Search results for "Endopeptidase"

showing 10 items of 361 documents

Antigen-processing machinery breakdown and tumor growth.

2000

Defects in the major histocompatibility complex (MHC) class I antigen-processing machinery (APM) have been described in tumors of different histology. Murine data suggest that defects in the MHC class II APM might also be associated with malignant transformation of human cells. This article describes the pathophysiology of the MHC class I and II APM, reviews APM abnormalities in tumor cells and discusses their role in the escape of tumor cells from in vitro recognition by T cells.

MHC class IIAntigen PresentationProteasome Endopeptidase ComplexbiologyAntigen processingImmunologyAntigen presentationHistocompatibility Antigens Class IHistocompatibility Antigens Class IIATP-binding cassette transporterMajor histocompatibility complexIn vitroMalignant transformationCysteine EndopeptidasesATP Binding Cassette Transporter Subfamily B Member 3Multienzyme ComplexesNeoplasmsMHC class IImmunologybiology.proteinCancer researchAnimalsHumansATP-Binding Cassette TransportersImmunology today
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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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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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Investigating the Vascular Toxicity Outcomes of the Irreversible Proteasome Inhibitor Carfilzomib

2020

Background: Carfilzomib&rsquo

Male0301 basic medicinevasculature030204 cardiovascular system & hematologyPharmacologyDinoprostEndoplasmic Reticulumlcsh:ChemistryMicechemistry.chemical_compound0302 clinical medicineAMP-Activated Protein Kinase Kinasesvascular smooth muscle cellsCytotoxicitylcsh:QH301-705.5endoplasmatic-reticulum stressSpectroscopychemistry.chemical_classificationcarfilzomibCobaltGeneral MedicineMetforminComputer Science ApplicationsRespiratory burstMetforminDrug Therapy CombinationGlycolysisOligopeptidesProteasome Inhibitorsmedicine.drugProteasome Endopeptidase ComplexautophagyCell SurvivalMyocytes Smooth MuscleAntineoplastic AgentsNitric OxideArticleCatalysisInorganic Chemistry03 medical and health sciencesmedicineAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyReactive oxygen speciesbusiness.industryOrganic ChemistryAutophagyCarfilzomibActinsVasoprotectiveMice Inbred C57BLGlucose030104 developmental biologychemistrylcsh:Biology (General)lcsh:QD1-999Proteasome inhibitorTumor Suppressor Protein p53Reactive Oxygen SpeciesbusinessProtein KinasesInternational Journal of Molecular Sciences
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Measurement of inflammatory mediators of mast cells and eosinophils in native nasal lavage fluid in nasal polyposis.

2001

&lt;i&gt;Background:&lt;/i&gt; Nasal polyposis (NP) often coexists with asthma, rhinitis and sinusitis. Polyp histology typically shows chronic, eosinophilic inflammation. The inflammatory cell infiltrate generally includes eosinophils, lymphocytes, plasma cells and mast cells. &lt;i&gt;Objective:&lt;/i&gt; To gain insight into the natural history of NP, we analysed mediator levels and leukocyte values in nasal fluids and eosinophil cationic protein (ECP), total IgE levels and eosinophils in the blood in several groups of both allergic and non-allergic patients with nasal polyps and in patients with allergic rhinitis (AR). &lt;i&gt;Methods:&lt;/i&gt; Thirty-two patients with nasal polyps en…

MaleAllergyPathologyImmunoglobulin ESeverity of Illness IndexLeukocyte CountImmunology and AllergyMedicineMast CellsSinusitisEosinophil cationic proteinMitesbiologySerine EndopeptidasesGeneral MedicineBlood Proteinsrespiratory systemEosinophil Granule ProteinsMiddle AgedMast cellBody Fluidsmedicine.anatomical_structurePollenFemaleNasal Lavage FluidInflammation MediatorsNasal CavityHistamineAdultmedicine.medical_specialtyRhinitis Allergic PerennialAdolescentImmunologyTryptaseNasal PolypsRibonucleasesEosinophiliaotorhinolaryngologic diseasesAnimalsHumansTherapeutic IrrigationSkin Testsbusiness.industryRhinitis Allergic SeasonalEosinophilImmunoglobulin Emedicine.diseaseEosinophilsImmunologybiology.proteinTryptasesbusiness
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Extract of Caragana sinica as a potential therapeutic option for increasing alpha-secretase gene expression

2015

Abstract Background Alzheimer's disease represents one of the main neurological disorders in the aging population. Treatment options so far are only of symptomatic nature and efforts in developing disease modifying drugs by targeting amyloid beta peptide-generating enzymes remain fruitless in the majority of human studies. During the last years, an alternative approach emerged to target the physiological alpha-secretase ADAM10, which is not only able to prevent formation of toxic amyloid beta peptides but also provides a neuroprotective fragment of the amyloid precursor protein – sAPPalpha. Purpose To identify novel alpha-secretase enhancers from a library of 313 extracts of medicinal plant…

MaleAmyloid betaADAM10Pharmaceutical ScienceBiologyPharmacologyBlood–brain barrierGene Expression Regulation EnzymologicADAM10 ProteinAmyloid beta-Protein PrecursorMicealpha-Viniferinchemistry.chemical_compoundCell Line TumorDrug DiscoverymedicineAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansPromoter Regions GeneticBenzofuransMice KnockoutPharmacologyReporter genePlants MedicinalPlant ExtractsCaragana sinicaMembrane Proteinsbiology.organism_classificationCaraganaADAM Proteinsmedicine.anatomical_structureComplementary and alternative medicinechemistryAlpha secretaseBlood-Brain Barrierbiology.proteinMolecular MedicineAmyloid Precursor Protein SecretasesPhytomedicine
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Enhanced Activity of Meprin-α, a Pro-Migratory and Pro-Angiogenic Protease, in Colorectal Cancer

2011

Meprin-α is a metalloprotease overexpressed in cancer cells, leading to the accumulation of this protease in a subset of colorectal tumors. The impact of increased meprin-α levels on tumor progression is not known. We investigated the effect of this protease on cell migration and angiogenesis in vitro and studied the expression of meprin-α mRNA, protein and proteolytic activity in primary tumors at progressive stages and in liver metastases of patients with colorectal cancer, as well as inhibitory activity towards meprin-α in sera of cancer patient as compared to healthy controls. We found that the hepatocyte growth factor (HGF)- induced migratory response of meprin-transfected epithelial c…

MaleAngiogenesisColorectal cancerCancer TreatmentGene Expressionlcsh:MedicineBiochemistry0302 clinical medicineCell MovementMolecular Cell BiologyGastrointestinal CancersMorphogenesisPathologylcsh:ScienceAged 80 and over0303 health sciencesMetalloproteinaseMultidisciplinaryHepatocyte Growth FactorLiver NeoplasmsMetalloendopeptidasesMiddle AgedImmunohistochemistryRecombinant ProteinsEnzymes3. Good healthOncology030220 oncology & carcinogenesisMedicineFemaleHepatocyte growth factorAntiangiogenesis TherapyColorectal NeoplasmsResearch Articlemedicine.drugAdultmedicine.medical_specialtyImmunoblottingHistopathologyNeovascularization PhysiologicCell MigrationGastroenterology and HepatologyIn Vitro TechniquesBiologyMannose-Binding LectinCell LineRectal CancerYoung Adult03 medical and health sciencesDogsDiagnostic MedicineInternal medicineGastrointestinal TumorsmedicineAnimalsHumansImmunoprecipitationBiologyAged030304 developmental biologylcsh:RCancers and NeoplasmsCancerPlasminogenBlotting Northernmedicine.diseaseRatsEndocrinologyAnatomical PathologyTumor progressionZymogen activationCancer cellCancer researchlcsh:QDevelopmental BiologyPLoS ONE
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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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Fluorovinylsulfones and -Sulfonates as Potent Covalent Reversible Inhibitors of the Trypanosomal Cysteine Protease Rhodesain: Structure–Activity Rela…

2021

Rhodesain is a major cysteine protease of Trypanosoma brucei rhodesiense, a pathogen causing Human African Trypanosomiasis, and a validated drug target. Recently, we reported the development of α-halovinylsulfones as a new class of covalent reversible cysteine protease inhibitors. Here, α-fluorovinylsulfones/-sulfonates were optimized for rhodesain based on molecular modeling approaches. 2d, the most potent and selective inhibitor in the series, shows a single-digit nanomolar affinity and high selectivity toward mammalian cathepsins B and L. Enzymatic dilution assays and MS experiments indicate that 2d is a slow-tight binder (Ki = 3 nM). Furthermore, the nonfluorinated 2d-(H) shows favorabl…

MaleBiodistributionVinyl CompoundsMolecular modelTrypanosoma brucei bruceiCysteine Proteinase InhibitorsMiceStructure-Activity RelationshipParasitic Sensitivity TestsIn vivoDrug DiscoveryAnimalsHumansStructure–activity relationshipSulfonesEnzyme Assayschemistry.chemical_classificationMolecular StructureChemistryTrypanosoma brucei rhodesienseTrypanocidal AgentsCysteine proteaseMolecular Docking SimulationCysteine EndopeptidasesKineticsEnzymeBiochemistryCovalent bondMolecular MedicineFemaleSulfonic AcidsHeLa CellsProtein BindingJournal of Medicinal Chemistry
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High frequency of functionally active Melan-a-specific T cells in a patient with progressive immunoproteasome-deficient melanoma.

2004

AbstractTumor-reactive T cells play an important role in cancer immunosurveillance. Applying the multimer technology, we report here an unexpected high frequency of Melan-A–specific CTLs in a melanoma patient with progressive lymph node metastases, consisting of 18 and 12.8% of total peripheral blood and tumor-infiltrating CD8+ T cells, respectively. Melan-A–specific CTLs revealed a high cytolytic activity against allogeneic Melan-A–expressing target cells but failed to kill the autologous tumor cells. Loading of the tumor cells with Melan-A peptide reversed the resistance to killing, suggesting impaired function of the MHC class I antigen processing and presentation pathway. Mutations of t…

MaleCancer ResearchProteasome Endopeptidase ComplexEpitopeImmune systemMART-1 AntigenTapasinAntigens NeoplasmMultienzyme ComplexesMHC class IHLA-A2 AntigenmedicineHumansMelanomabiologyMHC class I antigenMelanomaMiddle Agedmedicine.diseaseNeoplasm ProteinsImmunosurveillanceCysteine EndopeptidasesOncologyImmunologyMutationCancer researchbiology.proteinLymph NodesCD8T-Lymphocytes CytotoxicCancer research
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