Search results for "Cathepsins"

showing 10 items of 66 documents

Autophagy, cathepsin L transport, and acidification in cultured rat fibroblasts.

1992

The mechanisms of enzyme delivery to and acidification of early autophagic vacuoles in cultured fibroblasts were elucidated by cryoimmunoelectron microscopic methods. The cation-independent mannose-6-phosphate receptor (MPR) was used as a marker of the pre-lysosomal compartment, and cathepsin L and an acidotropic amine (3-(2,4-dinitroanilino)-3'-amino-N-methyl-dipropylamine (DAMP), a cytochemical probe for low-pH organelles) as markers of both pre-lysosomal and lysosomal compartments. In addition, cationized ferritin was used as an endocytic marker. In ultrastructural double labeling experiments, the bulk of all the antigens was found in vesicles containing tightly packed membrane material…

HistologyCathepsin LEndocytic cycleFluorescent Antibody TechniqueReceptors Cell SurfaceVacuoleReceptor IGF Type 2Cathepsin LEndopeptidasesOrganelleAutophagyAnimalsMicroscopy ImmunoelectronCells CulturedCathepsinMannosephosphatesbiologyVesicleBiological TransportFibroblastsHydrogen-Ion ConcentrationCathepsinsRatsCell biologyFerritinCysteine EndopeptidasesDinitrobenzenesBiochemistryCytoplasmbiology.proteinAnatomyJournal of Histochemistry & Cytochemistry
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Histochemical and electron microscopic analysis of spiculogenesis in the demosponge Suberites domuncula.

2006

The skeleton of demosponges is built of spicules consisting of biosilica. Using the primmorph system from Suberites domuncula, we demonstrate that silicatein, the biosilica-synthesizing enzyme, and silicase, the catabolic enzyme, are colocalized at the surface of growing spicules as well as in the axial filament located in the axial canal. It is assumed that these two enzymes are responsible for the deposition of biosilica. In search of additional potential structural molecules that might guide the mineralization process during spiculogenesis to species-specific spicules, electron microscopic studies with antibodies against galectin and silicatein were performed. These studies showed that …

HistologybiologyHistocytochemistryGalectinsMolecular Sequence DataFlagellumbiology.organism_classificationSilicon DioxideMineralization (biology)CathepsinsMicrobiologySilica depositionSuberites domunculaMicroscopy ElectronDemospongeSponge spiculeBiophysicsAnimalsAmino Acid SequenceCollagenAnatomySuberitesElectron microscopicGalectinThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
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Bacterial sensors based on biosilica immobilization for label-free OWLS detection

2013

In the last years, a new group of enzymes, the so-called silicateins, have been identified and characterized, which form the axial filaments of the spicules of the siliceous sponges, consisting of not only amorphous silica among others. These enzymes are able to catalyze the polycondensation and deposition of silica at mild conditions. Silicateins can be expressed in Escherichia coli. The recombinant proteins are expressed on the surface of the cell wall and are able to catalyze the formation of a polysilicate net around the bacterial cells providing the possibility for further attachment to the surface of SiO2 containing sensor chips. With this mild immobilization process it is now possibl…

InsecticidesBioengineeringBiosensing Techniquesmedicine.disease_causeBacterial cell structurelaw.inventionCell wallCarbofuranchemistry.chemical_compoundlawEscherichia colimedicineHydrogen peroxideMolecular BiologyEscherichia colichemistry.chemical_classificationbiologyChloramphenicolPenicillin GHydrogen PeroxideGeneral MedicineOxidantsSilicon Dioxidebiology.organism_classificationCathepsinsAnti-Bacterial AgentsOxidative StressChloramphenicolEnzymechemistryBiochemistryRecombinant DNABacteriaBiotechnologymedicine.drugNew Biotechnology
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Collagenolytic proteinases in keratoconus.

2006

To study the proteolytic phenomena contributing to the pathogenesis of keratoconus, corneal enzymes with potential to cleave fibrillar collagen were studied.Immunohistochemical labeling was undertaken of conventional and novel mammalian collagenases (MMP-1, -2, -8, -13, and -14) of the matrix metalloproteinase (MMP) family and other collagenolytic proteinases of the serine (human trypsin-2) and cysteine (cathepsin K) endoproteinase families. The results were analyzed using a semiquantitative scoring system.Labeling of MMP-8 was moderate in healthy controls, but weak in keratoconus. Moderate MMP-2 and weak MMP-14 expressions were similar in controls and keratoconus. MMP-1 was slightly overex…

KeratoconusPathologymedicine.medical_specialtygenetic structuresCathepsin KMatrix metalloproteinaseKeratoconusPathogenesisCorneaImmunoenzyme TechniquesCorneamedicineCathepsin KHumansTrypsinCollagenaseschemistry.chemical_classificationmedicine.diseaseCathepsinseye diseasesMatrix MetalloproteinasesOphthalmologyEnzymemedicine.anatomical_structurechemistryCollagenaseTrypsinogenImmunohistochemistrysense organsKeratoplasty Penetratingmedicine.drugCornea
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mTORC1 activation in B cells confers impairment of marginal zone microarchitecture by exaggerating cathepsin activity

2018

Mammalian target of rapamycin complex 1 (mTORC1) is a key regulator of cell metabolism and lymphocyte proliferation. It is inhibited by the tuberous sclerosis complex (TSC), a heterodimer of TSC1 and TSC2. Deletion of either gene results in robust activation of mTORC1. Mature B cells reside in the spleen at two major anatomical locations, the marginal zone (MZ) and follicles. The MZ constitutes the first line of humoral response against blood‐borne pathogens and undergoes atrophy in chronic inflammation. In previous work, we showed that mice deleted for TSC1 in their B cells (TSC1(BKO)) have almost no MZ B cells, whereas follicular B cells are minimally affected. To explore potential underl…

Lymphotoxin-beta0301 basic medicinecongenital hereditary and neonatal diseases and abnormalitiesImmunologyMice TransgenicSpleenCHO CellsmTORC1Lymphocyte proliferationMechanistic Target of Rapamycin Complex 1Tuberous Sclerosis Complex 1 ProteinCathepsin BCell LineMice03 medical and health sciencesCricetulus0302 clinical medicineLymphotoxin beta ReceptorTuberous Sclerosis Complex 2 ProteinmedicineAnimalsImmunology and AllergyReceptorLymphotoxin-alphaSirolimusCathepsinB-LymphocytesChemistryOriginal ArticlesMarginal zoneCathepsinsCell biology030104 developmental biologymedicine.anatomical_structureLymphotoxinSpleen030215 immunologyImmunology
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Fine-tuning nucleophosmin in macrophage differentiation and activation

2011

Abstract M-CSF–driven differentiation of peripheral blood monocytes is one of the sources of tissue macrophages. In humans and mice, the differentiation process involves the activation of caspases that cleave a limited number of proteins. One of these proteins is nucleophosmin (NPM1), a multifunctional and ubiquitous protein. Here, we show that caspases activated in monocytes exposed to M-CSF cleave NPM1 at D213 to generate a 30-kDa N-terminal fragment. The protein is further cleaved into a 20-kDa fragment, which involves cathepsin B. NPM1 fragments contribute to the limited motility, migration, and phagocytosis capabilities of resting macrophages. Their activation with lipopolysaccharides …

Macrophage colony-stimulating factorLipopolysaccharidesCellular differentiationImmunologyBiochemistryProinflammatory cytokine03 medical and health sciencesPhagocytes Granulocytes and MyelopoiesisMice0302 clinical medicineAnimalsHumansNuclear proteinCaspaseCells Cultured030304 developmental biologyMice Knockout0303 health sciencesNucleophosminbiologyMacrophage Colony-Stimulating FactorMacrophagesNuclear ProteinsCell DifferentiationCell BiologyHematologyMacrophage ActivationNFKB1Molecular biologyCathepsinsCell biologyProtein Structure TertiaryCXCL1Mice Inbred C57BL030220 oncology & carcinogenesisCaspasesbiology.proteinNucleophosminProtein Processing Post-TranslationalBlood
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Osteoclast-like Giant Cell Tumor of the Pancreas With Ductal Adenocarcinoma: Case Report with Novel Data on Histogenesis

2002

MalePathologymedicine.medical_specialtyPancreatic diseaseEndocrinology Diabetes and MetabolismCathepsin KOsteoclastsBiologyHistogenesisCathepsin BEndocrinologyImmunophenotypingOsteoclastInternal MedicinemedicineHumansPancreatic ductHepatologyGiant Cell TumorsOsteoclast-Like Giant CellMiddle Agedmedicine.diseaseCathepsinsImmunohistochemistryPancreatic Neoplasmsmedicine.anatomical_structureAdenocarcinomaPancreasCarcinoma Pancreatic DuctalPancreas
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Lysosomal changes related to ageing and physical exercise in mouse cardiac and skeletal muscles.

1982

Physical exercise increased the activities of arylsulphatase, cathepsin D and β-glucuronidase in mouse skeletal muscle but not in cardiac muscle. Exercise-induced lysosomal response was more prominent in young adult than in senescent mice. The lipofuscin content of cardiac and skeletal muscles increased markedly during ageing and was also found to increase slightly after exertion in young mice, but not in senescent ones.

Malemedicine.medical_specialtyAgingPhysical ExertionCathepsin DPhysical exerciseCathepsin DLipofuscinLipofuscinCellular and Molecular NeuroscienceMiceInternal medicinemedicineAnimalsExertionYoung adultMolecular BiologyArylsulfatasesGlucuronidasePharmacologybusiness.industryMusclesMyocardiumCardiac muscleSkeletal muscleCell BiologyAnatomyCathepsinsmedicine.anatomical_structureEndocrinologyAgeingMolecular MedicinebusinessLysosomesExperientia
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Acid proteolytic capacity in mouse cardiac and skeletal muscles after prolonged submaximal exercise

1980

Acid proteolytic capacity in mouse cardiac muscle and in predominantly white (distal head of m. vastus lateralis) or predominantly red (proximal red heads of m. vastus lateralis, m. v. medialis, and m. v. intermedius) skeletal muscle was estimated 5 days after 3 h, 6 h or 9 h prolonged running at a speed of 13.5 m/min. The activities of acid protease and beta-glucuronidase together with the rate of acid autolysis considerably increased in both skeletal muscle types, especially in red muscle, but did not increase in cardiac muscle. Acid proteolytic capacity and beta-glucuronidase activity increased in relation to the duration of running. Protein content and oxidative capacity (the activities…

Malemedicine.medical_specialtyAutolysis (biology)Time FactorsPhysiologyPhysical ExertionClinical BiochemistryIschemiaProtein metabolismMuscle ProteinsCitrate (si)-SynthaseCathepsin DMalate dehydrogenaseMicechemistry.chemical_compoundMalate DehydrogenasePhysiology (medical)Internal medicinemedicineAnimalsCitrate synthaseExertionGlucuronidasebiologyMusclesMyocardiumCardiac muscleSkeletal muscleAnatomymedicine.diseaseCathepsinsEndocrinologymedicine.anatomical_structurechemistrybiology.proteinPfl�gers Archiv European Journal of Physiology
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Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities

1978

The activity of certain enzymes of energy metabolism (cytochrome c oxidase, citrate synthase, malate dehydrogenase, and lactate dehydrogenase) and of lysosomes (beta-glucuronidase, beta-N-acetylglucosamindase, arylsuphatase, ribonuclease, deoxyribonuclease, acid phosphatase, and cathepsin D) was assayed from m. rectus femoris of mice trained 5 days per week, 1 hr per day for 4 weeks according to 4 different programmes: I. running speed 20 m/min, horizontal track, II. 25 m/min, horizontal track, III. 20 m/min 8 degrees uphill inclination, and IV. 25 m/min 8 degrees uphill inclination. Oxidative capacity increased and anaerobic capacity decreased without distinction between the different tran…

Malemedicine.medical_specialtyPhysiologyAcid PhosphataseCathepsin DCitrate (si)-SynthaseMalate dehydrogenaseElectron Transport Complex IVMicechemistry.chemical_compoundRibonucleasesMalate DehydrogenaseEndurance trainingLactate dehydrogenaseInternal medicineAcetylglucosaminidasemedicineAnimalsCitrate synthaseCytochrome c oxidaseArylsulfatasesGlucuronidaseDeoxyribonucleasesPhysical Education and TrainingL-Lactate DehydrogenasebiologyHistocytochemistryMusclesAcid phosphataseSkeletal muscleCathepsinsEndocrinologymedicine.anatomical_structurechemistryBiochemistrybiology.proteinEnergy MetabolismLysosomesActa Physiologica Scandinavica
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