Search results for "metalloprotease"

showing 10 items of 42 documents

Sialotranscriptomics of the argasid tick ornithodoros moubata along the trophogonic cycle

2021

32 páginas, 8 tablas, 6 figuras

Proteomics0301 basic medicineSwinePhysiologyRC955-962Gene ExpressionDisease VectorsProteomicsBiochemistryTranscriptomeMedical Conditions0302 clinical medicineTicksArctic medicine. Tropical medicineGene expressionMedicine and Health SciencesHuman relapsing feverGeneticsbiologyEukaryotaGenomicsProteasesBody FluidsEnzymesBloodInfectious DiseasesFemaleMetabolic PathwaysAnatomyPublic aspects of medicineRA1-1270Transcriptome analysisVitellogeninsMetabolic Networks and PathwaysResearch ArticleIxodidaeArthropoda030231 tropical medicineTickSalivary glandsArthropod Proteins03 medical and health sciencesExocrine GlandsOrnithodoros moubataArachnidaGeneticsAnimalsXenobiotic MetabolismTick ControlOrnithodorosSalivaIllumina dye sequencingIxodesAsfarviridaeImmunityOrganismsPublic Health Environmental and Occupational HealthBiology and Life SciencesComputational BiologyProteinsGenome Analysisbiology.organism_classificationInvertebratesOrnithodoros moubataPhospholipases A2Species InteractionsMetabolism030104 developmental biologyAfricaEnzymologyMetalloproteasesAfrican swine feverTranscriptomeDigestive SystemZoology
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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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The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

2012

The in vivo roles of meprin metalloproteases in pathophysiological conditions remain elusive. Substrates define protease roles. Therefore, to identify natural substrates for human meprin α and β we employed TAILS (terminal amine isotopic labeling of substrates), a proteomics approach that enriches for N-terminal peptides of proteins and cleavage fragments. Of the 151 new extracellular substrates we identified, it was notable that ADAM10 (a disintegrin and metalloprotease domain-containing protein 10)—the constitutive α-secretase—is activated by meprin β through cleavage of the propeptide. To validate this cleavage event, we expressed recombinant proADAM10 and after preincubation with meprin…

Proteomicsalpha-2-HS-Glycoproteinmedicine.medical_treatmentADAM10ADAM10 ProteinMice0302 clinical medicine610 Medicine & healthMice KnockoutExtracellular Matrix Proteins0303 health sciencesMetalloproteinaseDegradomeMetalloendopeptidasesMeprinADAM10Terminal amine isotopic labeling of substratesADAM ProteinsElafinBiochemistryTAILSCytokinesMolecular MedicineElafinResearch Article610 Medicine & healthBiologyCell Line03 medical and health sciencesCellular and Molecular NeurosciencemedicineDisintegrinAnimalsHumansAmino Acid SequenceCystatin CMolecular Biology030304 developmental biologyPharmacologyProteaseMeprin; ADAM10; Metalloproteases; Proteomics; TAILS; DegradomeMembrane ProteinsCell BiologyADAM ProteinsHEK293 CellsMembrane proteinbiology.proteinMetalloproteases570 Life sciences; biologyAmyloid Precursor Protein SecretasesCaco-2 Cells030217 neurology & neurosurgery
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Heteroaromatic Inhibitors of the Astacin Proteinases Meprin α, Meprin β and Ovastacin Discovered by a Scaffold-Hopping Approach.

2020

Abstract Astacin metalloproteinases, in particular meprins α and β, as well as ovastacin, are emerging drug targets. Drug‐discovery efforts have led to the development of the first potent and selective inhibitors in the last few years. However, the most recent compounds are based on a highly flexible tertiary amine scaffold that could cause metabolic liabilities or decreased potency due to the entropic penalty upon binding to the target. Thus, the aim of this study was to discover novel conformationally constrained scaffolds as starting points for further inhibitor optimization. Shifting from flexible tertiary amines to rigid heteroaromatic cores resulted in a boost in inhibitory activity. …

ScaffoldTertiary amineStereochemistryCell SurvivalAntineoplastic Agentsscaffold hoppingMatrix metalloproteinaseScaffold hoppinghydroxamate01 natural sciencesBiochemistryHydrocarbons AromaticmetalloproteinasesStructure-Activity RelationshipmeprinVery Important PaperDrug DiscoveryTumor Cells CulturedHumansProtease InhibitorsGeneral Pharmacology Toxicology and PharmaceuticsAminesPharmacologyDose-Response Relationship DrugMolecular StructureFull Paper010405 organic chemistryChemistryOrganic ChemistryMetalloendopeptidasesFull PapersovastacinRecombinant Proteinsheteroaromatics0104 chemical sciences010404 medicinal & biomolecular chemistryMetalloproteasesMolecular MedicineAstacinDrug Screening Assays AntitumorSelectivityChemMedChem
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Interleukin 13 (IL-13)-regulated expression of the chondroprotective metalloproteinase ADAM15 is reduced in aging cartilage

2020

Objective The adamalysin metalloproteinase 15 (ADAM15) has been shown to protect against development of osteoarthritis in mice. Here, we have investigated factors that control ADAM15 levels in cartilage. Design Secretomes from wild-type and Adam15−/− chondrocytes were compared by label-free quantitative mass spectrometry. mRNA was isolated from murine knee joints, either with or without surgical induction of osteoarthritis on male C57BL/6 mice, and the expression of Adam15 and other related genes quantified by RT-qPCR. ADAM15 in human normal and osteoarthritic cartilage was investigated similarly and by fluorescent immunohistochemistry. Cultured HTB94 chondrosarcoma cells were treated with …

Senescencemedicine.medical_specialtyADAM15medicine.medical_treatmentOsteoarthritisDiseases of the musculoskeletal systemArticleMetalloproteaseAgeSettore BIO/13 - Biologia ApplicataInternal medicineOsteoarthritismedicineddc:610MetalloproteinaseMetalloproteinaseADAM15ChemistryCartilageAutophagyGeneral Medicinemedicine.diseasemedicine.anatomical_structureEndocrinologyCytokineRC925-935IL-13Interleukin 13OsteoarthritiOsteoarthritis and Cartilage Open
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Differing expression of metalloprotease and of adhesion molecules in signet-ring cell and intestinal colorectal carcinoma.

2009

Abstract. Background: Pure signet-ring cell colorectal carcinoma (SRCC) is an infrequent and highly malignant histological variant of colorectal cancer (CRC), while it is present as a histological component in colorectal carcinomas more frequently. Materials and Methods: The aim of this work was to widen the knowledge of the biological factors involved in the pathogenesis and aggressiveness of SRCC by the identification and evaluation of possible molecular abnormalities. By means of immunohistochemistry the expression of the proteolytic degradation enzyme matrix metalloprotease (MMP)-1, that is a collagenase specifically degrading collagens I, II, III and of the adhesion proteins Ecadherin,…

Settore MED/08 - Anatomia PatologicaColorectal cancer cadherin catenin fibronectin metalloprotease-1 signet-ring cell.
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Ulcere venose: rilievi riguardanti sia aspetti reologici e funzionali dei polimorfonucleati che le concentrazioni plasmatiche delle gelatinasi e dei …

2014

Settore MED/09 - Medicina Internametalloprotease chronic venous insufficiency granulocyte membrane
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Pharmacologic Inhibition of ADAM10 Attenuates Brain Tissue Loss, Axonal Injury and Pro-inflammatory Gene Expression Following Traumatic Brain Injury …

2021

The α-secretase A disintegrin and metalloprotease 10 (ADAM10) regulates various physiological and pathophysiological processes. Despite its broad functional implications during development, plasticity, and disease, no pharmacological approaches to inhibit ADAM10 in acute brain injury have been reported. Here, we examined the effects of the ADAM10 inhibitor GI254023X on the neurological and histopathological outcome after experimental traumatic brain injury (TBI). C57BL/6N mice were subjected to the controlled cortical impact (CCI) model of TBI or sham procedure and received GI254023X or vehicle during the acute phase of injury (n = 40, 100 mg/kg, 25% DMSO, 0.1 M Na2CO3, intraperitoneal, 30 …

Traumatic brain injuryADAM10PharmacologyBlood–brain barrierNeuroprotectionneuroinflammationaxonal injuryCell and Developmental Biologymedicinelcsh:QH301-705.5NeuroinflammationOriginal ResearchMicrogliabiologybusiness.industrytraumatic brain injuryADAM10 (a disintegrin and metalloprotease 10)Glutamate receptorCell Biologymedicine.diseaseGI254023Xmedicine.anatomical_structurelcsh:Biology (General)biology.proteinneuroprotectionGRIN2BbusinessDevelopmental BiologyFrontiers in Cell and Developmental Biology
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In Vivo Modulation of Angiogenesis and Immune Response on a Collagen Matrix via Extracorporeal Shockwaves

2020

The effective management of tissue integration and immunological responses to transplants decisively co-determines the success of soft and hard tissue reconstruction. The aim of this in vivo study was to evaluate the eligibility of extracorporeal shock wave therapy (ESWT) with respect to its ability to modulate angiogenesis and immune response to a collagen matrix (CM) for tissue engineering in the chorioallantoic membrane (CAM) assay, which is performed with fertilized chicken eggs. CM were placed on the CAM on embryonic development day (EDD) 7

Vascular Endothelial Growth Factor A0301 basic medicineAngiogenesismedicine.medical_treatmentNitric Oxide Synthase Type IIChick EmbryoChorioallantoic Membranelcsh:ChemistryNeovascularizationangiogenesischemistry.chemical_compoundmacrophage response0302 clinical medicineTissue engineeringlcsh:QH301-705.5Spectroscopyoral inflammationTissue Scaffoldsvascular endothelial growth factorGeneral MedicineComputer Science ApplicationsVascular endothelial growth factorChorioallantoic membraneExtracorporeal shockwave therapyCollagenmedicine.symptomchorioallantoic membrane assayNeovascularization PhysiologicArticleCatalysisAvian ProteinsInorganic ChemistryAndrology03 medical and health sciencesImmune systemIn vivomatrix metalloproteasesmucoderm®medicineAnimalsddc:610Physical and Theoretical Chemistrymucoderm<sup>®</sup>Molecular BiologyTissue Engineeringbusiness.industryOrganic Chemistrycollagen matrix030206 dentistryextracorporeal shockwave therapyHypoxia-Inducible Factor 1 alpha SubunitMatrix Metalloproteinases030104 developmental biologylcsh:Biology (General)lcsh:QD1-999chemistrybusiness
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Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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