Search results for "PROTEASES"

showing 10 items of 196 documents

Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates

2011

Astacins are secreted and membrane-bound metalloproteases with clear associations to many important pathological and physiological processes. Yet with only a few substrates described their biological roles are enigmatic. Moreover, the lack of knowledge of astacin cleavage site specificities hampers assay and drug development. Using PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000 cleavage sites were proteomically identified for five different astacins. Such broad coverage enables family-wide determination of specificities N- and C-terminal to the scissile peptide bond. Remarkably, me…

KeratinocytesModels MolecularProteomicsVascular Endothelial Growth Factor AProteasesmedicine.medical_treatmentProteolysisMolecular Sequence DataBiologyCleavage (embryo)BiochemistryCell LineSubstrate SpecificityAnalytical Chemistry03 medical and health sciencesTandem Mass SpectrometrymedicineHumansAmino Acid SequenceMolecular BiologyPeptide sequencePhylogeny030304 developmental biologyEnzyme Precursors0303 health sciencesProteaseStaining and LabelingEdman degradationmedicine.diagnostic_testResearch030302 biochemistry & molecular biologyTioproninMetalloendopeptidasesTerminal amine isotopic labeling of substratesRecombinant ProteinsKineticsBiochemistryProteolysisKallikreinsAstacinPeptidesSequence AlignmentChromatography LiquidMolecular & Cellular Proteomics
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Inhibition Mechanism of SARS‐CoV‐2 Main Protease with Ketone‐Based Inhibitors Unveiled by Multiscale Simulations: Insights for Improved Designs**

2021

Abstract We present the results of classical and QM/MM simulations for the inhibition of SARS‐CoV‐2 3CL protease by a hydroxymethylketone inhibitor, PF‐00835231. In the noncovalent complex the carbonyl oxygen atom of the warhead is placed in the oxyanion hole formed by residues 143 to 145, while P1–P3 groups are accommodated in the active site with interactions similar to those observed for the peptide substrate. According to alchemical free energy calculations, the P1′ hydroxymethyl group also contributes to the binding free energy. Covalent inhibition of the enzyme is triggered by the proton transfer from Cys145 to His41. This step is followed by the nucleophilic attack of the Sγ atom on …

KetoneMolecular modelStereochemistrySubstituentMolecular Dynamics SimulationSARS‐CoV‐2 Inhibitors | Hot PaperCatalysisQM/MM3CL proteasechemistry.chemical_compoundCatalytic DomaininhibitorsHumansHydroxymethylProtease InhibitorsCoronavirus 3C ProteasesResearch Articleschemistry.chemical_classificationPF-00835231Binding SitesbiologySARS-CoV-2molecular modelingActive siteCOVID-19General ChemistryGeneral MedicineKetonesCOVID-19 Drug TreatmentKineticschemistryCovalent bondDrug Designbiology.proteinThermodynamicsOxyanion holeResearch ArticleAngewandte Chemie
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Obesity, type 2 diabetes and risk of digestive cancer.

2010

The frequency of obesity has been increasing worldwide for 20 years. Many epidemiological studies support a correlation between obesity and increased risk of cancer, particularly digestive cancers in both genders, and gynaecological cancer in women. Currently, about 5% of cancers could be directly related to overweight. Carcinogenesis mechanisms induced by obesity involve insulin resistance, adipokine and angiogenic factor secretions, and inflammation. Experimental and clinical evidence suggest that insulin resistance plays a major role in carcinogenesis. Insulin and non-protein banded IGF-1, whose levels are increased in type 2 diabetes, stimulate cellular growth and inhibit apoptosis. Abn…

Leptinmedicine.medical_specialtySerine Proteinase Inhibitorsmedicine.medical_treatmentAdipokineType 2 diabetesOverweightBioinformaticsGlobal HealthRisk AssessmentBody Mass IndexDiabetes ComplicationsBiological FactorsInsulin resistanceAdipokinesRisk FactorsInternal medicineDiabetes mellitusPlasminogen Activator Inhibitor 1PrevalenceMedicineHumansInsulinAdiponectin secretionObesityInsulin-Like Growth Factor IGastrointestinal NeoplasmsEvidence-Based Medicinebusiness.industryInsulinIncidenceGastroenterologyCancerGeneral Medicinemedicine.diseasePrognosisEndocrinologyAdipose TissueDiabetes Mellitus Type 2MetalloproteasesFrancemedicine.symptomInsulin ResistancebusinessGastroenterologie clinique et biologique
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The prophenoloxidase system is activated during the tunic inflammatory reaction of Ciona intestinalis

2008

Phenoloxidase (PO) activity was examined in the tunic tissue of Ciona intestinalis following lipopolysaccharide (LPS) intratunic injection. Tunic homogenate supernatant (THS), assayed with the Dopa-MBTH reaction, displayed Ca(2+)-independent PO activity that was raised by LPS and further enhanced by proteases. Specific inhibitors (tropolone, phenylthiourea, diethylthiocarbamate) supported the specificity of the reaction. Assay with soybean trypsin inhibitor showed that, in the tunic, PO activation with trypsin was not significantly inhibited suggesting that proteases diverse from serine proteases were involved. In vivo experiments were carried out by injecting isosmotic medium or LPS, and T…

LipopolysaccharidesProteasesHistologyBlotting WesternSettore BIO/05 - ZoologiaEnzyme-Linked Immunosorbent AssayPathology and Forensic MedicinemedicineAnimalsCiona intestinalisInflammationchemistry.chemical_classificationEnzyme PrecursorsbiologyKunitz STI protease inhibitorprophenoloxidase Ciona intestinalisCell BiologyProphenoloxidasebiology.organism_classificationTrypsinImmunohistochemistryMolecular biologyIn vitroCiona intestinalisUp-RegulationCionaEnzymechemistryPhenoloxidase . Hemocyte . Tunic . Inflammation . Lipopolysaccharide . SDS-polyacrylamide gel electrophoresis . Ciona intestinalisElectrophoresis Polyacrylamide GelCatechol Oxidasemedicine.drugCell and Tissue Research
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Mer Tyrosine Kinase (MERTK) modulates liver fibrosis progression and hepatocellular carcinoma development.

2022

BackgroundMerTK is a tyrosine kinase receptor that belongs to the TAM (Tyro3/Axl/Mer) receptor family. It is involved in different processes including cellular proliferation/survival, cellular adhesion/migration, and release of the inflammatory/anti-inflammatory cytokines. Although it is reported that MERTK polymorphisms affect the severity of viral and metabolic liver diseases, being able to influence fibrosis progression and hepatocellular carcinoma development, the mechanisms remain unknown. Methods: using a microarray approach, we evaluated the liver expression of genes involved in fibrogenesis and hepatocarcinogenesis in patient with chronic hepatitis C (CHC), stratified for MERTK geno…

Liver CirrhosisSettore MED/12 - GastroenterologiaCarcinoma Hepatocellularc-Mer Tyrosine KinaseMer Tyrosine Kinase polymorphism (MERTK polymorphism) WNT gene family pathway (WNT pathway) hepatocellular carcinoma liver fibrosis matrix metallopeptidase Metalloproteases Protein-Tyrosine Kinases Liver CirrhosisImmunologyLiver NeoplasmsProtein-Tyrosine KinasesFibrosisSettore BIO/13 - Biologia ApplicataProto-Oncogene ProteinsMetalloproteasesImmunology and AllergyHumansFrontiers in immunology
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New Tetromycin Derivatives with Anti-Trypanosomal and Protease Inhibitory Activities

2011

Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001(T) cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV M(pro), and PL(pro). The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteas…

Magnetic Resonance Spectroscopyanti-trypanosomalmedicine.medical_treatmentCathepsin LStreptomyces axinellaePharmaceutical ScienceCathepsin BCathepsin BCathepsin LCathepsin ODrug DiscoveryPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5Coronavirus 3C ProteasesLeishmania major0303 health sciencesbiology030302 biochemistry & molecular biologytetromycin; anti-trypanosomal; protease inhibition; <em>Streptomyces axinellae</em>; marine spongeTrypanocidal AgentsStreptomycesCysteine EndopeptidasesBiochemistrySevere acute respiratory syndrome-related coronavirusStreptomyces axinellaetetromycinBiologiemarine spongeddc:547ProteasesTrypanosoma brucei bruceiAntiprotozoal AgentsTrypanosoma bruceiHeterocyclic Compounds 4 or More RingsArticle03 medical and health sciencesViral ProteinsAxinellaparasitic diseasesmedicineAnimalsProtease Inhibitorsddc:610protease inhibition ; anti-trypanosomal ; Streptomyces axinellae ; tetromycin ; marine sponge030304 developmental biologyCathepsinProteasebiology.organism_classificationprotease inhibitionlcsh:Biology (General)biology.protein
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Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida

2017

Study question How and where is pro-ovastacin activated and how does active ovastacin regulate zona pellucida hardening (ZPH) and successful fertilization? Study finding Ovastacin is partially active before exocytosis and pre-hardens the zona pellucida (ZP) before fertilization. What is known already The metalloproteinase ovastacin is stored in cortical granules, it cleaves zona pellucida protein 2 (ZP2) upon fertilization and thereby destroys the ZP sperm ligand and triggers ZPH. Female mice deficient in the extracellular circulating ovastacin-inhibitor fetuin-B are infertile due to pre-mature ZPH. Study design, samples/materials, methods We isolated oocytes from wild-type and ovastacin-de…

Male0301 basic medicineEmbryologyPrimary Cell CultureFertilization in VitroBiologyCleavage (embryo)Zona Pellucida GlycoproteinsExocytosisExocytosisMice03 medical and health sciences0302 clinical medicineHuman fertilizationGeneticsmedicineAnimalsChymotrypsinZona pellucidaMolecular BiologyMetaphaseZona PellucidaOriginal Research030219 obstetrics & reproductive medicineGene Expression Regulation DevelopmentalObstetrics and GynecologyOocyte activationEmbryoCell BiologyPolyspermySpermatozoaSpermFetuin-BCell biology030104 developmental biologymedicine.anatomical_structureReproductive MedicineProteolysisMetalloproteasesOocytesFemaleSignal TransductionDevelopmental Biology
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Gluten Degrading Enzymes for Treatment of Celiac Disease

2020

Celiac disease (CeD) affects about 1% of most world populations. It presents a wide spectrum of clinical manifestations, ranging from minor symptoms to mild or severe malabsorption, and it may be associated with a wide variety of autoimmune diseases. CeD is triggered and maintained by the ingestion of gluten proteins from wheat and related grains. Gluten peptides that resist gastrointestinal digestion are antigenically presented to gluten specific T cells in the intestinal mucosa via HLA-DQ2 or HLA-DQ8, the necessary genetic predisposition for CeD. To date, there is no effective or approved treatment for CeD other than a strict adherence to a gluten-free diet, which is difficult to maintain…

Male0301 basic medicineProteasesGlutensDrug CompoundingT-Lymphocytesenzyme therapylcsh:TX341-641ReviewBiologyDiet Gluten-Free03 medical and health sciences0302 clinical medicineAntigenIntestinal mucosaglutenasewheatHLA-DQ AntigensEnzyme StabilityGenetic predispositionHumansGenetic Predisposition to Diseaseenteric coatingSubtilisinsendopeptidasechemistry.chemical_classificationNutrition and Dieteticstreatmentfungiautoimmunitynutritional and metabolic diseasesGlutendigestive system diseasesGlutamine030104 developmental biologyEnzymeBiochemistrychemistryglutenProteolysisFemale030211 gastroenterology & hepatologyProlyl OligopeptidasesSubtilisinslcsh:Nutrition. Foods and food supplyceliac diseaseFood ScienceNutrients
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Role of meprins to protect ileal mucosa of Crohn's disease patients from colonization by adherent-invasive E. coli

2011

Ileal lesions in Crohn's disease (CD) patients are colonized by pathogenic adherent-invasive Escherichia coli (AIEC) able to adhere to and invade intestinal epithelial cells (IEC), and to survive within macrophages. The interaction of AIEC with IEC depends on bacterial factors mainly type 1 pili, flagella, and outer membrane proteins. In humans, proteases can act as host defence mechanisms to counteract bacterial colonization. The protease meprin, composed of multimeric complexes of the two subunits alpha and beta, is abundantly expressed in IECs. Decreased levels of this protease correlate with the severity of the inflammation in patients with inflammatory bowel disease. The aim of the pre…

MaleBacterial Diseasesmedicine.medical_treatmentACTIVATION MECHANISMBiochemistryBacterial AdhesionPilusMice0302 clinical medicineCrohn DiseaseIntestinal mucosaMolecular Cell BiologyGastrointestinal InfectionsIntestinal MucosaAged 80 and over0303 health sciencesMultidisciplinaryQRMetalloendopeptidasesMiddle AgedEnzymesBacterial Pathogens3. Good healthHost-Pathogen InteractionInfectious DiseasesCytokineESCHERICHIA-COLI030220 oncology & carcinogenesisAlimentation et NutritionMedicineFemaleINFLAMMATORY-BOWEL-DISEASE;INTESTINAL EPITHELIAL-CELLS;URINARY-TRACT-INFECTIONS;ESCHERICHIA-COLI;ALPHA-SUBUNIT;STRAIN LF82;METALLOPROTEASE MEPRIN;ACTIVATION MECHANISM;BETA-SUBUNIT;TYPE-1 PILICellular Typesmedicine.symptomBacterial outer membraneALPHA-SUBUNITResearch ArticleAdultProteasesScienceMédecine humaine et pathologieInflammationGastroenterology and HepatologyBiologyMETALLOPROTEASE MEPRINMicrobiologyMicrobiologyURINARY-TRACT-INFECTIONS03 medical and health sciencesTYPE-1 PILIEscherichia colimedicineAnimalsHumansFood and NutritionSecretionInterleukin 8BETA-SUBUNITBiologyAged030304 developmental biologySTRAIN LF82Interleukin-8Inflammatory Bowel DiseaseEpithelial Cellsdigestive system diseasesMice Inbred C57BLHuman health and pathologyINTESTINAL EPITHELIAL-CELLS[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyINFLAMMATORY-BOWEL-DISEASE
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Morphological studies on CLN2

2001

Electron microscopic, fluorescence microscopic, and immunohistochemical studies earlier performed on archivalcerebral tissue from Max Bielchowsky's original three patients revealed curvilinear bodies rich in subunit C of mitochondrial ATP synthase (SCMAS). Recent progress in the elucidation of CLN2, i.e. identification of the defective lysosomal enzyme tripeptidyl-peptidase I (TPP-I) and mutations in the CLN2 gene have further corroborated earlier data. Immunohistochemically the absence of the TPP-I protein could be confirmed in the archival tissues using pathological controls. Unlike biochemistry, immunohistochemistry enables examination of these archival tissues elucidating the causative …

MaleCell typePathologymedicine.medical_specialtyProtein subunitEncephalopathyBiologymedicine.disease_causeAminopeptidasesNeuronal Ceroid-LipofuscinosesChloroquineEndopeptidasesmedicineHumansChildDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMyopathyGeneMutationTripeptidyl-Peptidase 1BrainGeneral MedicineMitochondrial Proton-Translocating ATPasesmedicine.diseaseImmunohistochemistryProton-Translocating ATPasesMutationPediatrics Perinatology and Child HealthImmunohistochemistryFemaleNeurology (clinical)Serine Proteasesmedicine.symptomPeptide Hydrolasesmedicine.drugEuropean Journal of Paediatric Neurology
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