Search results for "Glucuronidase"

showing 6 items of 46 documents

Kinetic analysis and molecular modeling of the inhibition mechanism of roneparstat (SST0001) on human heparanase

2016

Heparanase is a β-d-glucuronidase which cleaves heparan sulfate chains in the extracellular matrix and on cellular membranes. A dysregulated heparanase activity is intimately associated with cell invasion, tumor metastasis and angiogenesis, making heparanase an attractive target for the development of anticancer therapies. SST0001 (roneparstat; Sigma-Tau Research Switzerland S.A.) is a non-anticoagulant 100% N-acetylated and glycol-split heparin acting as a potent heparanase inhibitor, currently in phase I in advanced multiple myeloma. Herein, the kinetics of heparanase inhibition by roneparstat is reported. The analysis of dose-inhibition curves confirmed the high potency of roneparstat (I…

Protein Conformation alpha-Helical0301 basic medicineSST0001Molecular modelhomology modelingAmino Acid MotifsPlasma protein bindingMolecular Dynamics SimulationBiochemistryMolecular Docking SimulationheparanaseSubstrate Specificity03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePolysaccharidesHumansProtein Interaction Domains and MotifsHeparanaseHomology modelingEnzyme InhibitorsGlucuronidaseBinding Siteskinetic inhibition analysisHeparinComputational BiologyHeparan sulfateRecombinant ProteinsAcidobacteriaMolecular Docking SimulationEnzyme bindingKinetics030104 developmental biologyCarbohydrate SequenceFondaparinuxchemistryBiochemistryStructural Homology ProteinDocking (molecular)030220 oncology & carcinogenesisBiophysicsroneparstatThermodynamicsProtein Conformation beta-StrandORIGINAL ARTICLESProtein BindingGlycobiology
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Nuclear factors binding to the extensin promoter exhibit differential activity in carrot protoplasts and cells

1992

The expression of the cell wall protein extensin, a hydroxyproline-rich glycoprotein, is induced by several different stimuli, including wounding. The process of protoplast preparation mimics the wounding effect and results in the induction of extensin. Using transient expression in protoplasts we analyzed several deletions of the extensin promoter. We identified an important transcriptional regulatory element located between the two TATA boxes that characterize the extensin promoter. Other regulatory elements, located further upstream between -719 to -658, are necessary for maximum level of expression. Employing electrophoretic mobility shift assays and methylation interference experiments…

Transcription GeneticMolecular Sequence DataPlant ScienceBiologyDNA-binding proteinCell wallGene expressionGeneticsCloning MolecularPromoter Regions GeneticExtensinGlucuronidaseGlycoproteinsPlant ProteinsBinding SitesBase SequenceProtoplastsNuclear ProteinsDNAGeneral MedicineMethylationPlantsProtoplastMolecular biologyDNA-Binding ProteinsGene Expression RegulationRegulatory sequencebiology.proteinTrans-actingAgronomy and Crop SciencePlant Molecular Biology
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A newin vitroapproach for the simultaneous determination of phase I and phase II enzymatic activities of human hepatocyte preparations

2007

Primary hepatocytes are still the best qualified in vitro system to anticipate drug metabolism in man. Recent advances in hepatocytes cryopreservation have notably increased their use not only for drug metabolism studies, but also for other applications such as cell transplantation. Evaluation of the drug-metabolizing competence of each hepatocytes preparation is needed. To date, the metabolic characterization of hepatocytes preparations relies on the assessment of phase I activities and the role of phase II enzymes receives little attention. A novel approach for the rapid assessment of the metabolic functionality of hepatocytes has been developed. A five-probe cocktail was used to simultan…

chemistry.chemical_classificationSpectrometry Mass Electrospray IonizationSulfotransferaseCYP3A4Organic ChemistryTandem mass spectrometryMetabolic Detoxication Phase IICryopreservationIn vitroAnalytical ChemistryGlucuronidaseEnzymeCytochrome P-450 Enzyme SystemBiochemistrychemistryTandem Mass SpectrometryHepatocytesHumansMetabolic Detoxication Phase IGlucuronosyltransferaseSulfotransferasesCells CulturedChromatography High Pressure LiquidSpectroscopyDrug metabolismRapid Communications in Mass Spectrometry
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Activity of acid hydrolases in skeletal muscle of untrained, trained and detrained mice of different ages.

1978

The activities of p-nitrophenylphosphatase, beta-glucuronidase and beta-N-acetylglucosaminidase from crude skeletal muscle homogenates of 4 and 7 months old mice were assayed after short-term intensive and long-term moderate training and after terminated training. In the older untrained mice the activity of the hydrolases was higher than in the younger mice. The level increased with training and this increase was far more pronounced in the older animals. Cessation of training for 7 and 21 days decreased this activity in the older animals but it was again increased 42 days later and close to the level observed in the trained mice. In young mice 3 days' terminated training increased the activ…

medicine.medical_specialty4-NitrophenylphosphatasePhysiologyCatabolismMuscleseducationPhysical ExertionAge FactorsSkeletal musclePhysiologyMetabolismBiologyPhosphoric Monoester HydrolasesMicemedicine.anatomical_structureHexosaminidasesAcetylglucosaminidasePhysical therapymedicineAnimalsGlucuronidaseActa physiologica Scandinavica
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Increased mRNAs for procollagens and key regulating enzymes in rat skeletal muscle following downhill running.

1999

The purpose of the study was to investigate pre-translational regulation of collagen expression after a single bout of exercise. We analysed steady-state messenger ribonucleic acid (mRNA) levels for collagen types I, III and IV, alpha- and beta-subunits of prolyl 4-hydroxylase and lysyl oxidase (enzymes modifying procollagen chains), and enzyme activity of prolyl 4-hydroxylase from rat soleus muscle (MS) and the red parts of quadriceps femoris muscle (MQF) after 12 h and after 1, 2, 4, 7 and 14 days of downhill (-13.5 degrees ) treadmill running at a speed of 17 m.min-1 for 130 min. Histological and biochemical assays revealed exercise-induced muscle damage in MQF but not MS. Steady-state m…

medicine.medical_specialtyPhysiologyClinical BiochemistryPhysical ExertionProcollagen-Proline DioxygenaseLysyl oxidaseBiologyRunningProtein-Lysine 6-OxidaseHydroxyprolinechemistry.chemical_compoundType IV collagenPhysiology (medical)Internal medicineGene expressionmedicineAnimalsExertionRNA MessengerRats WistarMuscle SkeletalGlucuronidaseSoleus muscleSkeletal muscleBlotting NorthernRatsProcollagen peptidaseEndocrinologymedicine.anatomical_structurechemistryFemaleCollagenProcollagenPflugers Archiv : European journal of physiology
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Acute exercise induced changes in rat skeletal muscle mRNAs and proteins regulating type IV collagen content

2001

This experiment tested the hypothesis that running-induced damage to rat skeletal muscle causes changes in synthesis and degradation of basement membrane type IV collagen and to proteins regulating its degradation. Samples from soleus muscle and red and white parts of quadriceps femoris muscle (MQF) were collected 6 h or 1, 2, 4, or 7 days after downhill running. Increased muscle β-glucuronidase activity indicated greater muscle damage in the red part of MQF than in the white part of MQF or soleus. In the red part of MQF, type IV collagen expression was upregulated at the pretranslational level and the protein concentration decreased, whereas matrix metalloproteinase-2 (MMP-2), a protein th…

medicine.medical_specialtyTime FactorsTranscription GeneticPhysiologyPhysical ExertionMatrix metalloproteinaseBiologyRunningType IV collagenPhysiology (medical)Internal medicineGene expressionmedicineAnimalsRNA MessengerRats WistarMuscle SkeletalGlucuronidaseSoleus muscleBasement membranechemistry.chemical_classificationTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1Skeletal muscleTissue inhibitor of metalloproteinaseRatsmedicine.anatomical_structureEndocrinologyGene Expression RegulationMatrix Metalloproteinase 9chemistryProtein BiosynthesisMuscle Fibers Fast-TwitchMatrix Metalloproteinase 2FemaleCollagenGlycoproteinAmerican Journal of Physiology-Regulatory, Integrative and Comparative Physiology
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