Search results for "proteolytic enzyme"

showing 10 items of 60 documents

Brain met-enkephalin immunostaining after subacute and subchronic exposure to benzene

1994

Benzene is used in a wide variety of domestic and occupational activities, and due to its lipophilic nature, it accumulates in lipid-rich tissues like the brain. In this sense, neurotoxic action has long been associated with organic solvent exposure and it has been shown that benzene, injected in a single dose or during a prolongued administration, modifies the content of dopamine, noradrenaline, serotonin and its main metabolite 5-hydroxy indolacetic acid, in several brain regions of the rat, then revealing a stimulating action on brain monoamine synthesis and turnover. However, information concerning neurotoxic action of benzene exposure in vivo on peptidergic neuromodulatory systems is s…

MaleMet-enkephalinmedicine.medical_specialtyTime FactorsEnkephalin MethionineHealth Toxicology and MutagenesisCentral nervous systemNeuropeptideBiologyToxicologyRats Sprague-Dawleychemistry.chemical_compoundDopamineInternal medicineImage Processing Computer-AssistedmedicineAnimalsBrain ChemistryStaining and LabelingProteolytic enzymesBrainBenzeneGeneral MedicinePollutionRatsEndocrinologyMonoamine neurotransmittermedicine.anatomical_structurechemistryImmunologic TechniquesSerotoninImmunostainingmedicine.drugBulletin of Environmental Contamination and Toxicology
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Prognostic value of tissue inhibitor of metalloproteinase-1 for cardiovascular death among patients with cardiovascular disease: results from the Ath…

2005

Aims Metalloproteinases are proteolytic enzymes, which decompose the extracellular matrix, influence cardiac remodelling, and are inhibited by tissue inhibitor of metalloproteinases (TIMPs). Little is known about the prognostic impact of the TIMP-1/matrix metalloproteinase complex in patients with future cardiovascular death. Methods and results In 1979 patients with suspected coronary artery disease (CAD), TIMP-1 has been determined at baseline. Among 1945 (98.4%) patients with a mean follow-up period of 2.6±1.2 years, 75 patients died because of cardiovascular causes. Mean concentrations of TIMP-1 were higher among patients who experienced a fatal cardiovascular event than among those who…

Malemedicine.medical_specialtymedicine.drug_classDiseaseCoronary Artery DiseaseCoronary artery diseaseRisk FactorsInternal medicinemedicineNatriuretic peptideHumansTissue Inhibitor of Metalloproteinase-1business.industryHazard ratioConfoundingProteolytic enzymesTissue inhibitor of metalloproteinaseMiddle Agedmedicine.diseasePrognosisEndocrinologyCardiovascular DiseasesCirculatory systemCardiologyFemaleCardiology and Cardiovascular MedicinebusinessBiomarkersFollow-Up StudiesEuropean heart journal
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Atomic-force microscopy imaging of plasma membranes purified from spinach leaves

2000

Summary: Plasma membranes purified from spinach leaves by aqueous two-phase partitioning were examined by atomic-force microscopy (AFM) in phosphate buffer, and details on their structure were reported at nanometric scale. Examination of the fresh membrane preparation deposited on mica revealed a complex organization of the surface. It appeared composed of a first layer of material, about 8 nm in thickness, that practically covered all the mica surface and on which stand structures highly heterogeneous in shape and size. High-resolution imaging showed that the surface of the first layer appeared relatively smooth in some regions, whereas different characteristic features were observed in ot…

Materials scienceAqueous solutionbiologyProteolytic enzymesAtomic-force microscopyCell BiologyPlant ScienceGeneral MedicineSurface finishSpinachbiology.organism_classificationLeaf cellsPlasmalemmaMembraneddc:580Chemical engineeringBiochemistryPhase partitionMicroscopySpinachMicaLayer (electronics)
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Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength.

2013

Type I fibrillar collagen is the most abundant protein in the human body, crucial for the formation and strength of bones, skin, and tendon. Proteolytic enzymes are essential for initiation of the assembly of collagen fibrils by cleaving off the propeptides. We report that Mep1a −/− and Mep1b −/− mice revealed lower amounts of mature collagen I compared with WT mice and exhibited significantly reduced collagen deposition in skin, along with markedly decreased tissue tensile strength. While exploring the mechanism of this phenotype, we found that cleavage of full-length human procollagen I heterotrimers by either meprin α or meprin β led to the generation of mature collagen molecules that s…

Materials scienceConnective tissueCHO CellsCollagen Type IMiceCricetulusFibrosisCricetinaeTensile StrengthmedicineAnimalsHumansProtein precursorSkinMice KnockoutMetalloproteinaseMultidisciplinaryProteolytic enzymesMetalloendopeptidasesProcollagen N-EndopeptidaseBiological Sciencesmedicine.diseaseCell biologyProcollagen peptidaseCollagen type I alpha 1medicine.anatomical_structureHEK293 CellsBiochemistryProteolysisProcollagen N-EndopeptidaseProceedings of the National Academy of Sciences of the United States of America
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Vibrio Proteases for Biomedical Applications: Modulating the Proteolytic Secretome of V. alginolyticus and V. parahaemolyticus for Improved Enzymes P…

2019

Proteolytic enzymes are of great interest for biotechnological purposes, and their large-scale production, as well as the discovery of strains producing new molecules, is a relevant issue. Collagenases are employed for biomedical and pharmaceutical purposes. The high specificity of collagenase-based preparations toward the substrate strongly relies on the enzyme purity. However, the overall activity may depend on the cooperation with other proteases, the presence of which may be essential for the overall enzymatic activity, but potentially harmful for cells and tissues. Vibrios produce some of the most promising bacterial proteases (including collagenases), and their exo-proteome includes s…

Microbiology (medical)ProteasesV. alginolyticusproteases productionMicrobiologyArticle<i>V. parahaemolyticus</i>03 medical and health sciences<i>V. alginolyticus</i>V. AlginolyticuSettore BIO/10 - BiochimicaVirologymedicinelcsh:QH301-705.5030304 developmental biology2. Zero hungerchemistry.chemical_classificationVibrio alginolyticus0303 health sciencesbiology030306 microbiologyChemistryVibrio parahaemolyticusProteolytic enzymesSubstrate (chemistry)biology.organism_classificationVibriocollagenaseEnzymeBiochemistrylcsh:Biology (General)proteolytic secretomeCollagenaseV. parahaemolyticusmedicine.drugMicroorganisms
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A synthetic method for diversification of the P1′ substituent in phosphinic dipeptides as a tool for exploration of the specificity of the S1′ bindin…

2007

Abstract A novel, general, and versatile method of diversification of the P1′ position in phosphinic pseudodipeptides, presumable inhibitors of proteolytic enzymes, was elaborated. The procedure was based on parallel derivatization of the amino group in the suitably protected phosphinate building blocks with appropriate alkyl and aryl halides. This synthetic strategy represents an original approach to phosphinic dipeptide chemistry. Its usefulness was confirmed by obtaining a series of P1′ modified phosphinic dipeptides, inhibitors of cytosolic leucine aminopeptidase, through computer-aided design basing on the structure of homophenylalanyl-phenylalanine analogue (hPheP[CH 2 ]Phe) bound in …

Models MolecularStereochemistryClinical BiochemistryLAP inhibitorsSubstituentPharmaceutical SciencePhosphinateLigandsBiochemistryAminopeptidaseLeucyl AminopeptidaseStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoveryP1′ diversificationcross-couplingMolecular BiologyalkylationBinding SitesDipeptideMolecular StructurebiologyOrganic ChemistryProteolytic enzymesActive siteHydrogen BondingStereoisomerismDipeptidesPhosphinic Acidsphosphinic pseudodipeptideschemistrybiology.proteinMolecular MedicineLeucineLead compoundBioorganic & Medicinal Chemistry
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Comprehensive analysis of a Vibrio parahaemolyticus strain extracellular serine protease VpSP37

2015

Proteases play an important role in the field of tissue dissociation combined with regenerative medicine. During the years new sources of proteolytic enzymes have been studied including proteases from different marine organisms both eukaryotic and prokaryotic. Herein we have purified a secreted component of an isolate of Vibrio parahaemolyticus, with electrophoretic mobilities corresponding to 36 kDa, belonging to the serine proteases family. Sequencing of the N-terminus enabled the in silico identification of the whole primary structure consisting of 345 amino acid residues with a calculated molecular mass of 37.4 KDa. The purified enzyme, named VpSP37, contains a Serine protease domain be…

Models MolecularTMPRSS6Proteasesmedicine.medical_treatmentMolecular Sequence Datalcsh:MedicineBiologySettore BIO/19 - Microbiologia GeneraleSubstrate SpecificitySerine03 medical and health sciencesSettore BIO/10 - BiochimicamedicineAnimalsAmino Acid Sequencelcsh:Science030304 developmental biologySerine protease0303 health sciencesMultidisciplinaryProteaseEelsVibrio parahaemolyticuBiochemistry Genetics and Molecular Biology (all)030306 microbiologyAnimalMedicine (all)lcsh:RProteolytic enzymesEelVibrio InfectionTrypsinMolecular biology3. Good healthBiochemistryAgricultural and Biological Sciences (all)Vibrio InfectionsAmino Acid Sequence; Animals; Eels; Models Molecular; Molecular Sequence Data; Sequence Alignment; Serine Proteases; Substrate Specificity; Vibrio Infections; Vibrio parahaemolyticus; Agricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)biology.proteinlcsh:QVibrio parahaemolyticusSerine ProteaseSerine ProteasesSequence AlignmentMASP1medicine.drugResearch Article
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Roles of molecules involved in epithelial/mesenchymal transition during angiogenesis

2007

Formation of vessels requires "epithelial-mesenchymal" transition of endothelial cells, with several modifications at the level of endothelial cell plasma membranes. These processes are associated with redistribution of cell-cell and cell-substrate adhesion molecules, cross talk between external ECM and internal cytoskeleton through focal adhesion molecules and the expression of several proteolytic enzymes, including matrix metalloproteases and serine proteases. These enzymes with their degradative action on ECM components, generate molecules acting as activators and/or inhibitors of angiogenesis. The purpose of this review is to provide an overview of the molecules involved in epithelial-m…

Neovascularization PathologicbiologyAngiogenesisCell adhesion moleculeChemistryIntegrinProteolytic enzymesEpithelial CellsCadherinsModels BiologicalEpitheliumExtracellular MatrixCell biologyMesodermFocal adhesionTumor progressionCell Adhesionbiology.proteinAnimalsHumansEpithelial–mesenchymal transitionEnzyme InhibitorsCell adhesionCell Adhesion MoleculesFrontiers in Bioscience
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Comparative study on enzymatic activity and molecules stability of some commercial proteolytic enzymes used in pancreatic islet isolation.

2009

In pancreatic islets purification, for cell therapy applications, the major enzymes used are obtained from Clostridium hystoliticum; class I and class II collagenases (COLL G and COLL H). They are used in a defined tissue dissociation enzyme (TDE) mixtures together neutral protease (Dispase) or thermolysin (Thermostable Neutral Protease). The TDE mixtures were in part responsible for the success of the Edmonton protocol; however, just to now, people working in islets purification found discrepancy in an application to another one. This variability in application see in the enzymatic blend composition the higher accused, such as the contamination from endotoxines due to extractive production…

Neutral proteaseSettore BIO/10 - BiochimicaCollagenases Proteolytic enzymes Pancreatic islet isolationCollagenaseDencitometry assayProteolytic enzyme
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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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