Search results for "Endopeptidase"

showing 10 items of 361 documents

Tryptophan-Containing Dual Neuroprotective Peptides: Prolyl Endopeptidase Inhibition and Caenorhabditis elegans Protection from β-Amyloid Peptide Tox…

2018

Neuroprotective peptides represent an attractive pharmacological strategy for the prevention or treatment of age-related diseases, for which there are currently few effective therapies. Lactoferrin (LF)-derived peptides (PKHs) and a set of six rationally-designed tryptophan (W)-containing heptapeptides (PACEIs) were characterized as prolyl endopeptidase (PEP) inhibitors, and their effect on β-amyloid peptide (Aβ) toxicity in a Caenorhabditis elegans model of Alzheimer’s disease (AD) was evaluated. Two LF-derived sequences, PKH8 and PKH11, sharing a W at the C-terminal end, and the six PACEI heptapeptides (PACEI48L to PACEI53L) exhibited significant in vitro PEP inhibition. The inhibitory pe…

0301 basic medicineprolyl endopeptidase inhibitionPeptidelactoferrin-derived peptidesPharmacologyNeuroprotectionCatalysislcsh:ChemistryInorganic Chemistry03 medical and health sciencesneurodegenerative diseases; amyloid β peptide; <i>Caenorhabditis elegans</i>; prolyl endopeptidase inhibition; lactoferrin-derived peptides; rationally-designed peptides; tryptophan; molecular docking0302 clinical medicineProlyl endopeptidaseIn vivomedicineneurodegenerative diseasestryptophanPhysical and Theoretical ChemistryCaenorhabditis eleganslcsh:QH301-705.5Molecular BiologySpectroscopyCaenorhabditis elegansamyloid β peptidechemistry.chemical_classificationbiologyOrganic ChemistryTryptophanmolecular dockingGeneral Medicinebiology.organism_classificationIn vitroComputer Science Applications030104 developmental biologylcsh:Biology (General)lcsh:QD1-999chemistryrationally-designed peptidesToxicity030217 neurology & neurosurgerymedicine.drugInternational Journal of Molecular Sciences; Volume 19; Issue 5; Pages: 1491
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Antiprotozoal and cysteine proteases inhibitory activity of dipeptidyl enoates

2018

A family of dipeptidyl enoates has been prepared and tested against the parasitic cysteine proteases rhodesain, cruzain and falcipain-2 related to sleeping sickness, Chagas disease and malaria, respectively. They have also been tested against human cathepsins B and L1 for selectivity. Dipeptidyl enoates resulted to be irreversible inhibitors of these enzymes. Some of the members of the family are very potent inhibitors of parasitic cysteine proteases displaying k2nd (M−1s−1) values of seven orders of magnitude. In vivo antiprotozoal testing was also performed. Inhibitors exhibited IC50 values in the micromolar range against Plasmodium falciparum, Trypanosoma brucei, Trypanosoma cruzi and ev…

0301 basic medicinesleeping sicknessClinical BiochemistryPharmaceutical Science01 natural sciencesBiochemistryCathepsin BinhibitorsDrug Discoverychemistry.chemical_classificationbiologyChemistryDipeptidesHep G2 CellsMolecular Docking SimulationCysteine EndopeptidasesBiochemistryAntiprotozoalMolecular MedicineChagas diseaseProteasesCell Survivalmedicine.drug_classPlasmodium falciparumTrypanosoma brucei bruceimalariaAntiprotozoal AgentsCysteine Proteinase InhibitorsTrypanosoma bruceicysteine proteasesInhibitory Concentration 50Structure-Activity Relationship03 medical and health sciencesparasitic diseasesmedicineHumansTrypanosoma cruziMolecular Biologychagas diseaseBinding Sites010405 organic chemistryOrganic ChemistryPlasmodium falciparumbiology.organism_classificationmedicine.diseaseProtein Structure Tertiary0104 chemical sciences030104 developmental biologyEnzymeCysteineBioorganic &amp; Medicinal Chemistry
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Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

1999

Amyloid β peptide (Aβ), the principal proteinaceous component of amyloid plaques in brains of Alzheimer’s disease patients, is derived by proteolytic cleavage of the amyloid precursor protein (APP). Proteolytic cleavage of APP by a putative α-secretase within the Aβ sequence precludes the formation of the amyloidogenic peptides and leads to the release of soluble APPsα into the medium. By overexpression ofa disintegrinandmetalloprotease (ADAM), classified as ADAM 10, in HEK 293 cells, basal and protein kinase C-stimulated α-secretase activity was increased severalfold. The proteolytically activated form of ADAM 10 was localized by cell surface biotinylation in the plasma membrane, but the m…

ADAM10Molecular Sequence DataBiologyKidneyTransfectionCell LineSubstrate SpecificityADAM10 ProteinAmyloid beta-Protein PrecursorEndopeptidasesAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansPoint MutationADAM17 ProteinAmino Acid SequenceCloning MolecularProtein kinase AProtein Kinase CSecretory pathwayBinding SitesMultidisciplinaryHEK 293 cellsP3 peptideMembrane ProteinsMetalloendopeptidasesBiological SciencesPeptide FragmentsRecombinant Proteinscarbohydrates (lipids)ADAM ProteinsKineticsZincAlpha secretaseBiochemistryMutagenesis Site-Directedbiology.proteinCattleAmyloid Precursor Protein SecretasesProceedings of the National Academy of Sciences
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Down-regulation of Endogenous Amyloid Precursor Protein Processing due to Cellular Aging

2005

Processing of amyloid precursor protein (APP) is a well acknowledged central pathogenic mechanism in Alzheimer disease. However, influences of age-associated cellular alterations on the biochemistry of APP processing have not been studied in molecular detail so far. Here, we report that processing of endogenous APP is down-regulated during the aging of normal human fibroblasts (IMR-90). The generation of intracellular APP cleavage products C99, C83, and AICD gradually declines with increasing life span and is accompanied by a reduced secretion of soluble APP (sAPP) and sAPPalpha. Further, the maturation of APP was reduced in senescent cells, which has been shown to be directly mediated by a…

ADAM10NicastrinEndogenyBiochemistryCell LineAmyloid beta-Protein PrecursorMembrane MicrodomainsDownregulation and upregulationEndopeptidasesmental disordersPresenilin-1Amyloid precursor proteinAspartic Acid EndopeptidasesHumansSecretionMolecular BiologyCellular SenescenceMembrane GlycoproteinsbiologyChemistryMembrane ProteinsCell BiologyFibroblastsCholesterolBiochemistrybiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAmyloid precursor protein secretaseIntracellularJournal of Biological Chemistry
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Flow cytometric DNA analysis and lysosomal cathepsins B and L in locally advanced laryngeal cancer. Relationship with clinicopathologic parameters an…

1995

Background. The traditional factors of locally advanced laryngeal squamous cell carcinoma (LSCC) have limited predictive value for the identification of high risk patients. Therefore, it is extremely important to define prognostic factors that identify the more aggressive types. Reliable and reproducible prognostic indicators are being investigated to help clinicians identify high risk groups and address more rational treatment. Methods. Flow cytometric DNA ploidy and S‐phase fraction (SPF) measurements were performed on frozen tumor tissues from a consecutive series of 71 patients with Stage III and IV LSCC. Lysosomal cathepsin B and L activity levels were determined biochemically in match…

AdultAged 80 and overMaleCathepsin LDNA NeoplasmMiddle AgedAneuploidyFlow CytometryPrognosisCathepsinsCathepsin BS PhaseCysteine EndopeptidasesEndopeptidasesHumansFemalecathepsin B and L DNA ploidy flow cytometry laryngeal squamous cell carcinoma S‐phase fractionLysosomesLaryngeal NeoplasmsAgedCancer
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Cathepsin D, B and L circulating levels as prognostic markers of malignant progression

1996

Growing evidence indicates that lysosomal Cathepsins D (CD), B (CB) and L (CL) may promote carcinogenesis and tumor progression. Therefore, we evaluated their potential value as biochemical parameters of malignant progression in patients with benign diseases which may undergo malignant transformation, such as liver cirrhosis (LC) and chronic pancreatitis (CHP) as well as in hepatocellular carcinoma (HCC) and pancreatic cancer (DPC). CD, CB and CL serum levels were determined by immunoenzymatic assays in LC, CHP, HCC or DPC patients and correlated with a number of biochemical and clinical parameters of these diseases. CD serum levels were increased in LC, CHP and HCC, but not in the DPC grou…

AdultAged 80 and overMaleTumor progression.Carcinoma HepatocellularCirrhosiVHepatocellular carcinomaCathepsin LLiver NeoplasmsPancreatic cancerMiddle AgedPrognosisCathepsin DCathepsinsLCathepsin BPancreatic NeoplasmsCysteine EndopeptidasesChronic HepatiticEndopeptidasesBiomarkers TumorHumansFemaleAged
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MMP-7 promoter polymorphisms do not influence CD4+ recovery and changes in plasma viral load during antiretroviral therapy for HIV-1 infection.

2005

Summary Matrix metalloproteinase-7 (MMP-7) generates soluble Fas Ligand (FasL), which is involved in the apoptotic loss of CD4+ T cells during HIV infection. We evaluated whether two polymorphisms in MMP-7 promoter could influence CD4+ recover in response to antiretroviral therapy, and found that these polymorphisms are ineffective.

AdultCD4-Positive T-LymphocytesMaleImmunologyHuman immunodeficiency virus (HIV)HIV InfectionsMatrix metalloproteinasemedicine.disease_causeMMP-7; Fas ligand; CD4T cells; HIV infectionFas ligandPlasma viral loadGeneticsHumansMedicineMolecular BiologyGenetics (clinical)Polymorphism Geneticbusiness.industryMetalloendopeptidasesGeneral MedicineMiddle AgedViral LoadAntiretroviral therapySoluble fas ligandCD4 Lymphocyte CountAnti-Retroviral AgentsApoptosisMatrix Metalloproteinase 7ImmunologyHIV-1business
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Lysosomal cathepsins B and L and Stefin A blood levels in patients with hepatocellular carcinoma and/or liver cirrhosis: potential clinical implicati…

1997

The serum levels of lysosomal cathepsin B and L and Stefin A, an intracellular inhibitor of these proteolytic enzymes, were determined in patients with hepatocellular carcinoma (HCC) and/or liver cirrhosis (LC) and correlated with some clinical and biochemical parameters of these diseases. Cathepsin B serum levels were increased in HCC and in LC patients as compared to normal subjects (p &lt; 0.001). However no difference was observed between HCC and LC groups. Interestingly, a significant relationship was evidenced between cathepsin B serum content and the grade of severity of cirrhosis (r = 0.41; p &lt; 0.001). Cathepsin L was significantly elevated only in sera of cancer patients as comp…

AdultLiver CirrhosisMaleCancer Researchmedicine.medical_specialtyPathologyCirrhosisCarcinoma HepatocellularHepatocellular carcinomaoteinase inhibitorCathepsin LLysosomal proteinaseGastroenterologyCathepsin BLiver cirrhosiCathepsin BCathepsin LInternal medicineEndopeptidasesmedicineCarcinomaHumansCystatin AStefin AAgedTumor progression.Aged 80 and overEnzyme PrecursorsbiologyLiver NeoplasmsProteolytic enzymesCancerGeneral MedicineMiddle Agedmedicine.diseaseCathepsinsCystatinsPrCysteine EndopeptidasesOncologyCystatin AHepatocellular carcinomabiology.proteinFemalealpha-FetoproteinsLysosomesOncology
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THE LEVEL OF SOLUBLE GRANZYME A IS ELEVATED IN THE PLASMA AND IN THE Vgamma9/Vdelta2 T CELL CULTURE SUPERNATANTS OF PATIENTS WITH ACTIVE BEHCET'S DIS…

2004

Gramzyme A (GrA) is a serine proteinase with trypsin-like activity that is released extracellularly during the degranulation of cytotoxic cells. Among the cytotoxic cells, gamma/delta T cells participate in the early phases of the immune response and are known to express perforin and granzymes constitutively in agreement with their cytolytic pontential.GrA activity was detected using the synthetic substrate N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester in the plasma and supernatants of peripheral blood mononuclear cell cultured in the presence of Dimethylallyl pyrophosphate to obtain Vgamma9/Vdelta2 T cell expansion.Significantly high levels of GrA were found in the serum and supernat…

AdultMaleAdolescentDose-Response Relationship DrugBehcet SyndromeT-LymphocytesSerine EndopeptidasesReceptors Antigen T-Cell gamma-deltaMiddle AgedFlow CytometryGranzymesCulture Media ConditionedHumansFemaleCells CulturedAged
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The effect of short-term immunotherapy with molecular standardized grass and rye allergens on eosinophil cationic protein and tryptase in nasal secre…

1999

Activation of mast cells and eosinophils under pollen exposure can be inhibited by specific immunotherapy.The effect of short-term immunotherapy with 7 preseasonal injections of molecular standardized allergens from grass and rye pollen on eosinophil cationic protein (ECP) and tryptase levels in nasal secretions has been compared with symptomatic drug treatment in an open, randomized study with 48 patients.Nasal reactivity and mediator levels in nasal secretions were measured at baseline, before season, in season, and after season.Symptom scores in the immunotherapy group were 134.5 (95% CI, 65 to 336) versus 386. 0 (95% CI, 185 to 563), significantly lower as in the drug-treated group. ECP…

AdultMaleAllergyRhinitis Allergic PerennialTime FactorsAdolescentmedicine.medical_treatmentImmunologyTryptasemedicine.disease_causeNasal provocation testAllergenChymasesRibonucleasesmedicineImmunology and AllergyHumansEosinophil cationic proteinbiologybusiness.industrySerine EndopeptidasesAeroallergenImmunotherapyBlood ProteinsAllergensEosinophil Granule ProteinsMiddle AgedMast cellmedicine.diseaseNasal Mucosamedicine.anatomical_structureImmunologybiology.proteinFemaleTryptasesImmunotherapyInflammation MediatorsbusinessThe Journal of allergy and clinical immunology
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