Search results for " enzymes"

showing 10 items of 240 documents

Activation of the first component of complement, C1: comparison of the effect of sixteen different enzymes on serum C1.

1983

In this study, the effect of sixteen different enzymes on serum C1 and its subcomponents was investigated. The sixteen enzymes could be divided into three groups. First, enzymes which activate native C1: trypsin (optimal concentration 2.4 x 10(-4) mM); alpha-chymotrypsin (2.3 x 10(3) mM); thrombin (1.0 x 10(-5) mM); plasmin (1.9 x 10(-5) mM); elastase (5.8 x 10(-5) mM); pronase (3.0 x 10(-6) mM). All these enzymes are serine esterase and activate native serum C1 bound to EAC4 at the given concentration within 10 min at 30 degrees C. Furthermore, native C1 inhibited by a pentosanpolysulfoester, Sp54, is unable to undergo the internal activation but can be externally activated by the serine e…

PlasminComplement Activating EnzymesImmunologyGuinea PigsDose-Response Relationship ImmunologicPronaseSerinechemistry.chemical_compoundComplement C1medicineImmunology and AllergyAnimalsHumansTrypsinFibrinolysinComplement Activationchemistry.chemical_classificationPentosan Sulfuric PolyesterbiologyHematologyTrypsinCarboxypeptidaseKineticsEnzymeBiochemistrychemistrybiology.proteinCollagenaseCattleRabbitsLysozymemedicine.drugPeptide HydrolasesImmunobiology
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Poly-ADP-Ribose (PAR) as an epigenetic flag

2009

Epigenetics is the study of hereditable chromatin modifications, such as DNA methylation, histone modifications, and nucleosome-remodelling, which occur without alterations to the DNA sequence. The establishment of different epigenetic states in eukaryotes depends on regulatory mechanisms that induce structural changes in chromatin in response to environmental and cellular cues. Two classes of enzymes modulate chromatin accessibility: chromatin-covalent modifiers and ATP-dependent chromatin remodelling complexes. The first class of enzymes catalyzes covalent modifications of DNA as well as the amino- and carboxy-terminal tails of histones, while the second uses the energy of ATP hydrolysis …

Poly Adenosine Diphosphate RiboseCancer ResearchHistone-modifying enzymesEpigenetic regulation of neurogenesisDNA MethylationBiologyChromatin Assembly and DisassemblyChromatin remodelingEpigenesis GeneticChromatinHistonesEpigenetics of physical exerciseBiochemistryHistone methylationAnimalsHumansHistone codePARP epigeneticsPoly(ADP-ribose) PolymerasesMolecular BiologyEpigenomicsEpigenetics
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Silymarin and Cancer: A Dual Strategy in Both in Chemoprevention and Chemosensitivity

2020

Silymarin extracted from milk thistle consisting of flavonolignan silybin has shown chemopreventive and chemosensitizing activity against various cancers. The present review summarizes the current knowledge on the potential targets of silymarin against various cancers. Silymarin may play on the system of xenobiotics, metabolizing enzymes (phase I and phase II) to protect normal cells against various toxic molecules or to protect against deleterious effects of chemotherapeutic agents on normal cells. Furthermore, silymarin and its main bioactive compounds inhibit organic anion transporters (OAT) and ATP-binding cassettes (ABC) transporters, thus contributing to counteracting potential chemor…

Programmed cell deathsilymarinCellChemosensitizerPharmaceutical SciencechemopreventiveATP-binding cassette transporterApoptosisReviewProtective AgentsChemopreventionsilybinAnalytical Chemistrylcsh:QD241-44103 medical and health sciences0302 clinical medicinelcsh:Organic chemistryDrug DiscoverymedicineHumansPhysical and Theoretical ChemistryReceptor030304 developmental biology0303 health sciencesChemistryOrganic ChemistryCancerCell Cycle CheckpointsCell cyclemedicine.diseasemedicine.anatomical_structureChemistry (miscellaneous)intrinsic and extrinsic pathwayDrug Resistance Neoplasm030220 oncology & carcinogenesisCancer cellchemosensitizerCancer researchMolecular Medicinemetabolizing enzymesATP-Binding Cassette Transporterscell cycleABC transporterSignal TransductionMolecules
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Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenes…

2011

AbstractOver the past years the members of the type II transmembrane serine protease (TTSP) family have emerged as new players in mammalian biology. TMPRSS4 (transmembraneprotease/serine) is overexpressed in several human cancer tissues, promoting invasion, migration, and metastasis. However, the physiological function has not yet been elucidated. Here, we present morpholino knockdown studies targeting TMPRSS4a, a homolog of human TMPRSS4 in zebrafish embryos. By RT-PCR, we could demonstrate an expression of this protease already 5 h post-fertilization, suggesting important functions in the early stages of embryonic development. Indeed,in vivogene silencing caused severe defects in tissue d…

ProteasesEmbryo NonmammalianMorpholinoOrganogenesisCellular differentiationmedicine.medical_treatmentMolecular Sequence DataClinical BiochemistryBiologyBiochemistry03 medical and health sciences0302 clinical medicineCell AdhesionmedicineAnimalsHumansAmino Acid SequenceCell adhesionMolecular BiologyPhylogenyZebrafish030304 developmental biologySerine protease0303 health sciencesProteaseCell adhesion moleculeGene Expression ProfilingSerine EndopeptidasesProteolytic enzymesGene Expression Regulation DevelopmentalMembrane ProteinsCell DifferentiationZebrafish ProteinsMolecular biologyGene Knockdown Techniques030220 oncology & carcinogenesisbiology.proteinSequence AlignmentBiological Chemistry
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The Closed/Open Model for Lipase Activation. Addressing Intermediate Active Forms of Fungal Enzymes by Trapping of Conformers in Water-Restricted Env…

2001

The behavior of prototypic fungal lipases in a water-restricted environment has been investigated by exploiting the reported experimental strategy that allows the trapping (freeze-drying) of the enzyme in the conformation present in aqueous solution and to subsequently assay it in nonaqueous media [Mingarro, I., Abad, C., and Braco, L. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 3308-3312]. We now report, using simple esterification as well as acidolysis (triglycerides as substrates) as nonaqueous model reactions, that the presence of a detergent (n-octyl-beta-glucopyranoside) in the freeze-drying buffer, at concentrations below the critical micellar concentration, generates different catalyti…

Protein ConformationStereochemistryThioglucosidesDetergentsTrappingBuffersBiochemistryFungal ProteinsAscomycotaEnzyme StabilityMoleculeLipaseConformational isomerismMicellesTriglyceridesCandidachemistry.chemical_classificationAqueous solutionbiologyWaterLipaseGeotrichumEnzyme ActivationSolutionsFreeze DryingEnzymeModels ChemicalchemistryCritical micelle concentrationbiology.proteinFungal enzymesRhizopusBiochemistry
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Identification of Rothia Bacteria as Gluten-Degrading Natural Colonizers of the Upper Gastro-Intestinal Tract

2011

Background Gluten proteins, prominent constituents of barley, wheat and rye, cause celiac disease in genetically predisposed subjects. Gluten is notoriously difficult to digest by mammalian proteolytic enzymes and the protease-resistant domains contain multiple immunogenic epitopes. The aim of this study was to identify novel sources of gluten-digesting microbial enzymes from the upper gastro-intestinal tract with the potential to neutralize gluten epitopes. Methodology/Principal Findings Oral microorganisms with gluten-degrading capacity were obtained by a selective plating strategy using gluten agar. Microbial speciations were carried out by 16S rDNA gene sequencing. Enzyme activities wer…

ProteomicsApplied Microbiologylcsh:MedicineBiochemistryGliadinEpitopeSubstrate SpecificityUpper Gastrointestinal Tractlcsh:ScienceBifidobacterium2. Zero hungerchemistry.chemical_classification0303 health sciencesAniline CompoundsMultidisciplinarymedicine.diagnostic_testbiologyHydrolysisProteolytic enzymesfood and beveragesHydrogen-Ion ConcentrationEnzymes3. Good healthSolutionsBiochemistryMedical MicrobiologyMedicineSmall IntestineResearch ArticleProteasesGlutensProteolysisMolecular Sequence DataDental PlaqueGastroenterology and HepatologyMicrobiologydigestive systemMicrobiology03 medical and health sciencesAntigenmedicineHumansAmino Acid SequenceSalivaBiology030304 developmental biologyBinding Sites030306 microbiologylcsh:Rnutritional and metabolic diseasesbiology.organism_classificationGlutenPeptide Fragmentsdigestive system diseasesMolecular WeightCeliac DiseasechemistryProteolysisbiology.proteinlcsh:QGliadinMicrococcaceaePLoS ONE
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Increased oxidative stress and impaired antioxidant response in Lafora disease.

2014

15 páginas, 10 figuras

ProteomicsGenetically modified mouseAntioxidantmedicine.medical_treatmentNeuroscience (miscellaneous)Proteomic analysisMice TransgenicBiologymedicine.disease_causeBiochemistryAntioxidantsLafora diseaseMiceCellular and Molecular NeuroscienceLaforinPhysiology (medical)AutophagymedicineAnimalsHumansLafora diseaseMice Knockoutchemistry.chemical_classificationReactive oxygen speciesAutophagymedicine.diseaseMalinCell biologyNeurologychemistryBiochemistryOxidative stressMutationAntioxidant enzymesReactive Oxygen SpeciesLaforinOxidative stressIntracellularFree radical biologymedicine
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Integrated multi-omics investigations of metalloproteinases in colon cancer: Focus on MMP2 and MMP9

2021

Colorectal cancer (CRC) develops by genetic and epigenetic alterations. However, the molecular mechanisms underlying metastatic dissemination remain unclear and could benefit from multi-omics investigations of specific protein families. Matrix metalloproteinases (MMPs) are proteolytic enzymes involved in ECM remodeling and the processing of bioactive molecules. Increased MMP expression promotes the hallmarks of tumor progression, including angiogenesis, invasion, and metastasis, and is correlated with a shortened survival. Nevertheless, the collective role and the possible coordination of MMP members in CRC are poorly investigated. Here, we performed a multi-omics analysis of MMP expression…

ProteomicsMMP2Epithelial-Mesenchymal TransitionQH301-705.5Colorectal cancerBioinformaticsKaplan-Meier EstimateBiologyMatrix metalloproteinaseMMP9ArticleCatalysisEpigenesis GeneticMetastasisCohort StudiesInorganic ChemistryLymphocytes Tumor-InfiltratingmedicineHumansEpithelial–mesenchymal transitionBiology (General)Physical and Theoretical ChemistrySettore BIO/06 - Anatomia Comparata E CitologiaQD1-999Molecular BiologySpectroscopyTissue Inhibitor of Metalloproteinase-2Functional analysisMMP9Organic ChemistryProteolytic enzymesGeneral Medicinemedicine.diseasePrognosisComputer Science ApplicationsColon cancerExtracellular MatrixGene Expression Regulation NeoplasticChemistryMatrix metalloproteinasesMatrix Metalloproteinase 9Tumor progressionCase-Control StudiesColonic NeoplasmsCancer researchMatrix Metalloproteinase 2Gene expressionMMP2
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Oral enzymatic detoxification system: Insights obtained from proteome analysis to understand its potential impact on aroma metabolization

2021

The oral cavity is an entry path into the body, enabling the intake of nutrients but also leading to the ingestion of harmful substances. Thus, saliva and oral tissues contain enzyme systems that enable the early neutralization of xenobiotics as soon as they enter the body. Based on recently published oral proteomic data from several research groups, this review identifies and compiles the primary detoxification enzymes (also known as xenobiotic-metabolizing enzymes) present in saliva and the oral epithelium. The functions and the metabolic activity of these enzymes are presented. Then, the activity of these enzymes in saliva, which is an extracellular fluid, is discussed with regard to the…

ProteomicsSalivaProteomeContext (language use)03 medical and health scienceschemistry.chemical_compound0302 clinical medicineDetoxificationdetoxification enzymesAroma030304 developmental biologychemistry.chemical_classificationMouth0303 health sciencessalivabiologyChemistryfood and beveragesMetabolismbiology.organism_classification3. Good healthstomatognathic diseasesEnzymeBiochemistryaroma030220 oncology & carcinogenesisOdorantsProteomeoral cavityXenobioticmetabolism[SDV.AEN]Life Sciences [q-bio]/Food and NutritionFood Science
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Cigarette smoke exposure inhibits extracellular MMP-2 (gelatinase A) activity in human lung fibroblasts

2007

Abstract Background Exposure to cigarette smoke is considered a major risk factor for the development of lung diseases, since its causative role has been assessed in the induction and maintenance of an inflamed state in the airways. Lung fibroblasts can contribute to these processes, due to their ability to produce proinflammatory chemotactic molecules and extracellular matrix remodelling proteinases. Among proteolytic enzymes, gelatinases A and B have been studied for their role in tissue breakdown and mobilisation of matrix-derived signalling molecules. Multiple reports linked gelatinase deregulation and overexpression to the development of inflammatory chronic lung diseases such as COPD.…

Pulmonary and Respiratory MedicineGelatinase ABiologyMatrix metalloproteinaseProinflammatory cytokineExtracellular matrixExtracellularHumansGelatinaseRNA MessengerLungCells Culturedlcsh:RC705-779Cell DeathPlant ExtractsResearchProteolytic enzymessmoke MMP-2Tissue Inhibitor of MetalloproteinasesEnvironmental Exposurelcsh:Diseases of the respiratory systemEnvironmental exposureFibroblastsrespiratory systemrespiratory tract diseasesCulture Media ConditionedImmunologyMatrix Metalloproteinase 2Tobacco Smoke PollutionEnvironmental MonitoringRespiratory Research
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