

PhosphopeptidesMARCKSPRKRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsKidneyBiochemistryCell-free systemCell LineSerineStructural BiologyProtein kinase CGeneticsAnimalsAmino Acid SequenceBinding siteMARCKSPKCPhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateMolecular BiologyProtein kinase CGlutathione TransferaseBinding SitesCell-Free SystemKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsCell BiologyHaplorhiniPeptide FragmentsBiochemistryPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionSequence AnalysisSignal TransductionFEBS Letters
researchProduct

Fosildiagénesis del anélido Rotularia spirulaea (Lamarck, 1818) (Polychaeta, Serpulidae) en el Eoceno del dominio pirenaico occidental

2018

UNESCO::CIENCIES DE LA VIDA:CIENCIES DE LA VIDA [UNESCO]Fosildiagénesis del anélido Rotularia spirulaea (Lamarck 1818) (Polychaeta Serpulidae) en el Eoceno del dominio pirenaico occidental Artículo
researchProduct

The 3'-UTR of the mRNA coding for the major protein kinase C substrate MARCKS contains a novel CU-rich element interacting with the mRNA stabilizing …

2003

The expression of the major protein kinase C substrate MARCKS (myristoylated alanine-rich C kinase substrate) is controlled by the stability of its mRNA. While the MARCKS mRNA is long living in quiescent fibroblasts (t1/2 = 14 h), its half-life time is drastically reduced (t1/2 = 2 h) in cells treated with phorbol esters to activate protein kinase C (PKC) or treated with growth factors. In a first step to study the underlying mechanism we identified both a cis-element on the MARCKS mRNA and the corresponding trans-acting factors. Fusing the complete 3'-UTR or specific regions of the 3'-UTR of the MARCKS gene to a luciferase reporter gene caused a drastic decrease in luciferase expression to…

Untranslated regionRecombinant Fusion ProteinsELAV-Like Protein 1Down-RegulationNerve Tissue ProteinsELAV-Like Protein 4BiologyBiochemistryELAV-Like Protein 1MiceGenes ReporterAnimalsRNA MessengerMARCKSLuciferasesMyristoylated Alanine-Rich C Kinase Substrate3' Untranslated RegionsProtein Kinase CProtein kinase CAU-rich elementMessenger RNAThree prime untranslated regionIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsRNA-Binding Proteins3T3 CellsFibroblastsMolecular biologyELAV ProteinsAntigens SurfaceMARCKS GeneEuropean Journal of Biochemistry
researchProduct

The Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is Sequentially Phosphorylated by Conventional, Novel and Atypical Isotypes of Protein Kin…

1995

The myristoylated alanine-rich C-kinase substrate (MARCKS) is the major protein kinase C (PKC) substrate in many cell types including fibroblasts and brain cells. Here we describe the phosphorylation of MARCKS and the site specificity for different PKC isotypes. Conventional (c)PKC beta 1, novel (n)PKC delta and nPKC epsilon efficiently phosphorylated the MARCKS protein in vitro. The Km values were extremely low, reflecting a high affinity between kinases and substrate. The apparent affinity of nPKC delta (Km = 0.06 microM) was higher than that of nPKC epsilon and cPKC beta 1 (Km = 0.32 microM). The rate of substrate phosphorylation was inversely correlated with affinity and decreased in th…

inorganic chemicalsKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsContext (language use)macromolecular substancesenvironment and public healthBiochemistryMolecular biologyCell biologyIsoenzymesSerineKineticsenzymes and coenzymes (carbohydrates)Substrate-level phosphorylationbacteriaPhosphorylationPhosphorylationMARCKSMyristoylated Alanine-Rich C Kinase SubstrateProtein Kinase CProtein kinase CMyristoylationEuropean Journal of Biochemistry
researchProduct

Moraaliset tunteet ja maltillinen subjektivismi Edvard Westermarckin relativistisessa etiikan teoriassa

2002

kritiikkiWestermarck Edvardarvojen objektivointitunteeteettinen relativismievolutionistinen etiikkamaltillinen subjektivismimoraaliset tunteetetiikkaarvotuskonnollisen etiikan kritiikki
researchProduct

Sentimentalismi ja virheteoria Edvard Westermarckin moraalifilosofiassa

2015

Tutkimuksen tarkoituksena on selvittää voidaanko Edvard Westermarckin moraalifilosofiaa käsitellä nykyisessä metaetiikassa virheteorian ja sentimentalismin näkökulmasta. Tärkeäksi valitun näkökulman tekee se, että erityisesti Westermarckin esittämään virheteoriaan on kiinnitetty vähän huomiota. Sentimentalismin ja virheteorian käsittelyn lisäksi selvennän Westermarckin käsitystä subjektivismista ja relativismista, sillä Westermarckin on katsottu edustavan yksinkertaista subjektivismia tai kestämätöntä relativismia. Väitän, että nämä käsitykset ovat hänen moraalifilosofiasta riittämättömiä. Argumentoin Westermarckiin kohdistuneen kritiikin perustuvan pääosin väärinymmärrykselle tai virheelli…

metaetiikkavirheteoriasubjektivismimoraaliWestermarck Edvardantirealismietiikkarelativismi
researchProduct

Tiedolla vaikuttaja

2018

moraalifilosofiakirja-arvostelutosaelämäkerratWestermarck Edvardpsykologiatutkimushistoriaetiikkasosiaaliantropologiaelämäkerrat
researchProduct

Du vol des oiseaux à l'évolution des espèces animales

2013

National audience; Étienne-Jules Marey se range du côté des partisans de l’évolution des espèces expliquée par le transformisme (1809) de Jean-Baptiste Lamarck (1744-1829). Marey déplore cependant que Lamarck demeure « beaucoup trop vague dans ses explications lorsqu’il attribue les changements des organismes vivants à des circonstances extérieures. Entre un besoin qui se révèle et l’apparition d’une forme organique qui corresponde à un besoin, il y a une lacune que sa théorie n’a pas comblée » . D’où chez Marey, des interrogations et le désir dans son champ de compétences de relever quelques faits avérés de transformations d’adaptation des êtres vivants à de nouvelles conditions de vie.

évolution des espècesJean-Baptiste Lamarck[SHS.INFO]Humanities and Social Sciences/Library and information sciencesEtienne-Jules Marey[ SHS.INFO ] Humanities and Social Sciences/Library and information sciences[SHS.INFO] Humanities and Social Sciences/Library and information sciences
researchProduct