Search results for " post-translational"

showing 10 items of 148 documents

The N-glycan processing in HT-29 cells is a function of their state of enterocytic differentiation. Evidence for an atypical traffic associated with …

1991

International audience; When the human colon cancer cells HT-29 undergo enterocytic differentiation, they correctly process their N-glycans, whereas their undifferentiated counterpart are unable to process Man9-8-GlcNAc2 species, the natural substrate of alpha-mannosidase I. As this enzyme is fully active in both HT-29 cell populations, we hypothesize that N-glycoproteins are unable to reach the cis Golgi, the site where alpha-mannosidase I has been localized. We have demonstrated this point by using 1-deoxymannojirimycin, leupeptin, and monensin. In the presence of 1-deoxymannojirimycin, a specific inhibitor of alpha-mannosidase I, differentiated HT-29 cells, as expected, accumulate Man9-8…

Proteases1-DeoxynojirimycinColonLeupeptinsCellular differentiationCellIn Vitro TechniquesBiologyBiochemistry03 medical and health sciencessymbols.namesakechemistry.chemical_compoundPolysaccharidesalpha-Mannosidase[ CHIM.ORGA ] Chemical Sciences/Organic chemistryMannosidasesTumor Cells CulturedmedicineHumansMonensinMolecular Biology030304 developmental biologychemistry.chemical_classificationGlucosamine0303 health sciencesMembrane Glycoproteins[CHIM.ORGA]Chemical Sciences/Organic chemistryEndoplasmic reticulum030302 biochemistry & molecular biologyLeupeptinBiological TransportCell DifferentiationCell BiologyCompartment (chemistry)Golgi apparatus[CHIM.ORGA] Chemical Sciences/Organic chemistrymedicine.anatomical_structureBiochemistrychemistryColonic NeoplasmssymbolsGlycoproteinProtein Processing Post-Translational
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Heat shock proteins in hematopoietic malignancies

2012

Inducible heat shock proteins are molecular chaperones whose expression is increased after many different types of stress. They have a protective function helping the cell to cope with lethal conditions. Their basal expression is low in nonstressed, normal and nontransformed cells. However, in cancer cells and particularly in hematological malignancies, they are surprisingly abundant. Malignant cells have to rewire their metabolic requirements and therefore have a higher need for chaperones. This cancer cell addiction for HSPs is the basis for the use of HSP inhibitors in cancer therapy. HSPs have been shown to interact with different key apoptotic proteins. As a result, HSPs can essentiall…

ProteasesCell SurvivalCellular differentiationCellHSP27 Heat-Shock ProteinsApoptosisModels Biological03 medical and health sciences0302 clinical medicineHeat shock proteinmedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHeat-Shock ProteinsCaspaseCell Proliferation030304 developmental biology0303 health sciencesbiologyCell DifferentiationCell BiologyNeoplasm Proteins3. Good healthCell biologyHaematopoiesismedicine.anatomical_structureApoptosisHematologic NeoplasmsMyelodysplastic Syndromes030220 oncology & carcinogenesisCancer cellbiology.proteinProtein Processing Post-TranslationalMolecular ChaperonesSignal TransductionExperimental Cell Research
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Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational…

2003

The large L envelope protein of the hepatitis B virus utilizes a new folding pathway to acquire a dual transmembrane topology in the endoplasmic reticulum (ER). The process involves cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain into the ER. Here, we demonstrate that the conformational and functional heterogeneity of L depends on the action of molecular chaperones. Using coimmunoprecipitation, we observed specific interactions between L and the cytosolic Hsc70, in conjunction with Hsp40, and between L and the ER-resident BiP in mammalian cells. Complex formation between L and Hsc70 was abolished when preS translocation was artifici…

Protein ConformationImmunoprecipitationHSC70 Heat-Shock Proteinsmacromolecular substancesTopologyProtein structureViral Envelope ProteinsAnimalsHSP70 Heat-Shock ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyEndoplasmic reticulumHSC70 Heat-Shock ProteinsBiological SciencesPrecipitin TestsTransport proteinProtein TransportMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein topologyCarrier ProteinsProtein Processing Post-TranslationalMolecular ChaperonesProceedings of the National Academy of Sciences
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Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation

1995

Processing of the hepatitis C virus polyprotein is mediated by host cell signalases and at least two virally encoded proteinases. Of these, the serine-type proteinase encompassing the amino-terminal one-third of NS3 is responsible for cleavage at the four sites carboxy terminal of NS3. The activity of this proteinase is modulated by NS4A, a 54-amino-acid polyprotein cleavage product essential for processing at the NS3/4A, NS4A/4B, and NS4B/5A sites and enhancing cleavage efficiency between NS5A and NS5B. Using the vaccinia virus-T7 hybrid system to express hepatitis C virus polypeptides in BHK-21 cells, we studied the role of NS4A in proteinase activation. We found that the NS3 proteinase a…

Protein ConformationRecombinant Fusion ProteinsvirusesGenetic VectorsMolecular Sequence DataImmunologyVaccinia virusHepacivirusProtein Sorting SignalsViral Nonstructural ProteinsBiologyKidneyTransfectionCleavage (embryo)MicrobiologyAntibodiesCell LineSerineEpitopesViral Proteinschemistry.chemical_compoundProtein structureProteinase 3CricetinaeVirologyAnimalsAmino Acid SequenceProtein PrecursorsNS5BPeptide sequenceNS3Sequence Homology Amino AcidSerine Endopeptidasesvirus diseasesbiochemical phenomena metabolism and nutritiondigestive system diseasesNS2-3 proteaseBiochemistrychemistryInsect ScienceProtein Processing Post-TranslationalAlgorithmsRNA HelicasesResearch ArticleJournal of Virology
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Dithiothreitol Treatment of Madin-Darby Canine Kidney Cells Reversibly Blocks Export from the Endoplasmic Reticulum but Does Not Affect Vectorial Tar…

1995

Addition of dithiothreitol (DTT) to the culture medium of Madin-Darby canine kidney (MDCK) cells blocks transport of newly synthesized gp80 (clusterin, apolipoprotein J), a soluble marker protein for apical exocytosis in this epithelial cell line. In cells treated with DTT during pulse labeling, gp80 is retained in the endoplasmic reticulum. After removal of the reducing agent, gp80 is posttranslationally oxidized and secreted at the apical surface of MDCK cell monolayers. This demonstrates that when folded and oxidized posttranslationally, gp80 can acquire a conformation that exhibits sorting signals for vectorial targeting. In the continuous presence of DTT, the transepithelial electrical…

Protein FoldingProtein ConformationBiologyEndoplasmic ReticulumKidneySulfur RadioisotopesBiochemistryEpitheliumExocytosisDithiothreitolCell LineMembrane Potentialssymbols.namesakechemistry.chemical_compoundDogsMethioninemedicineAnimalsCysteineSalivary Proteins and PeptidesMolecular BiologySecretory pathwayGlycoproteinsTight junctionEndoplasmic reticulumCell MembraneCell BiologyGolgi apparatusEpitheliumCell biologyDithiothreitolClusterinmedicine.anatomical_structureSecretory proteinchemistrysymbolsOxidation-ReductionProtein Processing Post-TranslationalMolecular ChaperonesJournal of Biological Chemistry
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A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light on

2019

Tubulins and microtubules (MTs) represent targets for taxane-based chemotherapy. To date, several lines of evidence suggest that effectiveness of compounds binding tubulin often relies on different post-translational modifications on tubulins. Among them, methylation was recently associated to drug resistance mechanisms impairing taxanes binding. The sea urchin is recognized as a research model in several fields including fertilization, embryo development and toxicology. To date, some α- and β-tubulin genes have been identified in P. lividus, while no data are available in echinoderms for arginine methyl transferases (PRMT). To evaluate the exploiting of the sea urchin embryo in the field o…

Protein-Arginine N-MethyltransferasesEmbryo NonmammalianPRMTechinodermsIntracellular Signaling Peptides and Proteinsmacromolecular substancesCytostatic AgentsMethylationTubulin ModulatorsArticlearginine methylationsea urchintubulinpost-translational modificationSea Urchinsembryonic structuresToxicity TestsAnimalsProtein Processing Post-TranslationalInternational journal of molecular sciences
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Protein S-nitrosylation: What's going on in plants?

2012

International audience; Nitric oxide (NO) is now recognized as a key regulator of plant physiological processes. Understanding the mechanisms by which NO exerts its biological functions has been the subject of extensive research. Several components of the signaling pathways relaying NO effects in plants, including second messengers, protein kinases, phytohormones, and target genes, have been characterized. In addition, there is now compelling experimental evidence that NO partly operates through posttranslational modification of proteins, notably via S-nitrosylation and tyrosine nitration. Recently, proteome-wide scale analyses led to the identification of numerous protein candidates for S-…

ProteomeKinaseIn silicoRegulatorPlant ImmunityNitric oxideComputational biologyS-NitrosylationPlantBiologyPlantsPosttranslational protein modificationBiochemistryS-NitrosylationPlant immunityBiochemistry[ SDV.SA.AGRO ] Life Sciences [q-bio]/Agricultural sciences/AgronomyPhysiology (medical)Second messenger system[SDV.BV]Life Sciences [q-bio]/Vegetal BiologySignal transductionGeneProtein Processing Post-TranslationalPlant Proteins
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Investigation of cancer drug resistance mechanisms by phosphoproteomics

2020

Abstract Cancer cell mutations can be identified by genomic and transcriptomic techniques. However, they are not sufficient to understand the full complexity of cancer heterogeneity. Analyses of proteins expressed in cancers and their modification profiles show how these mutations could be translated at the functional level. Protein phosphorylation is a major post-translational modification critical for regulating several cellular functions. The covalent addition of phosphate groups to serine, threonine, and tyrosine is catalyzed by protein kinases. Over the past years, kinases were strongly associated with cancer, thus inhibition of protein kinases emanated as novel cancer treatment. Howev…

Proteomics0301 basic medicineProteomeAntineoplastic AgentsBiologyProteomics03 medical and health sciences0302 clinical medicineNeoplasmsBiomarkers TumormedicineAnimalsHumansProtein phosphorylationPhosphorylationProtein Kinase InhibitorsPharmacologyKinasePhosphoproteomicsCancermedicine.diseaseNeoplasm Proteins030104 developmental biologyDrug Resistance Neoplasm030220 oncology & carcinogenesisCancer cellCancer researchPhosphorylationProtein Processing Post-TranslationalTyrosine kinasePharmacological Research
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In Situ Detection of Phosphorylated Platelet-derived Growth Factor Receptor β Using a Generalized Proximity Ligation Method

2007

Improved methods are needed for in situ characterization of post-translational modifications in cell lines and tissues. For example, it is desirable to monitor the phosphorylation status of individual receptor tyrosine kinases in samples from human tumors treated with inhibitors to evaluate therapeutic responses. Unfortunately the leading methods for observing the dynamics of tissue post-translational modifications in situ, immunohistochemistry and immunofluorescence, exhibit limited sensitivity and selectivity. Proximity ligation assay is a novel method that offers improved selectivity through the requirement of dual recognition and increased sensitivity by including DNA amplification as a…

ProteomicsImmunoglobulinsProximity ligation assayKidneyBiochemistryReceptor tyrosine kinaseCell LineAnalytical ChemistryReceptor Platelet-Derived Growth Factor betaGrowth factor receptorPlatelet-Derived Growth Factor Receptor BetaHumansPhosphorylationMolecular BiologyWound HealingbiologyEndothelial CellsTransfectionFibroblastsImmunohistochemistryPrimary and secondary antibodiesMolecular biologyActinsCell culturebiology.proteinTyrosinePhosphorylationProtein Processing Post-TranslationalSignal TransductionMolecular & Cellular Proteomics
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mRNA as a versatile tool for exogenous protein expression.

2012

Several viral and non-viral vectors have been developed for exogenous protein expression in specific cells. Conventionally, this purpose is achieved through the use of recombinant DNA. But mainly due to the risks associated with permanent genetic alteration of cells, safety and ethical concerns have been raised for the use of DNA-based vectors in human clinical therapy. In the last years, synthetic messenger RNA has emerged as powerful tool to deliver genetic information. RNA vectors exhibit several advantages compared to DNA and are particularly interesting for applications that require transient gene expression. RNA stability and translation efficiency can be increased by cis-acting struc…

RNA StabilityGenetic VectorsGene ExpressionComputational biologyBiologySmall hairpin RNADrug DiscoveryGene expressionGeneticsAnimalsHumansVector (molecular biology)RNA MessengerMolecular BiologyPost-transcriptional regulationGenetics (clinical)GeneticsMessenger RNAGene Transfer TechniquesRNAGenetic TherapyImmunity InnateRNA silencingRegulatory sequenceMolecular MedicineProtein Processing Post-TranslationalCurrent gene therapy
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