Search results for "Cathepsin L1"

showing 4 items of 4 documents

Synovial giant cells in rheumatoid arthritis: Expression of cystatin C, but not of cathepsin B

2000

This study was designed to investigate the expression of the matrix degrading proteinase cathepsin B and its endogenous inhibitor cystatin C in rheumatoid arthritis (RA) with special regard to multinucleated synovial giant cells (SGC). We applied an immunohistochemical double-labeling technique. SGC strongly expressed cystatin C and CD68, but were negative for cathepsin B. This staining pattern occurred in osteoclasts as well. Our findings support the idea that in RA matrix destruction by cathepsin B is not mediated by SGC or osteoclasts, but by mononuclear synoviocytes.

inorganic chemicalsPathologymedicine.medical_specialtyArthritisCysteine Proteinase InhibitorsToxicologyGiant CellsCathepsin BCathepsin BPathology and Forensic MedicineArthritis RheumatoidOsteoclastCathepsin L1Synovial FluidmedicineHumansCystatin CCathepsinHyperplasiabiologyCell BiologyGeneral Medicinemedicine.diseaseCystatinsImmunohistochemistryMolecular biologymedicine.anatomical_structureCystatin Ccardiovascular systembiology.proteinCystatinSynovial membraneExperimental and Toxicologic Pathology
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Expression of cysteine proteinases cathepsins B and K and of cysteine proteinase inhibitor cystatin C in giant cell tumor of tendon sheath.

2001

The expression of cysteine proteinases cathepsins B and K and of the endogenous inhibitor of cysteine proteinases, cystatin C, was investigated in tissue specimens of patients with giant cell tumor of tendon sheath (GCTTS). Expression of both enzymes was examined by immunohistochemistry in tissue specimens of 14 patients with GCTTS. Applying double-labeling techniques, the coexpression of cathepsin B and its major endogenous inhibitor cystatin C was additionally studied. Cells expressing the respective proteins were further characterized with the macrophage markers HAM56 and anti-CD68 (clone PG-M1). Cathepsin B could be detected in numerous HAM56-positive mononuclear cells (MC), but only in…

AdultMaleCathepsin KAntigens Differentiation MyelomonocyticCathepsin ECell CountCathepsin FBiologyCysteine Proteinase InhibitorsGiant CellsCathepsin BPathology and Forensic MedicineCathepsin CCathepsin BImmunoenzyme TechniquesTendonsCathepsin OCathepsin HAntigens CDCathepsin L1HumansCystatin CCathepsin SAgedMuscle NeoplasmsGiant Cell TumorsAntibodies MonoclonalMiddle AgedMolecular biologyCathepsinsCystatinsBiochemistryLeukocytes MononuclearFemaleModern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc
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The Extracellular Vesicles of the Helminth Pathogen, Fasciola hepatica : Biogenesis Pathways and Cargo Molecules Involved in Parasite Pathogenesis

2015

Extracellular vesicles (EVs) released by parasites have important roles in establishing and maintaining infection. Analysis of the soluble and vesicular secretions of adult Fasciola hepatica has established a definitive characterisation of the total secretome of this zoonotic parasite. Fasciola secretes at least two sub-populations of EVs that differ according to size, cargo molecules and site of release from the parasite. The larger EVs are released from the specialised cells that line the parasite gastrodermus and contain the zymogen of the 37 kDa cathepsin L peptidase that performs a digestive function. The smaller exosome-like vesicle population originate from multivesicular bodies with…

Biochemistry & Molecular BiologyBIOCHEMICAL-CHARACTERIZATIONHelminth proteinHOST FIBRINOLYTIC SYSTEMPopulationSTATISTICAL-MODELBINDING PROTEINBiochemistryExosomeAnalytical ChemistryproteomicsLIVER FLUKEFasciola hepaticaParasite hostingAnimalsexosomeeducationMolecular BiologyhelminthTRICHOMONAS-VAGINALISSyncytiumeducation.field_of_studyFasciolabiologyResearchGene Expression ProfilingGene Expression Regulation DevelopmentalHelminth ProteinsIN-VITROFasciola hepaticaExtracellular vesiclesbiology.organism_classificationCell biologysecretomeCATHEPSIN L1transcriptomeLEUCINE AMINOPEPTIDASEBiogenesisSCHISTOSOMA-MANSONIMolecular & Cellular Proteomics
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Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.

2003

Objective—Modification with proteases and cholesterylesterase transforms LDL to a moiety that resembles lipoproteins isolated from atherosclerotic lesions and possesses atherogenic properties. To identify changes in monocyte-derived foam cells laden with enzymatically modified LDL (E-LDL), we compared patterns of the most abundant transcripts in these cells after incubation with LDL or E-LDL.Methods and Results—Serial analyses of gene expression (SAGE) libraries were constructed from human monocytes after treatment with LDL or E-LDL. Several tags were differentially expressed in LDL-treated versus E-LDL–treated cells, whereby marked selective induction by E-LDL of cathepsin H was conspicuou…

ProteasesCathepsin HCoronary Artery DiseaseBiologyCathepsin HCathepsin L1medicineMacrophageHumansFoam cellGene LibraryCathepsinMonocyteGene Expression ProfilingColocalizationSterol EsteraseMolecular biologyCathepsinsLipoproteins LDLCysteine Endopeptidasesmedicine.anatomical_structureCholesterolBiochemistryGene Expression Regulationlipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineFoam CellsArteriosclerosis, thrombosis, and vascular biology
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