Search results for "CLEAVAGE"

showing 10 items of 281 documents

The type of GnRH analogue used during controlled ovarian stimulation influences early embryo developmental kinetics: a time-lapse study

2013

OBJECTIVE: To explore if the GnRH analogue used for controlled ovarian stimulation (COS) and the ovulation triggering factor (GnRH agonist + hCG triggering versus GnRH antagonist + GnRH agonist triggering) affect embryo development and kinetics.STUDY DESIGN: In a retrospective cohort study in the Instituto Valenciano de Infertilidad (IVI) Alicante and the Instituto Universitario-IVI Valencia, Spain, 2817 embryos deriving from 400 couples undergoing oocyte donation were analysed. After controlled ovarian stimulation and IVF/intracytoplamic sperm injection, the timing of embryonic cleavages was assessed by a video time-lapse system. The results were analysed using Student's t test for compari…

Pregnancy RateZygoteGonadotropin-Releasing Hormone/adverse effectsmedicine.medical_treatmentGonadotropin-releasing hormoneChorionic GonadotropinGonadotropin-Releasing HormoneEmbryo Culture TechniquesCohort StudiesTime-lapsePregnancyGnRH analogueFertility Agents Female/adverse effectsmedia_commonOocyte DonationObstetrics and GynecologyEmbryoEmbryo transferembryonic structuresSpain/epidemiologyEctogenesis/drug effectsFemaleInfertility Femalehormones hormone substitutes and hormone antagonistsEmbryo qualityAdultAgonistInfertility Female/therapyendocrine systemmedicine.medical_specialtymedicine.drug_classCleavage Stage Ovummedia_common.quotation_subjectFertilization in VitroBiologyTime-Lapse ImagingOvulation InductionInternal medicinemedicineHumansOvulationRetrospective StudiesZygote/drug effectsFertility Agents FemaleOvulation Induction/methodsEmbryo TransferEmbryo developmental kineticsKineticsPregnancy rateEndocrinologyReproductive MedicineSpainEctogenesisChorionic Gonadotropin/pharmacologyOvulation inductionCleavage Stage Ovum/drug effectsEuropean Journal of Obstetrics & Gynecology and Reproductive Biology
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µ-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptos…

2011

Anti-apoptotic Bfl-1 and pro-apoptotic Bax, two members of the Bcl-2 family sharing a similar structural fold, are classically viewed as antagonist regulators of apoptosis. However, both proteins were reported to be death inducers following cleavage by the cysteine protease µ-calpain. Here we demonstrate that calpain-mediated cleavage of full-length Bfl-1 induces the release of C-terminal membrane active α-helices that are responsible for its conversion into a pro-apoptotic factor. A careful comparison of the different membrane-active regions present in the Bfl-1 truncated fragments with homologous domains of Bax show that helix α5, but not α6, of Bfl-1 induces cell death and cytochrome c r…

Programmed cell deathProtein StructureCancer Treatmentlcsh:MedicineApoptosisMitochondrionCleavage (embryo)BiochemistryProtein Structure SecondaryMinor Histocompatibility AntigensMiceCell Line TumorMolecular Cell BiologyAnimalsHumanslcsh:ScienceProtein InteractionsBiologyMultidisciplinaryMicroscopy ConfocalbiologyCell DeathCalpainCytochrome clcsh:RCytochromes cProteinsCalpainCysteine proteaseCell biologyMitochondriaProto-Oncogene Proteins c-bcl-2OncologyApoptosisbiology.proteinMedicinelcsh:QElectrophoresis Polyacrylamide GelGlobular ProteinsBCL2-related protein A1Research ArticlePloS one
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Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3

2012

Abstract Meprin α and β, members of the astacin family of zinc metalloproteinases, are unique plasma membrane and secreted proteases known to cleave a wide range of biological substrates involved in inflammation, cancer and fibrosis. In this study, we identified proMMP-9 as a novel substrate and show that aminoterminal meprin-mediated clipping improves the activation kinetics of proMMP-9 by MMP-3, an efficient activator of proMMP-9. Interestingly, the NH2-terminus LVLFPGDL, generated by incubation with meprin α, is identical to the form produced in conditioned media from human neutrophils and monocytes. Hence, this meprin-mediated processing and enhancement of MMP-9 activation kinetics may …

ProteasesNeutrophilsMolecular Sequence DataBiophysicsMatrix metalloproteinaseBiochemistryMonocytesProtein–protein interactionAminoterminal cleavageStructural BiologyGeneticsHumansProMMP-9ZymographyAmino Acid SequenceMolecular BiologyCells Culturedchemistry.chemical_classificationChemistryActivator (genetics)TioproninMeprinCell BiologyTissue inhibitor of metalloproteinaseEnzymeMatrix Metalloproteinase 9BiochemistryCulture Media ConditionedMatrix Metalloproteinase 3AstacinFEBS Letters
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Detection of proteolytic (C 3-cleaving) activity on mouse mastocytoma (P815) cells and other mouse cell lines by formation of cell contact with C 3-c…

1979

Mouse mastocytoma cells (P 815) formed rosettes with normal mouse spleen lymphocytes which had been coated with uncleaved human C 3; this interaction was clearly dependent on the amount of C 3. Lymphocytes treated with C 3 b or buffer alone were ineffective. Formation of cell contact could be inhibited by the presence of protease inhibitors such as diisopropyl fluorophosphate, phenyl methyl sulfonyl fluoride and tosyllysyl chloromethyl ketone. Seve n out of 13 different cell lines behaved like P 815 cells. The results strongly suggested that a proteolytic activity on mouse tumor cells led to a cooperation with uncleaved C 3 on a carrier cell to connect these two cells. We interpreted these …

ProteasesRosette FormationImmunologyCellMast-Cell SarcomaCell CountBiologyCleavage (embryo)Cell LineCell membraneMicemedicineAnimalsImmunology and AllergyProtease InhibitorsLymphocytesCell MembraneMastocytomaComplement C3medicine.diseaseMolecular biologymedicine.anatomical_structureCell cultureMast cell sarcomaDiisopropyl fluorophosphateSpleenmedicine.drugEuropean Journal of Immunology
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Specific processing of tenascin-C by the metalloprotease meprinβ neutralizes its inhibition of cell spreading

2009

The metalloprotease meprin has been implicated in tissue remodelling due to its capability to degrade extracellular matrix components. Here, we investigated the susceptibility of tenascin-C to cleavage by meprinbeta and the functional properties of its proteolytic fragments. A set of monoclonal antibodies against chicken and human tenascin-C allowed the mapping of proteolytic fragments generated by meprinbeta. In chicken tenascin-C, meprinbeta processed all three major splicing variants by removal of 10kDa N-terminal and 38kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern was found for large human tenascin-C variant where two N-terminal pep…

Proteasesanimal structuresColonRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataTenascinCleavage (embryo)Cell LineCrohn DiseaseCell AdhesionAnimalsHumansProtein IsoformsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPeptide sequencebiologyAlternative splicingTenascin CMetalloendopeptidasesTenascinMolecular biologyPeptide FragmentsExtracellular MatrixFibronectinsFibronectinAlternative SplicingProtein Subunitsembryonic structuresbiology.proteinProtein MultimerizationChickensMatrix Biology
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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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Identification of proteins cleaved downstream of caspase activation in monocytes undergoing macrophage differentiation.

2006

We have shown previously that caspases were specifically involved in the differentiation of peripheral blood monocytes into macrophages while not required for monocyte differentiation into dendritic cells. To identify caspase targets in monocytes undergoing macrophagic differentiation, we used the human monocytic leukemic cell line U937, whose macrophagic differentiation induced by exposure to 12-O-tetradecanoylphorbol 13-acetate (TPA) can be prevented by expression of the baculovirus caspase-inhibitory protein p35. A comparative two-dimensional gel proteomic analysis of empty vector- and p35-transfected cells after 12 h of exposure to 20 nm TPA, followed by mass spectrometry analysis, iden…

ProteomeCleavage (embryo)Caspase 8TransfectionBiochemistryMonocytesViral ProteinsHumansElectrophoresis Gel Two-DimensionalRNA Small InterferingMolecular BiologyCaspaseCaspase 8biologyU937 cellMacrophagesRNACell DifferentiationCell BiologyTransfectionU937 CellsMolecular biologyCaspase InhibitorsPeptide FragmentsCell biologyEnzyme ActivationCell cultureMonocyte differentiationCaspasesbiology.proteinCarcinogensTetradecanoylphorbol AcetateThe Journal of biological chemistry
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Bioassays to monitor taspase1 function for the identification of pharmacogenetic inhibitors

2011

Background Threonine Aspartase 1 (Taspase1) mediates cleavage of the mixed lineage leukemia (MLL) protein and leukemia provoking MLL-fusions. In contrast to other proteases, the understanding of Taspase1's (patho)biological relevance and function is limited, since neither small molecule inhibitors nor cell based functional assays for Taspase1 are currently available. Methodology/Findings Efficient cell-based assays to probe Taspase1 function in vivo are presented here. These are composed of glutathione S-transferase, autofluorescent protein variants, Taspase1 cleavage sites and rational combinations of nuclear import and export signals. The biosensors localize predominantly to the cytoplasm…

ProteomicsCytoplasmHydrolasesmedicine.medical_treatmentThreonine Aspartase 1Drug Evaluation Preclinicallcsh:MedicineBiosensing TechniquesBiochemistryMiceMolecular Cell BiologyBasic Cancer Researchlcsh:ScienceMultidisciplinaryEnzyme ClassesProteomic Databases3T3 CellsSmall moleculeCellular StructuresEnzymesBiochemistryOncologyMedicineBiological AssayBiologieResearch ArticleProteasesCell SurvivalIn silicoBiologyCleavage (embryo)In vivoGenetic Mutationddc:570EndopeptidasesChemical BiologyConsensus sequencemedicineGeneticsAnimalsHumansProtease InhibitorsBiologyCell NucleusProteaselcsh:RProteinsPharmacogeneticsSmall MoleculesMutagenesislcsh:Q
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The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species

2012

The amyloid β (Aβ) peptide, which is abundantly found in the brains of patients suffering from Alzheimer disease, is central in the pathogenesis of this disease. Therefore, to understand the processing of the amyloid precursor protein (APP) is of critical importance. Recently, we demonstrated that the metalloprotease meprin β cleaves APP and liberates soluble N-terminal APP (N-APP) fragments. In this work, we present evidence that meprin β can also process APP in a manner reminiscent of β-secretase. We identified cleavage sites of meprin β in the amyloid β sequence of the wild type and Swedish mutant of APP at positions p1 and p2, thereby generating Aβ variants starting at the first or seco…

ProteomicsMolecular Sequence DataMutantPeptideBiologyHydroxamic AcidsCleavage (embryo)BiochemistryCatalysis03 medical and health sciences0302 clinical medicineAlzheimer Diseasemental disordersmedicineAmyloid precursor proteinHumansProtein IsoformsAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMetalloproteinaseAmyloid beta-PeptidesWild typeBrainMetalloendopeptidasesMolecular Bases of DiseaseCell Biologymedicine.diseaseMolecular biologyProtein Structure TertiaryKineticsHEK293 CellsEnzymechemistryBiochemistryMutationMetalloproteasesbiology.proteinAmyloid Precursor Protein SecretasesAlzheimer's diseasePeptides030217 neurology & neurosurgeryJournal of Biological Chemistry
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LC–MS Based Cleavage Site Profiling of the Proteases ADAM10 and ADAM17 Using Proteome-Derived Peptide Libraries

2014

A Disintegrin and Metalloproteinase 10 (ADAM10) and ADAM17 catalyze ectodomain shedding of a number of cell surface proteins important for embryonic development and tissue homeostasis. Changes in the expression levels or dysregulated proteolytic activity of ADAM10 and ADAM17 have been shown to play important roles in multiple diseases such as inflammation, cancer, and neurodegenerative disorders. Despite the well documented substrate repertoire of ADAM10 and ADAM17, little is known about their cleavage site specificity. We optimized Q-PICS (Quantitative Proteomics for the Identification of Cleavage Sites) to elucidate the cleavage site specificity of recombinant murine ADAM10 and ADAM17. Tw…

ProteomicsProteasesProteomeQuantitative proteomicsADAM17 ProteinBiologyCleavage (embryo)BiochemistryMass SpectrometryADAM10 ProteinMicePeptide LibraryAnimalsHumansADAM17 ProteinPeptide libraryTissue homeostasisMembrane ProteinsGeneral ChemistryPeptide FragmentsADAM ProteinsBiochemistryEctodomainProteomeAmyloid Precursor Protein SecretasesChromatography LiquidJournal of Proteome Research
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