Search results for "post-translational"

showing 10 items of 176 documents

Synergistic targeting of FLT3 mutations in AML via combined menin-MLL and FLT3 inhibition

2020

Abstract The interaction of menin (MEN1) and MLL (MLL1, KMT2A) is a dependency and provides a potential opportunity for treatment of NPM1-mutant (NPM1mut) and MLL-rearranged (MLL-r) leukemias. Concomitant activating driver mutations in the gene encoding the tyrosine kinase FLT3 occur in both leukemias and are particularly common in the NPM1mut subtype. In this study, transcriptional profiling after pharmacological inhibition of the menin-MLL complex revealed specific changes in gene expression, with downregulation of the MEIS1 transcription factor and its transcriptional target gene FLT3 being the most pronounced. Combining menin-MLL inhibition with specific small-molecule kinase inhibitors…

NPM1Transcription GeneticImmunologyApoptosisBiochemistryMiceRandom AllocationMice Inbred NODCell Line TumorProto-Oncogene Proteinshemic and lymphatic diseasesAntineoplastic Combined Chemotherapy ProtocolsGene expressionmedicineAnimalsHumansMEN1PhosphorylationMyeloid Ecotropic Viral Integration Site 1 ProteinProtein Kinase InhibitorsneoplasmsbiologyGene Expression Regulation LeukemicKinaseNuclear ProteinsMyeloid leukemiaDrug SynergismHistone-Lysine N-MethyltransferaseCell BiologyHematologymedicine.diseaseCoculture TechniquesNeoplasm ProteinsLeukemia Myeloid AcuteLeukemiaKMT2Afms-Like Tyrosine Kinase 3biology.proteinCancer researchNucleophosminProtein Processing Post-TranslationalTyrosine kinaseMyeloid-Lymphoid Leukemia ProteinBlood
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Selective mono-de-O-acetylation of the per-O-acetylated brasilicardin carbohydrate side chain

2021

Abstract Methanol dried over powdered 4 A molecular sieves can be used for a selective mono-de-O-acetylation of the phenolic acetyl group of the per-O-acetyl protected brasilicardin A carbohydrate side chain. This reaction opens a practical procedure for a synthetic access to derivates of the immunosuppressive and cytotoxic natural product brasilicardin A.

Natural product010405 organic chemistryChemistryOrganic ChemistryCarbohydratesAcetylationGeneral MedicineCarbohydrate010402 general chemistryMolecular sieve01 natural sciencesBiochemistry0104 chemical sciencesAnalytical Chemistrychemistry.chemical_compoundAcetylationSide chainOrganic chemistryMethanolProtein Processing Post-TranslationalCarbohydrate Research
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Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?

2021

RNA-binding proteins (RBPs) are critical players in RNA expression and metabolism, thus, the proper regulation of this class of proteins is critical for cellular health. Regulation of RBPs often occurs through post-translational modifications (PTMs), which allow the cell to quickly and efficiently respond to cellular and environmental stimuli. PTMs have recently emerged as important regulators of RBPs implicated in neurodegenerative disorders, in particular amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Here, we summarize how disease-associated PTMs influence the biophysical properties, molecular interactions, subcellular localization, and function of ALS/FTD-linked …

NeurodegenerationCellAmyotrophic Lateral SclerosisRNA-Binding ProteinsRNA-binding proteinBiologymedicine.diseaseSubcellular localizationBiochemistrymedicine.anatomical_structureFrontotemporal Dementiamental disordersmedicinePosttranslational modificationHumansRNA-Binding Protein FUSAmyotrophic lateral sclerosisMolecular BiologyNeuroscienceProtein Processing Post-TranslationalFunction (biology)Frontotemporal dementiaTrends in biochemical sciences
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Phenylpropanoid and phenylisoprenoid metabolites from Asteraceae species as inhibitors of protein carbonylation.

2011

Abstract Three phenolic antioxidant and anti-inflammatory compounds: 7-methylaromadendrin, isoprenylhydroquinone glucoside, and 3.5-dicaffeoylquinic acid methyl ester, all isolated from Western Mediterranean Asteraceae species, have been studied for their inhibitory activity against protein carbonylation, a harmful post-translational modification of peptide chains associated with degenerative diseases. All compounds have proven to be effective, with 50% inhibitory concentration (IC 50 ) values in the micromolar range, against bovine serum albumin carbonylation caused by hypochlorite, peroxynitrite, and phorbol ester-induced leukocyte oxidative burst.

NeutrophilsProtein CarbonylationLeukocyte oxidative burstHypochloritePlant ScienceHorticultureAsteraceaeBiochemistryAntioxidantsProtein Carbonylationchemistry.chemical_compoundInhibitory Concentration 50GlucosideGlucosidesPhenolsPeroxynitrous AcidPhorbol EstersHumansBovine serum albuminMolecular BiologyRespiratory BurstFlavonoidsbiologyPhenylpropanoidCell-Free SystemSerum Albumin BovineGeneral MedicineHydroquinonesHypochlorous AcidchemistryBiochemistryFlavanonesbiology.proteinChlorogenic AcidCarbonylationProtein Processing Post-TranslationalPeroxynitritePhytochemistry
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Modification of the proteolytic fragmentation pattern upon oxidation of cysteines from ribulose 1,5-bisphosphate carboxylase/oxygenase.

2003

The proteolytic susceptibility of the native CO 2 -fixing photosynthetic enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39, Rubisco) has been shown to increase in vitro after oxidative treatments that affect cysteine thiols. A limited incubation of oxidized (pretreated with the disulfide cystamine) Rubisco from Chlamydomonas reinhardtii with subtilisin or proteinase K generated fragments of molecular mass about 53 kDa (band I in SDS-PAGE) and 47 kDa (band II) derived from the large subunit (55 kDa) of the enzyme. In contrast, proteolysis of the reduced Rubisco (pretreated with the free thiol cysteamine) produced only the 53 kDa band. The same fragmentation pattern was repr…

OxygenaseProtein subunitRibulose-Bisphosphate CarboxylaseMolecular Sequence DataBiochemistrychemistry.chemical_compoundEndopeptidasesAnimalsEuglena gracilisAmino Acid SequenceCysteineConserved SequenceRibulose 15-bisphosphatebiologyRibuloseHydrolysisfungiRuBisCOSubtilisinPeptide FragmentsKineticsProtein SubunitschemistryBiochemistryModels Chemicalbiology.proteinProtein quaternary structureHoloenzymesOxidation-ReductionProtein Processing Post-TranslationalChlamydomonas reinhardtiiCysteineBiochemistry
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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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Sequence evolution, processing, and posttranslational modification of zonadhesin D domains in primates, as inferred from cDNA data

2005

Zonadhesin is a mammalian transmembrane sperm ligand. Precursor zonadhesin essentially consists of MAM (meprin/A5 antigen/mu receptor tyrosine phosphatase) domains, a mucin-like repeat, and D domains (homologous to von Willebrand D). Recent immunovisualization and binding assays indicate that zonadhesin D domains 1–3 bind postacrosomally to the zona pellucida. This feature has attracted considerable interest in the evolution of zonadhesin and its possible biological and biomedical implications. Previous molecular evolutionary analyses, however, were confined to cDNA sequences of only few distantly related species. Moreover, except for rabbit and pig, little is known about zonadhesin’s proce…

PrimatesDNA ComplementaryBase pairMolecular Sequence DataBiologyPROSITEEvolution MolecularComplementary DNAGeneticsmedicineAnimalsAmino Acid SequenceSelection GeneticZona pellucidaPhylogenyGeneticsComputational BiologyMembrane ProteinsGeneral MedicineLigand (biochemistry)Transmembrane proteinProtein Structure Tertiarymedicine.anatomical_structureEvolutionary biologyGenBankDimerizationProtein Processing Post-TranslationalSequence AlignmentFunction (biology)Protein Modification TranslationalGene
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Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

2009

Abstract Both the cellular prion protein (PrPc) and the amyloid precursor protein (APP) are physiologically subjected to complex proteolytic processing events. While for APP the proteinases involved – alpha-, beta- and gamma-secretase – have been identified in vitro and in vivo, the cleavage of PrPc by now has been linked only to the shedding activity of the metalloproteinase ADAM10 and/or ADAM17 in cell culture. Here we show that neuronal overexpression of the alpha-secretase ADAM10 in mice reduces all PrPc species detected in the brain instead of leading to enhanced amounts of specific cleavage products of PrPc. Additionally, the incubation time of mice after scrapie infection is signific…

Prionsanimal diseasesADAM10Molecular Sequence DataPrion diseaseScrapieMice Transgeniclcsh:RC321-571ADAM10 ProteinMiceIn vivomental disordersNeurotoxicitymedicineAmyloid precursor proteinAnimalsHumansGliosisAmino Acid Sequencealpha-Secretaselcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySheddingMetalloproteinasebiologyChemistryBrainMembrane ProteinsMolecular biologyIn vitronervous system diseasesMice Inbred C57BLADAM ProteinsNeurologyAlpha secretaseGliosisbiology.proteinCattlemedicine.symptomAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalScrapieNeurobiology of disease
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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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