Search results for "Dipeptidyl-Peptidases and Tripeptidyl-Peptidases"

showing 9 items of 9 documents

Enzymatic Activity of CD26 (Dipeptidylpeptidase IV) is not Required for Its Signalling Function in T Cells

1993

Abstract CD26 is a proteolytic enzyme (dipeptidylpeptidase IV) expressed on the T cell surface that defines an alternative activation signal for human T lymphocytes. Crosslinking of CD26 via monoclonal antibodies triggers proliferation and cytotoxicity in preactivated T cells. In this study, we used highly specific competitive and irreversible inhibitors of dipeptidylpeptidase IV to study the role of the enzymatic activity in activation of CD26- transfected T cells as well as of CD26-expressing normal human T cell clones. These inhibitors at concentrations that blocked up to 95% of the enzymatic activity, did not specifically inhibit T cell activation neither via TCR/CD3 nor via CD26 itself…

Antigens Differentiation T-LymphocyteDipeptidyl Peptidase 4T-LymphocytesT cellCD3ImmunologyBiologyLymphocyte ActivationCell LineMiceTumor Cells CulturedmedicineAnimalsHumansImmunology and AllergyCytotoxic T cellDipeptidyl-Peptidases and Tripeptidyl-PeptidasesT-cell receptorProteolytic enzymesHematologyTransfectionT lymphocyteCytotoxicity Tests ImmunologicCell biologymedicine.anatomical_structureBiochemistrybiology.proteinInterleukin-2Clone (B-cell biology)Signal TransductionImmunobiology
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Function of Dipeptidyl Peptidase IV (CD26, Tp103) in Transfected Human T Cells

1993

CD26 (Tp103) is a proteolytic enzyme (dipeptidyl peptidase IV) expressed on the T cell surface that defines an alternative activation signal for human T lymphocytes. It is absent from or present in only low amounts on resting T cells but it is expressed strongly after activation. Crosslinking of CD26/Tp103 via the monoclonal antibody CB.1 triggers functional activities in preactivated T cells. To study the molecular requirements for T cell activation via CD26 we transfected a cDNA encoding CD26 into several CD26-negative cells. In Jurkat T cell leukemia cells that normally do not express the CD26 antigen, the transfected CD26 molecule is functional because the monoclonal antibody CB.1 induc…

Antigens Differentiation T-LymphocyteDipeptidyl Peptidase 4T-LymphocytesT cellZAP70ImmunologyT-cell receptorReceptors Antigen T-CellBiologyTransfectionNatural killer T cellMolecular biologyJurkat cellsRecombinant ProteinsCell LineMicemedicine.anatomical_structureAntigenTumor Cells CulturedmedicineAnimalsHumansCytotoxic T cellIL-2 receptorDipeptidyl-Peptidases and Tripeptidyl-PeptidasesCellular Immunology
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Decrease of mRNA levels and biosynthesis of sucrase-isomaltase but not dipeptidylpeptidase IV in forskolin or monensin-treated Caco-2 cells.

1991

International audience; Treatment for 48 h of differentiated, confluent Caco-2 cells with 2.5 10(-5) M forskolin or 10(-6) M monensin, which produces a significant decrease of the de novo biosynthesis of sucrase-isomaltase, does not change quantitatively the de novo biosynthesis of dipeptidylpeptidase IV. Western blot analysis and silver nitrate staining indicate that neither drug induces any modification in the steady state expression of these two brush border hydrolases. Northern blot analysis shows that the level of dipeptidylpeptidase IV mRNA does not change in treated as compared to control Caco-2 cells. In contrast, forskolin and monensin dramatically decrease the level of sucrase-iso…

Brush borderDipeptidyl Peptidase 4Blotting WesternAdenocarcinomaBiology03 medical and health sciencesCellular and Molecular Neurosciencechemistry.chemical_compoundWestern blot[ CHIM.ORGA ] Chemical Sciences/Organic chemistryCyclic AMPTumor Cells CulturedmedicineHumansRNA MessengerNorthern blotMonensinDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMolecular Biology030304 developmental biologyPharmacology0303 health sciencesForskolinmedicine.diagnostic_test[CHIM.ORGA]Chemical Sciences/Organic chemistryColforsin030302 biochemistry & molecular biologyMonensinAntibodies MonoclonalCell BiologyMetabolismBlotting Northern[CHIM.ORGA] Chemical Sciences/Organic chemistrySucrase-Isomaltase ComplexGlucosechemistryBiochemistryCell cultureColonic NeoplasmsMolecular MedicineSucrase-isomaltase
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Morphological studies on CLN2

2001

Electron microscopic, fluorescence microscopic, and immunohistochemical studies earlier performed on archivalcerebral tissue from Max Bielchowsky's original three patients revealed curvilinear bodies rich in subunit C of mitochondrial ATP synthase (SCMAS). Recent progress in the elucidation of CLN2, i.e. identification of the defective lysosomal enzyme tripeptidyl-peptidase I (TPP-I) and mutations in the CLN2 gene have further corroborated earlier data. Immunohistochemically the absence of the TPP-I protein could be confirmed in the archival tissues using pathological controls. Unlike biochemistry, immunohistochemistry enables examination of these archival tissues elucidating the causative …

MaleCell typePathologymedicine.medical_specialtyProtein subunitEncephalopathyBiologymedicine.disease_causeAminopeptidasesNeuronal Ceroid-LipofuscinosesChloroquineEndopeptidasesmedicineHumansChildDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMyopathyGeneMutationTripeptidyl-Peptidase 1BrainGeneral MedicineMitochondrial Proton-Translocating ATPasesmedicine.diseaseImmunohistochemistryProton-Translocating ATPasesMutationPediatrics Perinatology and Child HealthImmunohistochemistryFemaleNeurology (clinical)Serine Proteasesmedicine.symptomPeptide Hydrolasesmedicine.drugEuropean Journal of Paediatric Neurology
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Shotgun Proteomics of Isolated Urinary Extracellular Vesicles for Investigating Respiratory Impedance in Healthy Preschoolers

2021

Urine proteomic applications in children suggested their potential in discriminating between healthy subjects from those with respiratory diseases. The aim of the current study was to combine protein fractionation, by urinary extracellular vesicle isolation, and proteomics analysis in order to establish whether different patterns of respiratory impedance in healthy preschoolers can be characterized from a protein fingerprint. Twenty-one 3–5-yr-old healthy children, representative of 66 recruited subjects, were selected: 12 late preterm (LP) and 9 full-term (T) born. Children underwent measurement of respiratory impedance through Forced Oscillation Technique (FOT) and no significant differen…

MaleProteomePharmaceutical SciencePhysiologyUrineUrineProteomicsAminopeptidasesAnalytical Chemistry0302 clinical medicineDrug DiscoveryElectric ImpedanceMedicineRespiratory systemproteomic0303 health sciencesTripeptidyl-Peptidase 1urine fractionationExtracellular vesicleTripeptidyl peptidase IRespiratory Function Testsforced oscillation techniqueChemistry (miscellaneous)Child PreschoolMolecular MedicineFemaleUrinary systemReceptors Cell SurfaceArticlelcsh:QD241-441Extracellular Vesicles03 medical and health sciencesproteomicslcsh:Organic chemistryHumansNerve Growth FactorsPhysical and Theoretical ChemistryDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEye ProteinsShotgun proteomicsAngiopoietin-Like Protein 2Serpins030304 developmental biologypreschooler healthy childrenbusiness.industryOrganic ChemistryCubilinAngiopoietin-like Proteins030228 respiratory systemThy-1 Antigensextracellular vesicleSerine Proteasesbusiness
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Activation of EDTA-resistant Gelatinases in Malignant Human Tumors

2006

Abstract Among the many proteases associated with human cancer, seprase or fibroblast activation protein α, a type II transmembrane glycoprotein, has two types of EDTA-resistant protease activities: dipeptidyl peptidase and a 170-kDa gelatinase activity. To test if activation of gelatinases associated with seprase could be involved in malignant tumors, we used a mammalian expression system to generate a soluble recombinant seprase (r-seprase). In the presence of putative EDTA-sensitive activators, r-seprase was converted into 70- to 50-kDa shortened forms of seprase (s-seprase), which exhibited a 7-fold increase in gelatinase activity, whereas levels of dipeptidyl peptidase activity remaine…

Models MolecularCancer ResearchProteasesProtein ConformationDipeptidyl-peptidase activityIn situ hybridizationBiologyDipeptidyl peptidaseArticleCell LineFibroblast activation protein alphaNeoplasmsEndopeptidasesmedicineGelatinaseAnimalsHumansDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEdetic AcidSerine EndopeptidasesMembrane ProteinsHaplorhinimedicine.diseaseRecombinant Proteinsseprase fibroblast activation protein alpha (FAP-α) gelatinase activation malignant tumorEnzyme ActivationOncologyBiochemistryGelatinasesCancer researchImmunohistochemistryAdenocarcinoma
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Late infantile neuronal ceroid lipofuscinosis: Quantitative description of the clinical course in patients withCLN2 mutations

2002

We examined 26 individuals with clinical and electron microscopic signs of late infantile neuronal ceroid lipofuscinosis (LINCL). In 22 cases, we found both pathogenic alleles. Sixteen patients exclusively carried either one or a combination of the two common mutations R208X and IVS5-1G > C. In the remaining cases, four missense mutations could be detected, of which R127Q, N286S, and T353P represent novel, previously not described alleles. A clinical performance score was developed by rating motor, visual, and verbal functions and the incidence of cerebral seizures in 3-month intervals during the course of the disease. A Total Disability Score was derived by summing up the single scores for…

Pediatricsmedicine.medical_specialtyDNA Mutational AnalysisCerliponase alfaDiseaseNeurological disorderAminopeptidasesSeverity of Illness IndexNeuronal Ceroid-LipofuscinosesSeizuresEndopeptidasesSeverity of illnessmedicineMissense mutationDipeptidyl-Peptidases and Tripeptidyl-PeptidasesVision OcularGenetics (clinical)Tripeptidyl-Peptidase 1business.industryDNAmedicine.diseaseTripeptidyl peptidase INeuronal Ceroid Lipofuscinosis Type 2MutationNeuronal ceroid lipofuscinosisSerine ProteasesbusinessPsychomotor PerformancePeptide HydrolasesAmerican Journal of Medical Genetics
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Type-II transmembrane prolyl dipeptidases and matrix metalloproteinases in membrane vesicles of active endothelial cells.

2006

Conclusions: Endothelia cells in sparse culture are migratory and increase the production of gelatinases of serine- and metallo-classes in membrane vesicles. Collectively, proteases associated with membrane vesicles degrade extracellular matrix components including type-I and type-IV collagens, laminin and fibronectin. Inhibitor studies suggest the existence of small gelatinases that were derived from these serine- and metallo-proteases. Thus, further studies are warranted to demonstrate the cooperative action of metallo- and serine proteases on cell surfaces and in extracellular vesicles during endothelial cell migration in 3D collagenous matrices, and potential proteolytic activation mech…

TUMOR-CELLSCell MembraneBREAST-CARCINOMA CELLSEndothelial CellsUP-REGULATIONANGIOGENESISMatrix MetalloproteinasesExtracellular MatrixACTIVATIONEnzyme ActivationNEUROPEPTIDE-YCell MovementSEPRASESettore BIO/10 - BiochimicaMETASTASISPEPTIDASE-IVHumansDipeptidyl-Peptidases and Tripeptidyl-PeptidasesINTEGRINCells CulturedAdvances in experimental medicine and biology
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Protease-mediated processing of Argonaute proteins controls small RNA association

2020

SummarySmall RNA pathways defend the germlines of animals against selfish genetic elements and help to maintain genomic integrity. At the same time, their activity needs to be well-controlled to prevent silencing of ‘self’ genes. Here, we reveal a proteolytic mechanism that controls endogenous small interfering (22G) RNA activity in the Caenorhabditis elegans germline to protect genome integrity and maintain fertility. We find that WAGO-1 and WAGO-3 Argonaute (Ago) proteins are matured through proteolytic processing of their unusually proline-rich N-termini. In the absence of DPF-3, a P-granule-localized N-terminal dipeptidase orthologous to mammalian DPP8/9, processing fails, causing a cha…

Transposable elementSmall RNAanimal structuresDNA damageBiologyDipeptidyl peptidaseSubstrate Specificity03 medical and health sciences0302 clinical medicineAnimalsGene silencingRNA MessengerRNA Small InterferingCaenorhabditis elegansCaenorhabditis elegans ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMolecular BiologyGeneCaenorhabditis elegans030304 developmental biology0303 health sciencesWild typeRNACell BiologyArgonautebiology.organism_classificationCell biologyFertilityArgonaute ProteinsProteolysisRNA HelminthProtein Processing Post-Translational030217 neurology & neurosurgery
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