Search results for "Phosphopeptide"

showing 3 items of 13 documents

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
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Milk versus caseinophosphopeptides added to fruit beverage: Resistance and release from simulated gastrointestinal digestion

2010

The influence of simulated gastrointestinal digestion on caseinophosphopeptides (CPPs) formation in milk-based fruit beverage was evaluated, together with resistance of a pool of CPPs added to fruit beverage. In milk-based fruit beverage, four CPPs were identified that can be justified by their presence in raw milk or due to processing. When it was subjected to simulated gastrointestinal digestion, 10 CPPs were identified, and only 1 presented the cluster (SpSpSpEE) (3 phosphoseryl group followed by 2 glutamic acid residues), which corresponded to αs2-CN(1-19)4P. CPPs added to fruit beverage are resistant to simulated gastrointestinal digestion, and 16 CPPs were identified originating from …

PhosphopeptidesPhysiologyChemistryFruit drinksMolecular Sequence DataCaseinsfood and beveragesRaw milkBiochemistryPeptide FragmentsGastrointestinal digestionBeveragesGastrointestinal TractCellular and Molecular NeuroscienceMilkEndocrinologyMineral bioavailabilityMilk productsFruitAnimalsHumansDigestionAmino Acid SequenceFood scienceDigestion
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Correlations in palmitoylation and multiple phosphorylation of rat bradykinin B2 receptor in Chinese hamster ovary cells.

1999

Rat bradykinin B2 receptor from unstimulated Chinese hamster ovary cells transfected with the corresponding cDNA has been isolated, and subsequent mass spectrometric analysis of multiple phosphorylated species and of the palmitoylation attachment site is described. Bradykinin B2 receptor was isolated on oligo(dT)-cellulose using N-(epsilon-maleimidocaproyloxy)succinimide-Met-Lys-bradykinin coupled to a protected (dA)30-mer. This allowed a one-step isolation of the receptor on an oligo(dT)-cellulose column via variation solely of salt concentration. After enzymatic in-gel digestion, matrix-assisted laser desorption ionization and electrospray ion trap mass spectrometric analysis of the isola…

PhosphopeptidesReceptor Bradykinin B2AcylationMolecular Sequence DataPalmitatesCHO CellsTransfectionBiochemistryMass SpectrometryCell membranePhosphoserinePalmitoylationCricetinaemedicineAnimalsTrypsinAmino Acid SequenceBradykinin receptorPhosphorylationReceptorPhosphotyrosineMolecular BiologyChemistryChinese hamster ovary cellReceptors BradykininCell BiologyTransfectionPeptide FragmentsRatsmedicine.anatomical_structurePhosphothreonineBiochemistryPhosphorylationSignal transductionProtein Processing Post-TranslationalThe Journal of biological chemistry
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