Search results for " Post-Translational"

showing 10 items of 148 documents

Modeling Human Endometrial Decidualization from the Interaction between Proteome and Secretome

2011

Context: Decidualization of the human endometrium, which involves morphological and biochemical modifications of the endometrial stromal cells (ESCs), is a prerequisite for adequate trophoblast invasion and placenta formation. Objective: This study aims to investigate the proteome and secretome of in vitro decidualized ESCs. These data were combined with published genomic information and integrated to model the human decidualization interactome. Design: Prospective experimental case–control study. Setting: A private research foundation. Patients: Sixteen healthy volunteer ovum donors. Intervention: Endometrial samples were obtained, and ESCs were isolated and decidualized in vitro. Main Ou…

AdultProteomicsmedicine.medical_specialtyAdolescentProteomeEndocrinology Diabetes and MetabolismBlotting WesternClinical BiochemistryEnzyme-Linked Immunosorbent AssayBiologyProteomicsModels BiologicalBiochemistryInteractomeEndometriumYoung AdultEndocrinologyCytokines metabolismInternal medicineDeciduamedicineHumansCell shapeCell ShapeCells CulturedBiochemistry (medical)DeciduaComputational BiologyDecidualizationmedicine.anatomical_structureEndocrinologyPost translationalCase-Control StudiesCulture Media ConditionedSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomeCytokinesElectrophoresis Polyacrylamide GelFemaleStromal CellsProtein Processing Post-TranslationalBiomarkersThe Journal of Clinical Endocrinology & Metabolism
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Natural Proteolytic Processing of Hemofiltrate Cc Chemokine 1 Generates a Potent Cc Chemokine Receptor (Ccr)1 and Ccr5 Agonist with Anti-HIV Properti…

2000

Hemofiltrate CC chemokine (HCC)-1 is a recently described human chemokine that is constitutively expressed in numerous tissues and is present at high concentrations in normal plasma. Using a cell line expressing CC chemokine receptor (CCR)5 as a bioassay, we isolated from human hemofiltrate an HCC-1 variant lacking the first eight amino acids. HCC-1[9–74] was a potent agonist of CCR1, CCR3, and CCR5 and promoted calcium flux and chemotaxis of T lymphoblasts, monocytes, and eosinophils. It also blocked entry of HIV-1 strains using CCR5 as coreceptor. Limited tryptic digestion of HCC-1 generated the active variant. Conditioned media from several tumor cell lines activated HCC-1 with a high ef…

AdultReceptors CCR5Anti-HIV AgentsReceptors CCR3Molecular Sequence DataImmunologyReceptors CCR1C-C chemokine receptor type 6BiologyChemokine receptorEndopeptidasesHumansImmunology and AllergyCCL17Amino Acid SequenceCalcium SignalingCCL15CCL13endopeptidaseChemotactic FactorsHIVBlood ProteinsMolecular biologyPeptide FragmentsChemotaxis LeukocyteBiochemistryChemokines CCCulture Media ConditionedXCL2Biological AssayReceptors ChemokineOriginal ArticleCC chemokine receptorsProtein Processing Post-TranslationalCCL21Journal of Experimental Medicine
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Elevated Protein Content and Prolyl 4-Hydroxylase Activity in Severely Degenerated Human Annulus Fibrosus

2000

Alterations involved with the intervertebral disc degeneration are partly well described, however, it is not so well known how collagen network is affected by the disease. We analyzed the rate of collagen biosynthesis (estimated by the enzymic activities of prolyl 4-hydroxylase and galactosylhydroxylysyl glucosyltransferase) and the level of hydroxylysylpyridinoline and lysylpyridinoline crosslinks both in normal (n=7) and degenerated (n=7) human annulus fibrosus. The activity of prolyl 4-hydroxylase was significantly increased in degenerated tissue. However, no significant changes in the collagen content or in the amount of hydroxylysylpyridinoline and lysylpyridinoline collagen crosslinks…

Adultmedicine.medical_specialtyProcollagen-Proline DioxygenaseDegeneration (medical)BiochemistryProtein content03 medical and health sciences0302 clinical medicineRheumatologyInternal medicineCollagen networkmedicineHumansOrthopedics and Sports MedicineAmino AcidsIntervertebral DiscMolecular Biology030304 developmental biologyAnnulus (mycology)0303 health sciencesChemistryProteinsIntervertebral discCell BiologyMiddle Agedmusculoskeletal systemGalactosylhydroxylysyl glucosyltransferaseCollagen biosynthesisHydroxyprolineCollagen type I alpha 1Endocrinologymedicine.anatomical_structureBiochemistrySpinal DiseasesCollagenProtein Processing Post-Translational030217 neurology & neurosurgeryConnective Tissue Research
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Assessment of determinants affecting the dual topology of hepadnaviral large envelope proteins

2004

For functional diversity, the large (L) envelope protein of hepatitis B virus (HBV) acquires a dual transmembrane topology via co-translational membrane integration of the S region and partial post-translational translocation of the preS subdomain. Because each process requires the second transmembrane segment (TM2), we explored the action of this determinant by using protease protection analysis of mutant L proteins. We demonstrated that neither the disruption of a leucine zipper-like motif by multiple alanine substitutions nor the flanking charges of TM2 affected the topological reorientation of L. The dispensability of both putative subunit interaction modules argues against a link betwe…

AlanineHepatitis B virusHepatitis B virusVirus AssemblyAmino Acid MotifsMolecular Sequence DataProtein domainPhenotype mixingBiological TransportBiologyEndoplasmic Reticulummedicine.disease_causeVirologyTransmembrane domainDual topologyAmino Acid SubstitutionViral Envelope ProteinsVirologyMembrane topologymedicineHepadnavirusAmino Acid SequenceProtein Processing Post-TranslationalJournal of General Virology
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Phosphorylation of serine residues is fundamental for the calcium-binding ability of Orchestin, a soluble matrix protein from crustacean calcium stor…

2003

International audience; Orchestia cavimana is a terrestrial crustacean, which cyclically stores calcium in diverticula of the midgut, in the form of calcified amorphous concretions. These concretions are associated with a proteinaceous matrix, the main constituent of the soluble matrix is Orchestin, an acidic calcium-binding protein [Testenière et al., Biochem. J. 361 (2002) 327-335]. In the present paper, we clearly demonstrate that Orchestin is phosphorylated on serine and tyrosine residues, but that calcium binding only occurs via the phosphoserine residues. To our knowledge, this is the first example of an invertebrate mineralization for which a post-translational modification is clearl…

BiomineralizationMESH: Amino Acid SequenceMESH: Calcium-Binding ProteinsMatrix (biology)01 natural sciencesBiochemistryCalcium in biologyMESH: TyrosineSerinechemistry.chemical_compoundMESH: Structure-Activity RelationshipStructural BiologyCrustaceaSerineElectrophoresis Gel Two-DimensionalMESH: AnimalsTyrosinePhosphorylation0303 health sciencesBiochemistryMESH: CalciumPhosphorylationElectrophoresis Polyacrylamide GelOrganic matrixProtein BindingMolecular Sequence DataBiophysicschemistry.chemical_elementCrustaceanCalciumBiology010402 general chemistryMESH: Calcification Physiologic03 medical and health sciencesStructure-Activity RelationshipCalcification PhysiologicMESH: CrustaceaGeneticsAnimalsMESH: Protein Binding[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMESH: SerineMolecular Biology030304 developmental biologyCalcium metabolismMESH: Molecular Sequence DataMESH: PhosphorylationCalcium-Binding ProteinsCell BiologyMESH: Electrophoresis Gel Two-Dimensional0104 chemical scienceschemistryPhosphoserineMESH: Protein Processing Post-TranslationalTyrosineCalciumCalcium bindingProtein Processing Post-TranslationalMESH: Electrophoresis Polyacrylamide Gel
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Phosphorylation of cytochromes P450: First discovery of a posttranslational modification of a drug-metabolizing enzyme

2005

Cytochromes P450 (CYP) are important components of xenobiotic-metabolizing monooxygenases (CYP-dependent monooxygenases). Their regulation by induction, most commonly by transcriptional activation, mediated by xenobiotics, normally substrates of the corresponding CYP, is well known and has been widely studied. Our team has discovered an additional important regulation of xenobiotic-metabolizing CYPs pertaining to posttranslational modification by phosphorylation. Individual CYPs are phosphorylated by different protein kinases, leading to CYP isoenzyme-selective changes in the metabolism of individual substrates and consequent drastic changes in the control of genotoxic metabolites. Best stu…

Biophysicsurologic and male genital diseasesBiochemistryCytochrome P-450 Enzyme SystemAnimalsHumansheterocyclic compoundsPhosphorylationEnzyme inducerProtein kinase AMolecular BiologyTranscription factorRegulation of gene expressionbiologyKinaseorganic chemicalsCell Biologyrespiratory systemMonooxygenaseenzymes and coenzymes (carbohydrates)LiverBiochemistrybiology.proteinPhosphorylationProtein Processing Post-TranslationalNuclear localization sequenceMutagensBiochemical and Biophysical Research Communications
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Cleavage of endometrial α-integrins into their functional forms is mediated by proprotein convertase 5/6.

2012

Background Proprotein convertases (PCs) post-translationally activate a large number of protein precursors through limited cleavage. PC5/6 (PC6) in the human endometrium is tightly regulated during receptivity for embryo implantation. Integrins are transmembrane glycoproteins, some of which play an important role in the adhesive interactions between the trophoblast (blastocyst) and uterine epithelium at implantation. Integrins require PC cleavage for post-translational modification. We hypothesize that pro-integrin-αs in the endometrial epithelium are post-translationally cleaved by PC6 into functional subunits for the binding of blastocyst and adhesion of extracellular matrix proteins. Met…

BiopsyIntegrinCleavage (embryo)Gene Expression Regulation EnzymologicEndometriumPregnancymedicineCell AdhesionHumansBlastocystEmbryo ImplantationCell adhesionCells CulturedGlycoproteinsbiologyRehabilitationObstetrics and GynecologyTrophoblastTransfectionMolecular biologyFibronectinsFibronectinmedicine.anatomical_structureBlastocystReproductive Medicinebiology.proteinProprotein Convertase 5CalciumFemaleProprotein ConvertasesIntegrin alpha ChainsProtein Processing Post-TranslationalHuman reproduction (Oxford, England)
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The histone deacetylase sirtuin 2 is a new player in the regulation of platelet function

2015

SummaryBackground Histone deacetylases (HDACs) play a key role in signaling in many cell types. However, little is known about the participation of HDACs, particularly sirtuins (SIRTs), in platelet reactivity. Objective To investigate the role of HDACs in platelets, we examined the effects of SIRT inhibition on platelet function and protein acetylation in human platelets. Methods We used washed platelets obtained from healthy subjects. Cambinol (SIRT1 and SIRT2 inhibitor), AGK2 (specific SIRT2 inhibitor) and EX527 (specific SIRT1 inhibitor) were used as SIRT inhibitors. Platelets were stimulated with collagen, thrombin, or U46619, and platelet responses were determined according to optical …

Blood PlateletsPlatelet AggregationCytoplasmic GranulesSIRT2Glycogen Synthase Kinase 3Akt3 protein kinaseSirtuin 2sirtuinsHumansPlateletRNA MessengerPhosphorylationProtein kinase Bacetylationblood plateletGlycogen Synthase Kinase 3 betabiologySecretory VesiclesAcetylationHematologyCell biologyHistone Deacetylase InhibitorsBiochemistryAcetylationSirtuinbiology.proteinPhosphorylationPlatelet aggregation inhibitorCalciumHistone deacetylaseProtein Processing Post-TranslationalProto-Oncogene Proteins c-aktPlatelet Aggregation Inhibitorssignal transductionSignal TransductionJournal of Thrombosis and Haemostasis
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Deciphering of ADP-induced, phosphotyrosine-dependent signaling networks in human platelets by Src-homology 2 region (SH2)-profiling.

2012

Tyrosine phosphorylation plays a central role in signal transduction controlling many important biological processes. In platelets, the activity of several signaling proteins is controlled by tyrosine phosphorylation ensuring proper platelet activation and aggregation essential for regulation of the delicate balance between bleeding and hemostasis. Here, we applied Src-homology 2 region (SH2)-profiling for deciphering of the phosphotyrosine state of human platelets activated by adenosine diphosphate (ADP). Applying a panel of 31 SH2-domains, rapid and complex regulation of the phosphotyrosine state of platelets was observed after ADP stimulation. Specific inhibition of platelet P2Y receptor…

Blood PlateletsProtein tyrosine phosphataseSH2 domainBiochemistryReceptor tyrosine kinasePhosphorylation cascadesrc Homology Domainschemistry.chemical_compoundReceptors Purinergic P2Y1Tandem Mass SpectrometryHumansProtease-activated receptorProtein phosphorylationIloprostPhosphorylationPhosphotyrosineMolecular BiologybiologyTyrosine phosphorylationPlatelet ActivationCyclic AMP-Dependent Protein KinasesAdenosine MonophosphateReceptors Purinergic P2Y12Cell biologyAdenosine DiphosphateEnzyme ActivationBiochemistrychemistrybiology.proteinPurinergic P2Y Receptor AntagonistsPhosphorylationProtein Processing Post-TranslationalSignal TransductionProteomics
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Molecular Proteomics and Signalling of Human Platelets in Health and Disease

2021

Platelets are small anucleate blood cells that play vital roles in haemostasis and thrombosis, besides other physiological and pathophysiological processes. These roles are tightly regulated by a complex network of signalling pathways. Mass spectrometry-based proteomic techniques are contributing not only to the identification and quantification of new platelet proteins, but also reveal post-translational modifications of these molecules, such as acetylation, glycosylation and phosphorylation. Moreover, target proteomic analysis of platelets can provide molecular biomarkers for genetic aberrations with established or non-established links to platelet dysfunctions. In this report, we review …

Blood PlateletsProteomicsADPProteomeQH301-705.5receptorsProstacyclinReviewPROTEIN-COMPOSITIONProteomicsCatalysisInorganic ChemistryThromboxane A2chemistry.chemical_compoundThrombinREVEALSGPVImedicineHumansSYKPlateletPlatelet activationPhysical and Theoretical ChemistrysignallingBiology (General)Molecular BiologyQD1-999SpectroscopyNITRIC-OXIDEChemistryOrganic ChemistryACTIVATED PLATELETSPATHWAYSGLOBAL PROTEOMEGeneral MedicinePlatelet ActivationproteinsComputer Science ApplicationsCell biologyChemistrypost-translational modificationProteomeplateletsBlood Platelet DisordersGPVIProtein Processing Post-TranslationalSignal Transductionmedicine.drugInternational Journal of Molecular Sciences
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