Search results for "cathepsin L"

showing 10 items of 42 documents

Effects of E-64 (cysteine-proteinase inhibitor) and pepstatin (aspartyl-proteinase inhibitor) on metastasis formation in mice with mammary and ovaria…

1994

The effects of E-64 (Cathepsin B and L inhibitor) and Pepstatin A (Cathepsin D inhibitor) on spontaneous and experimental metastasis formation were investigated in mice with MCa mammary carcinoma, M5076 ovarian sarcoma and L1210 leukemia. Pepstatin induced a marked decrease in the number of spontaneous metastasis in MCa or M5076 tumor bearing mice. This phenomenon was also noted with E-64 but only in M5076 tumor bearing mice. On the other hand, both these agents were unable to prevent the formation of experimental metastasis in mice injected i.v. with L1210, MCa or M5076 tumor cells or with tumor cells in which Cathepsin B, L and D activities were inhibited by a 24 hour continuous exposure …

Ovarian NeoplasmsCathepsin LMammary Neoplasms ExperimentalpepstatinCysteine Proteinase Inhibitorsproteinase inhibitors.Cathepsin DCathepsinsCathepsinCathepsin BCysteine EndopeptidasesMiceLeucineEndopeptidasesPepstatinsTumor Cells CulturedAnimalsmetastasiFemaleNeoplasm MetastasisLeukemia L1210E-64In vivo (Athens, Greece)
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2012

Diazepinomicin is a dibenzodiazepine alkaloid with an unusual structure among the known microbial metabolites discovered so far. Diazepinomicin was isolated from the marine sponge-associated strain Micromonospora sp. RV115 and was identified by spectroscopic analysis and by comparison to literature data. In addition to its interesting preclinical broad-spectrum antitumor potential, we report here new antioxidant and anti-protease activities for this compound. Using the ferric reducing antioxidant power (FRAP) assay, a strong antioxidant potential of diazepinomicin was demonstrated. Moreover, diazepinomicin showed a significant antioxidant and protective capacity from genomic damage induced …

ProteasesAntioxidantDiazepinomicinAntiparasiticmedicine.drug_classmedicine.medical_treatmentPharmaceutical ScienceBiologyTrypanosoma brucei01 natural sciencesMicrobiologyCathepsin L03 medical and health sciencesDrug DiscoverymedicineMicromonosporaPharmacology Toxicology and Pharmaceutics (miscellaneous)030304 developmental biologychemistry.chemical_classification0303 health sciencesReactive oxygen species010405 organic chemistrybiology.organism_classification0104 chemical scienceschemistryBiochemistrybiology.proteinMarine Drugs
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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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Development of rhodesain inhibitors with a 3-bromoisoxazoline warhead

2013

Novel rhodesain inhibitors were obtained by combining an enantiomerically pure 3-bromoisoxazoline warhead with a specific peptidomimetic recognition moiety. All derivatives behaved as inhibitors of rhodesain, with low micromolar Ki values. Their activity against the enzyme was found to be paralleled by an in vitro antitrypanosomal activity, with IC50 values in the mid-micromolar range. Notably, a preference for parasitic over human proteases, specifically cathepsins B and L, was observed.

ProteasesStereochemistryPeptidomimeticCathepsin LMolecular ConformationStereoisomerismCysteine Proteinase InhibitorsBiologyCrystallography X-RayBiochemistryCysteine Proteinase InhibitorsCathepsin BCathepsin LinhibitorsDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticstrypanosomarhodesainPharmacologychemistry.chemical_classificationOrganic ChemistryStereoisomerismIsoxazolesisoxazolinesCombinatorial chemistryIn vitroCysteine EndopeptidasesEnzymechemistrypeptidomimeticsbiology.proteinMolecular Medicineinhibitors; isoxazolines; peptidomimetics; rhodesain; trypanosomaProtein Binding
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Definitive host influences the proteomic profile of excretory/secretory products of the trematode Echinostoma caproni

2016

Background Echinostoma caproni is an intestinal trematode extensively used as experimental model for the study of factors that determine the course of intestinal helminth infections, since this markedly depends on the host species. Although the host-dependent mechanisms for either chronic establishment or early parasite rejection have been broadly studied, little is known regarding the parasite response against different host environments. Methods To identify host-dependent differentially expressed proteins, a comparative proteomic analysis of the excretory/secretory products released from E. caproni adults, isolated from hosts displaying different compatibility with this trematode, was per…

Proteomics0301 basic medicineProteomeHelminth proteinEchinostoma caproniMalate dehydrogenaseHydroxyacylglutathione hydrolaseMicrobiologyCathepsin LMice03 medical and health sciencesExcretory/secretory productsIntestinal mucosaEchinostomaHelminthAnimalsHelminthsbiologyResearchHelminth Proteinsbiology.organism_classificationRatsProteome plasticity2-dimensional gel electrophoresis030104 developmental biologyInfectious DiseasesExcretory systemHost-Pathogen InteractionsImmunologybiology.proteinParasitologyEchinostomaParasites & Vectors
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Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellid Monorhaphis chuni.

2008

SUMMARYSilicateins, members of the cathepsin L family, are enzymes that have been shown to be involved in the biosynthesis/condensation of biosilica in spicules from Demospongiae (phylum Porifera), e.g. Tethya aurantium and Suberites domuncula. The class Hexactinellida also forms spicules from this inorganic material. This class of sponges includes species that form the largest biogenic silica structures on earth. The giant basal spicules from the hexactinellids Monorhaphis chuni and Monorhaphis intermedia can reach lengths of up to 3 m and diameters of 10 mm. The giant spicules as well as the tauactines consist of a biosilica shell that surrounds the axial canal, which harbours the axial f…

SpiculePhysiologyOceans and SeasMolecular Sequence DataAquatic ScienceCysteine Proteinase InhibitorsCathepsin LDemospongeSponge spiculeAnimalsAmino Acid SequenceTethya aurantiumMolecular BiologyEcology Evolution Behavior and SystematicsPhylogenyBinding SitesbiologyHexactinellidAnimal StructuresAnatomybiology.organism_classificationCathepsinsCystatinsPoriferaSuberites domunculaMolecular WeightSpongeBiochemistryInsect ScienceMolecular Probesbiology.proteinAnimal Science and ZoologyProtein Processing Post-TranslationalThe Journal of experimental biology
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Synthesis and biological evaluation of papain-family cathepsin L-like cysteine protease inhibitors containing a 1,4-benzodiazepine scaffold as antipr…

2014

Novel papain-family cathepsin L-like cysteine protease inhibitors endowed with antitrypanosomal and antimalarial activity were developed, through an optimization study of previously developed inhibitors. In the present work, we studied the structure-activity relationships of these derivatives, with the aim to develop new analogues with a simplified and more synthetically accessible structure and with improved antiparasitic activity. The structure of the model compounds was significantly simplified by modifying or even eliminating the side chain appended at the C3 atom of the benzodiazepine scaffold. In addition, a simple methylene spacer of appropriate length was inserted between the benzod…

Trypanosomamedicine.drug_classPeptidomimeticStereochemistryAntiparasiticCell SurvivalCathepsin LAntiprotozoal AgentsCysteine Proteinase InhibitorsBiochemistryCathepsin BCell LineCathepsin Lchemistry.chemical_compoundBenzodiazepinesMiceStructure-Activity RelationshipDrug DiscoverymedicineMoietyAnimalsGeneral Pharmacology Toxicology and PharmaceuticsPharmacologyCathepsinbiologyOrganic ChemistryCombinatorial chemistryCysteine proteasePapainantiprotozoal agents; inhibitors; Malaria; Peptidomimetics; structure-activity relationshipsCysteine EndopeptidaseschemistryAntiprotozoalbiology.proteinMolecular MedicineProtein BindingChemMedChem
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Cathepsin D activity levels in colorectal cancer: Correlation with cathepsin B and L and other biological and clinical parameters

1994

Cathepsin D, B and L activity levels were determined in colorectal cancer and correlated with a number of biological and clinical parameters. Our studies have evidenced significant higher activity levels of these lysosomal enzymes in tumor cytosol compared to paired normal mucosa as well as an evident increase of tumor specific cathepsin D activity in Dukes' stage A tumors compared to later stages (B, C and D). Furthermore, significant higher cathepsin B and L activity levels were observed in Dukes' stage A compared to Dukes' stage D tumors while significant higher cathepsin B activity levels were observed in tumors ≤5 cm than in those >5 cm as well as in moderately differentiated tumors…

Tumor progression.Cathepsin LMetastasiLysosomal proteinaseCathepsin DColorectal cancerCathepsin B
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Cathepsin L in Normal and Pathological Bone Remodeling

2011

Abstract Cathepsin L is a ubiquitous lysosomal cysteine endopeptidase that is mainly involved in the metabolic turnover of intracellular proteins. However, it is now well established that this enzyme may also be implicated in the regulation of other important biological processes includ- ing bone resorption. Therefore, altered expression levels of Cathepsin L may result in disturbances of bone homeo- stasis and, eventually, in the onset of pathological condi- tions associated with altered bone turnover. These observations support the concept that Cathepsin L may be regarded as an additional target for the development of novel therapeutic options for the treatment of patients with bone disea…

chemistry.chemical_classificationmedicine.medical_specialtybiologyEndocrinology Diabetes and MetabolismBone metastasisBone diseases Bone metastasis Cancer Cathepsin L Cysteine proteinases Proteinase inhibitorsmedicine.diseaseBone resorptionCell biologyBone remodelingCathepsin LEndocrinologyEndocrinologyEnzymechemistryInternal medicinemedicineCathepsin Kbiology.proteinOrthopedics and Sports MedicinePathologicalHomeostasisClinical Reviews in Bone and Mineral Metabolism
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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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