Search results for "Peptidase"

showing 10 items of 567 documents

Fractionated External Beam Radiotherapy as a Suitable Preparative Regimen for Hepatocyte Transplantation After Partial Hepatectomy

2010

Purpose Hepatocyte transplantation is strongly considered to be a promising option to correct chronic liver failure through repopulation of the diseased organ. We already reported on extensive liver repopulation by hepatocytes transplanted into rats preconditioned with 25-Gy single dose selective external beam irradiation (IR). Herein, we tested lower radiation doses and fractionated protocols, which would be applicable in clinical use. Methods and Material Livers of dipeptidylpeptidase IV (DPPIV)-deficient rats were preconditioned with partial liver external beam single dose IR at 25 Gy, 8 Gy, or 5 Gy, or fractionated IR at 5 × 5 Gy or 5 × 2 Gy. Four days after completion of IR, a partial …

Cancer ResearchTransplantation ConditioningDipeptidyl Peptidase 4medicine.medical_treatmentmedicineAnimalsHepatectomyRadiology Nuclear Medicine and imagingExternal beam radiotherapyPreparative RegimenRadiationbusiness.industryDose fractionationRatsRadiation therapyTransplantationmedicine.anatomical_structureLiverOncologyHepatocyteHepatocytesDose Fractionation RadiationTransplantation ConditioningHepatectomyNuclear medicinebusinessBiomarkersInternational Journal of Radiation Oncology*Biology*Physics
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Tetanus Toxin Inhibits Neuroexocytosis Even When Its Zn2+-dependent Protease Activity Is Removed

1995

Tetanus toxin (TeTX) is a dichain protein that blocks neuroexocytosis, an action attributed previously to Zn(2+)-dependent proteolysis of synaptobrevin (Sbr) by its light chain (LC). Herein, its cleavage of Sbr in rat cerebrocortical synaptosomes was shown to be minimized by captopril, an inhibitor of certain metalloendoproteases, whereas this agent only marginally antagonized the inhibition of noradrenaline release, implicating a second action of the toxin. This hypothesis was proven by preparing three mutants (H233A, E234A, H237A) of the LC lacking the ability to cleave Sbr and reconstituting them with native heavy chain. The resultant dichains were found to block synaptosomal transmitter…

CaptoprilSynaptobrevinProteolysismedicine.medical_treatmentGuinea PigsInhibitory postsynaptic potentialmedicine.disease_causeBiochemistryExocytosisNorepinephrinechemistry.chemical_compoundTetanus ToxinCadaverineAplysiaEndopeptidasesmedicineAnimalsEnzyme InhibitorsNeurotransmitterMolecular BiologyCerebral CortexTransglutaminasesProteasemedicine.diagnostic_testbiologyToxinHydrolysisWild typeCell Biologybiology.organism_classificationRecombinant ProteinsRatsZincBiochemistrychemistryAplysiaBiophysicsSynaptosomesJournal of Biological Chemistry
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SGLT2 Inhibitors as the Most Promising Influencers on the Outcome of Non-Alcoholic Fatty Liver Disease

2022

Non-alcoholic fatty liver disease (NAFLD), the most frequent liver disease in the Western world, is a common hepatic manifestation of metabolic syndrome (MetS). A specific cure has not yet been identified, and its treatment is currently based on risk factor therapy. Given that the initial accumulation of triglycerides in the liver parenchyma, in the presence of inflammatory processes, mitochondrial dysfunction, lipotoxicity, glucotoxicity, and oxidative stress, can evolve into non-alcoholic steatohepatitis (NASH). The main goal is to identify the factors contributing to this evolution because, once established, untreated NASH can progress through fibrosis to cirrhosis and, ultimately, be co…

Carcinoma HepatocellularSettore MED/09 - Medicina Internatype 2 diabetes mellituSGLT2metabolic syndromeCatalysisInorganic ChemistryNon-alcoholic Fatty Liver DiseaseNAFLDAnimalsHumansHypoglycemic AgentsPhysical and Theoretical ChemistrySodium-Glucose Transporter 2 InhibitorsMolecular BiologySpectroscopyDipeptidyl-Peptidase IV InhibitorsHypoglycemic AgentLiver NeoplasmsOrganic Chemistrynutritional and metabolic diseasesGeneral Medicinedigestive system diseasesComputer Science ApplicationsGlucoseLiverDiabetes Mellitus Type 2HumanInternational Journal of Molecular Sciences
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Synergistic Effect of Carfilzomib and Metformin in Vascular Plasticity; The Emerging Role of Autophagy

2019

Introduction: Carfilzomib (Cfz) correlates with a risk of reversible cardiotoxicity in 5-10% of multiple myeloma (MM) patients. We have recently shown that metformin (Met) has a prophylactic role against the Cfz-induced cardiotoxicity in vivo, through activation of AMPKα signaling (Blood 2019;133:710-23). However, the impact of Cfz on vascular function is obscure. Therefore, we sought to investigate: i) the acute, ii) the sub-chronic effect of Cfz on the vascular reactivity, iii) the effect of metformin co-administration on the vascular phenotype and iv) the impact of Cfz and Met co-administration on aged Human Aortic Smooth Muscle Cells (HAoSMCs). Methods: Forty male C57Bl/6 mice were assi…

CardiotoxicityMulticatalytic endopeptidase complexbusiness.industryMTOR Serine-Threonine KinasesImmunologyAutophagyCell BiologyHematologyBiochemistryCarfilzomibAngiotensin IIMetforminchemistry.chemical_compoundchemistryAnimals laboratoryCancer researchmedicinebusinessmedicine.drugBlood
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Fetuin-A and Cystatin C Are Endogenous Inhibitors of Human Meprin Metalloproteases

2010

Meprin α and β, zinc metalloproteinases, play significant roles in inflammation, including inflammatory bowel disease (IBD), possibly by activating cytokines, like interleukin 1β, interleukin 18, or tumor growth factor α. Although a number of potential activators for meprins are known, no endogenous inhibitors have been identified. In this work, we analyzed the inhibitory potential of human plasma and identified bovine fetuin-A as an endogenous meprin inhibitor with a K(i) (inhibition constant) of 4.2 × 10(-5) M for meprin α and a K(i) of 1.1 × 10(-6) M meprin β. This correlated with data obtained for a fetuin-A homologue from carp (nephrosin inhibitor) that revealed a potent meprin α and β…

Carpsalpha-2-HS-GlycoproteinMolecular Sequence DataMatrix metalloproteinaseBiochemistryPlasma03 medical and health sciencesmedicineAnimalsHumansAmino Acid SequenceCystatin C030304 developmental biology0303 health sciencesMetalloproteinasebiology030302 biochemistry & molecular biologyProteolytic enzymesMetalloendopeptidasesBlood ProteinsTrypsinFetuinProtease inhibitor (biology)3. Good healthBiochemistryCystatin Cbiology.proteinCattleCystatinSequence Alignmentmedicine.drugBiochemistry
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Silicateins, the major biosilica forming enzymes present in demosponges: protein analysis and phylogenetic relationship.

2007

Silicateins are enzymes, which are restricted to sponges (phylum Porifera), that mediate the catalytic formation of biosilica from monomeric silicon compounds. The silicatein protein is compartmented in the sponges in the axial filaments which reside in the axial canals of the siliceous spicules. In the present study silicatein has been isolated from the freshwater sponge Lubomirskia baicalensis where it occurs in isoforms with sizes of 23 kDa, 24 kDa and 26 kDa. Since the larger protein is glycosylated we posit that it is a processed form of one of the smaller size forms. The silicatein isoforms are post-translationally modified by phosphorylation; at least four isoforms exist with pI's of…

Cathepsin LMolecular Sequence DataCathepsin LDemospongeCatalytic triadGeneticsAnimalsAmino Acid SequenceGenePeptide sequencePhylogenyCathepsinbiologySequence Homology Amino AcidGeneral MedicineExonsbiology.organism_classificationSilicon DioxideCathepsinsIntronsPoriferaSuberites domunculaSpongeCysteine EndopeptidasesMicroscopy ElectronBiochemistrybiology.proteinGene
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Altered morphological and electrophysiological properties of Cajal-Retzius cells in cerebral cortex of embryonic Presenilin-1 knockout mice

2004

Mutations of Presenilin-1 are the major cause of familial Alzheimer's disease. Presenilin-1 knockout (PS1-/-) mice develop severe cortical dysplasia related to human type 2 lissencephaly. This overmigration syndrome has been attributed to the premature loss of Cajal-Retzius cells (CRcs), pioneer neurons required for the termination of radial neuronal migration. To elucidate the potential cellular mechanisms responsible for this premature neuronal loss, we investigated the morphological and electrophysiological properties of visually identified CRcs of wild-type (WT) and PS1-/- mouse brains at embryonic day 16.5. The density of CRcs was substantially reduced in the cerebral cortex of PS1-/-.…

Cell Adhesion Molecules NeuronalNerve Tissue ProteinsBiologyBicucullineMembrane PotentialsGABA AntagonistsMicemental disordersExcitatory Amino Acid AgonistsPresenilin-1medicineAnimalsneoplasms6-Cyano-7-nitroquinoxaline-23-dioneCerebral CortexMice KnockoutNeuronsMembrane potentialExtracellular Matrix ProteinsGABAA receptorStem CellsGeneral NeuroscienceSerine EndopeptidasesExcitatory Postsynaptic PotentialsMembrane ProteinsCortical dysplasiaBicucullineEmbryo Mammalianmedicine.diseaseImmunohistochemistryElectric Stimulationdigestive system diseasesnervous system diseasesCell biologyReelin ProteinElectrophysiologymedicine.anatomical_structure2-Amino-5-phosphonovaleratenervous systemCerebral cortexKnockout mouseExcitatory postsynaptic potentialExcitatory Amino Acid AntagonistsNeurosciencemedicine.drugEuropean Journal of Neuroscience
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Autocatalytic cleavage of Clostridium difficile toxin B.

2007

Clostridium difficile, the causative agent of nosocomial antibiotic-associated diarrhoea and pseudomembranous colitis, possesses two main virulence factors: the large clostridial cytotoxins A and B. It has been proposed that toxin B is cleaved by a cytosolic factor of the eukaryotic target cell during its cellular uptake. Here we report that cleavage of not only toxin B, but also all other large clostridial cytotoxins, is an autocatalytic process dependent on host cytosolic inositolphosphate cofactors. A covalent inhibitor of aspartate proteases, 1,2-epoxy-3-(p-nitrophenoxy)propane, completely blocked toxin B function on cultured cells and was used to identify its catalytically active prote…

Cell ExtractsProteasesPhytic AcidSwineVirulence Factorsmedicine.medical_treatmentBacterial ToxinsClostridium difficile toxin AVirulenceClostridium difficile toxin Bmedicine.disease_causeCatalysisMicrobiologyCell LineNitrophenolsBiological FactorsBacterial ProteinsmedicineAnimalsAspartic Acid EndopeptidasesMultidisciplinaryProteaseBinding SitesToxinChemistryClostridioides difficilePseudomembranous colitisClostridium difficileProtein TransportBiochemistryEpoxy CompoundsProtein Processing Post-TranslationalSpleenNature
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Inhibitors of Rho-kinase modulate amyloid-β (Aβ) secretion but lack selectivity for Aβ42

2005

Certain non-steroidal anti-inflammatory drugs (NSAIDs) preferentially inhibit production of the amyloidogenic Abeta42 peptide, presumably by direct modulation of gamma-secretase activity. A recent report indicated that NSAIDs could reduce Abeta42 by inhibition of the small GTPase Rho, and a single inhibitor of Rho kinase (ROCK) mimicked the effects of Abeta42-lowering NSAIDs. To investigate whether Abeta42 reduction is a common property of ROCK inhibitors, we tested commercially available compounds in cell lines that were previously used to demonstrate the Abeta42-lowering activity of NSAIDs. Surprisingly, we found that two ROCK inhibitors reduced total Abeta secretion in a dose-dependent m…

Cell SurvivalMutantPeptideCHO CellsProtein Serine-Threonine KinasesPharmacologyBiochemistryAmyloid beta-Protein PrecursorCellular and Molecular NeuroscienceCricetulusCricetinaeEndopeptidasesmental disordersAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesSecretionSmall GTPaseEnzyme InhibitorsRho-associated protein kinasechemistry.chemical_classificationrho-Associated KinasesAmyloid beta-PeptidesbiologyAnti-Inflammatory Agents Non-SteroidalIntracellular Signaling Peptides and ProteinsIn vitro toxicologyProtein-Tyrosine KinasesPeptide Fragmentsnervous system diseasesBiochemistrychemistrybiology.proteinAmyloid Precursor Protein SecretasesSelectivityProtein Processing Post-TranslationalJournal of Neurochemistry
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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