Search results for "Carboxypeptidases"

showing 6 items of 6 documents

Demonstration of High-Affinity Binding Sites for C3a Anaphylatoxin on Guinea-Pig Platelets

1978

3H-serotonin release from guinea-pig platelets was demonstrated to be the consequence of C3a binding to these cells. A Scatchard analysis of dose-response data of the 125I-C3a binding pattern to guinea-pig platelets pointed to the existence of binding sites with high and low affinity for the C3a molecule (HA and LA receptors). HA receptors are specific for C3a with intact C-terminal arginine. whereas C3adesarg only interacts with LA receptors. The release of serotonin may be induced by a combined reaction of C3a with HA receptors and LA receptors on the platelet membrane.

Blood PlateletsAnaphylatoxinsSerotoninBinding SitesArginineChemistryGuinea PigsImmunologyTemperaturechemical and pharmacologic phenomenaCarboxypeptidasesComplement C3General MedicineGuinea pigBiochemistryAnimalsProtease-activated receptorPlateletAnaphylatoxinSerotoninBinding sitePeptidesReceptorScandinavian Journal of Immunology
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Cre-mediated cell ablation contests mast cell contribution in models of antibody- and T cell-mediated autoimmunity.

2011

SummaryImmunological functions of mast cells remain poorly understood. Studies in Kit mutant mice suggest key roles for mast cells in certain antibody- and T cell-mediated autoimmune diseases. However, Kit mutations affect multiple cell types of both immune and nonimmune origin. Here, we show that targeted insertion of Cre-recombinase into the mast cell carboxypeptidase A3 locus deleted mast cells in connective and mucosal tissues by a genotoxic Trp53-dependent mechanism. Cre-mediated mast cell eradication (Cre-Master) mice had, with the exception of a lack of mast cells and reduced basophils, a normal immune system. Cre-Master mice were refractory to IgE-mediated anaphylaxis, and this defe…

Cell typeEncephalomyelitis Autoimmune ExperimentalCarboxypeptidases AT cellT-LymphocytesImmunologyAutoimmunityImmunoglobulin E03 medical and health sciencesMice0302 clinical medicineImmune systemTh2 CellsmedicineImmunology and AllergyAnimalsGenetic Predisposition to DiseaseMast CellsIntestinal MucosaInterleukin 5Anaphylaxis030304 developmental biologyAutoantibodiesMice Knockout0303 health sciencesStem Cell FactorbiologyIntegrasesGene Expression ProfilingImmunoglobulin EMast cellArthritis Experimental3. Good healthInterleukin 33Mice Inbred C57BLDisease Models Animalmedicine.anatomical_structureInfectious DiseasesImmunologyGene Targetingbiology.proteinAntibodyTumor Suppressor Protein p53030215 immunologyImmunity
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d-Alanyl-d-Alanine Carboxypeptidase in the Bacterial Form and L-Form of Proteus mirabilis

1975

Membranes of the bacterial form and the stable and unstable L-forms of Proteus mirabilis contain LD and DD-carboxypeptidase. The DD-carboxypeptidase is inhibited non-competitively by penicillin G. The enzyme of the bacterial form is highly penicillin-sensitive (Ki - 4 X 10(-9) M penicillin G). Inhibition is only partly reversible by treatment with penicillinase or by dialysis against buffer. In contrast, the DD-carboxypeptidase of the unstable L-form, grown in the presence of penicillin, is 175-fold less penicillin-sensitive (Ki = 7 X 10(7) M penicillin G). Inhibition is completely reversed by penicillinase or dialysis. After inhibition by penicillin and subsequent reactivation the penicill…

D-Amino-Acid OxidaseDetergentsPenicillin sensitivityL FormsCarboxypeptidasesSpheroplastsBiochemistryDD PeptidaseCell wallpolycyclic compoundsmedicineProteus mirabilischemistry.chemical_classificationAlaninebiologyProtoplastsCell MembranePenicillin GHydrogen-Ion Concentrationbiology.organism_classificationProteus mirabilisPenicillinKineticsMembraneEnzymechemistryBiochemistryPenicillin VPenicillin bindingmedicine.drugEuropean Journal of Biochemistry
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Two different aggregation principles in reaggregation process of dissociated sponge cells (Geodia cydonium)

1974

Chemisch dissoziierte Zellen des KieselschwammesGeodia cydonium reaggregieren aufgrund zweier verschiedenr Reaggregationsprinzipien. Der Aggnegationsfaktor, auf den die Primaraggregation zuruckgeht, ist membrangebunden und wird durch Proteasen nicht inaktiviert. Der sekundare Aggregationsfaktor wurde 500fach angereichert. Das Molekulargewicht dieses Aggregationsfaktors betragt etwa 20000 Daltons; er ist mit einem ringformigen Makromolekul (2×109 Daltons) assoziiert.

PharmacologybiologySurface PropertiesChemistryGeodia cydoniumCarboxypeptidasesCell Biologybiology.organism_classificationMolecular biologyPoriferaMicroscopy ElectronCellular and Molecular NeuroscienceSpongeCell AdhesionBiophysicsAnimalsMolecular MedicineGeodiaMolecular BiologyCell AggregationExperientia
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Sequence of the M28 dsRNA: Preprotoxin Is Processed to an α/β Heterodimeric Protein Toxin

1995

The killer and immunity phenotypes of K28 killer strains of Saccharomyces cerevisiae are determined by the 1.75-kb M28 dsRNA virus. In the plus strand, M28p, the K28 preprotoxin gene, comprises bases 13-1047 and is followed, after an additional 85 bases, by a 63-bp poly(A) sequence and a 553-base 3'-sequence. This 3'-sequence contains two potential stem-loop structures predicted to bind the L-A encoded cap-pol protein, initiating encapsidation; high-level expression results in curing of M1 dsRNA. Expression of M28p confers the complete K28 killer and immunity phenotype on a cell lacking M28 dsRNA. K28 toxin is a disulfide-bonded heterodimer of alpha (10.5 kDa) and beta (11 kDa) components w…

Signal peptideDNA ComplementaryGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationMolecular Sequence DataMutantCarboxypeptidasesSaccharomyces cerevisiaeBiologymedicine.disease_causeCleavage (embryo)Fungal Proteinschemistry.chemical_compoundGene Expression Regulation FungalVirologyEndopeptidasesmedicineSecretionAmino Acid SequenceSubtilisinsGeneDNA PrimersRNA Double-StrandedBase SequenceToxinSerine EndopeptidasesMembrane ProteinsRNA FungalMycotoxinsMolecular biologyKiller Factors YeastRNA silencingchemistryProprotein ConvertasesProtein Processing Post-TranslationalVirology
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Reduced serum protease activity in Complex Regional Pain Syndrome: The impact of angiotensin-converting enzyme and carboxypeptidases.

2021

Complex Regional Pain Syndrome (CRPS) occurs in about 2% of patients after fracture of the limbs. In an earlier clinical study with 102 probands we have shown that the serum protease network in CRPS might be less effective. Based on these results we hypothesized that angiotensin-converting enzyme (ACE) and carboxypeptidase N (CPN) activity contribute to the differences of labeled bradykinin (DBK) degradation by patients' sera. Details of the enzymatic processes remained however unclear. The contributions of ACE and CPN in the serum degradation of DBK were studied using specific inhibitors. CPN1-ELISA was performed in serum. It was confirmed that the majority of DBK was degraded by ACE and C…

medicine.medical_specialtyAngiotensinsmedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceBradykininCarboxypeptidasesBradykininAnalytical Chemistrychemistry.chemical_compoundInternal medicineDrug DiscoverymedicineHumansSpectroscopyProteasebiologyCaptoprilAngiotensin-converting enzymemedicine.diseaseBlood proteinsCarboxypeptidasePathophysiologyEndocrinologyComplex regional pain syndromechemistrybiology.proteinFemaleComplex Regional Pain Syndromesmedicine.drugPeptide HydrolasesJournal of pharmaceutical and biomedical analysis
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