Search results for "Cysteine proteinase"

showing 10 items of 50 documents

Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spa…

2006

Missense mutations in the humanPLP1gene lead to dysmyelinating diseases with a broad range of clinical severity, ranging from severe Pelizaeus–Merzbacher disease (PMD) to milder spastic paraplegia type 2 (SPG-2). The molecular pathology has been generally attributed to endoplasmic reticulum (ER) retention of misfolded proteolipid protein (PLP) (and its splice isoform DM20) and induction of the unfolded protein response. As opposed to previous studies of heterologous expression systems, we have analyzed PLP/DM20 trafficking in oligodendroglial cells, thereby revealing differences between PMD and SPG-2-associated PLP/DM20 isoforms. PLPA242Vand DM20A242V(jimpy-msdin mice), associated with seve…

Proteolipid protein 1Time FactorsLeupeptinsBlotting WesternGene Expressionchemical and pharmacologic phenomenaNerve Tissue ProteinsBiologyProtein degradationCysteine Proteinase InhibitorsTransfectionMiceMice Neurologic MutantsCricetulusMembrane MicrodomainsMutant proteinimmune system diseasesCricetinaeAnimalsImmunoprecipitationMyelin Proteolipid ProteinLipid raftCells CulturedGeneral NeuroscienceEndoplasmic reticulumCholesterol bindingER retentionArticlesImmunohistochemistryCell biologynervous system diseasesOligodendrogliaProtein TransportCholesterolBiochemistryUnfolded protein responselipids (amino acids peptides and proteins)Mutant ProteinsSubcellular FractionsThe Journal of neuroscience : the official journal of the Society for Neuroscience
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Hamster Bcl-2 Protein Is Cleaved in Vitro and in Cells by Caspase-9 and Caspase-3

2001

Full-length cDNA of hamster bcl-2 (771 nt) was cloned by RT-PCR and inserted into pGEX-4T-1 to produce the recombinant hamster Bcl-2 protein. The purified recombinant Bcl-2 protein (26.4 kDa) was used as a substrate for the active human caspase-3 and caspase-9 in vitro. It is shown here that Bcl-2 is efficiently cleaved by caspase-3 to a 23 kDa fragment. Although not possessing a putative caspase-9 cleavage site in its sequence, hamster Bcl-2 was also cleaved by caspase-9 into exactly the same 23 kDa cleavage product, indicating that cleavage occurred at the same site. Caspase-3- and caspase-9-mediated cleavage of Bcl-2 was efficiently blocked by caspase-3 (zDEVD) and caspase-9 (zLEHD) inhi…

Recombinant Fusion ProteinsBlotting WesternBiophysicsHamsterCaspase 3CHO CellsCysteine Proteinase InhibitorsCleavage (embryo)Biochemistrylaw.inventionlawCricetinaeComplementary DNAAnimalsHumansMolecular BiologyCaspaseGlutathione TransferaseCleavage stimulation factorbiologyCaspase 3Chinese hamster ovary cellThrombinCell BiologyCaspase InhibitorsMolecular biologyCaspase 9Proto-Oncogene Proteins c-bcl-2Caspasesbiology.proteinRecombinant DNAOligopeptidesBiochemical and Biophysical Research Communications
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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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Proteasome comprising a beta1 inducible subunit acts as a negative regulator of NADPH oxidase during elicitation of plant defense reactions.

2005

Elicitation of defense reactions in tobacco by cryptogein, triggered a production of active oxygen species (AOS) via the NADPH oxidase, NtrbohD, and an accumulation of beta1din, a defense induced beta-type subunit of 20S proteasome. The proteasome inhibitor, MG132, stimulated this AOS production. Tobacco cells transformed with sense constructs of beta1din showed an inhibition of the AOS production following elicitin treatment, whereas the antisense transformed cells showed a strongly enhanced AOS production. In cells transformed with sense construct of beta1din, the NtrbohD transcripts failed to be induced by cryptogein as observed in control and antisense transformed cells. Conversely, in …

Tobacco BY-2 cellsHypersensitive responseProteasome Endopeptidase ComplexLeupeptinsBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyCysteine Proteinase InhibitorsBiochemistrychemistry.chemical_compoundStructural BiologyMG132Sense (molecular biology)TobaccoGeneticsmedicineNADPH OXIDASEPROTEASOMEMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSPlant ProteinsCRYPTOGEINNADPH oxidaseTOBACCO BY-2 CELLSNADPH OxidasesElicitinCell BiologyOligonucleotides AntisenseProtein SubunitsProteasomechemistryBiochemistryProteasome inhibitorbiology.proteinPLANT DEFENSEAOS PRODUCTIONReactive Oxygen SpeciesProteasome Inhibitorsmedicine.drugFEBS letters
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Development of Novel Benzodiazepine-Based Peptidomimetics as Inhibitors of Rhodesain from Trypanosoma brucei rhodesiense.

2020

Starting from the reversible rhodesain inhibitors 1 a-c, which have Ki values towards the target protease in the low-micromolar range, we have designed a series of peptidomimetics, 2 a-g, that contain a benzodiazepine scaffold as a β-turn mimetic; they are characterized by a specific peptide sequence for the inhibition of rhodesain. Considering that irreversible inhibition is strongly desirable in the case of a parasitic target, a vinyl ester moiety acting as Michael-acceptor was introduced as the warhead; this portion was functionalized in order to evaluate the size of corresponding enzyme pocket that could accommodate this substituent. With this investigation, we identified an irreversibl…

Trypanosoma brucei rhodesiensehuman African trypanosomiasiStereochemistryPeptidomimeticmedicine.medical_treatmentSubstituentAntiprotozoal AgentsTrypanosoma bruceiCysteine Proteinase Inhibitors01 natural sciencesBiochemistrychemistry.chemical_compoundBenzodiazepinesStructure-Activity RelationshipDrug DevelopmentParasitic Sensitivity TestsDrug DiscoverymedicineMoietyTrypanosoma bruceiGeneral Pharmacology Toxicology and PharmaceuticsPeptide sequencePharmacologyrhodesainProteasebiologyDose-Response Relationship DrugMolecular Structure010405 organic chemistryOrganic ChemistryTrypanosoma brucei rhodesiensebenzodiazepine scaffoldbiology.organism_classificationpeptidomimetic0104 chemical sciences010404 medicinal & biomolecular chemistryCysteine EndopeptidaseschemistryMolecular MedicinePeptidomimeticsMichael acceptorLead compoundChemMedChem
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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 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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Synergistic cytotoxic interactions between sodium butyrate, MG132 and camptothecin in human retinoblastoma Y79 cells.

2000

This paper studies the effects caused in human retinoblastoma Y79 cells by treatment with combinations of sodium butyrate, the inhibitor of topoisomerase I camptothecin and the inhibitor of 26S proteasome MG132. The combination of sodium butyrate and camptothecin resulted in a strong synergistic cytotoxicity, as revealed by combination indices of 0.77 and 0.52 calculated at IC(50) and IC(75). Synergistic interactions were also demonstrated for combinations of sodium butyrate and MG132, camptothecin and MG132 and for a combination of all three compounds. The cytotoxic effects observed after the combined treatments can be considered a consequence of apoptosis, as suggested by the appearance o…

medicine.drug_classCell SurvivalLeupeptinsSodiumchemistry.chemical_elementApoptosisButyrateBiologyCysteine Proteinase Inhibitorschemistry.chemical_compoundMG132Antineoplastic Combined Chemotherapy ProtocolsmedicineTumor Cells CulturedHumansheterocyclic compoundsEnzyme InhibitorsRetinoblastomaCaspase 3TopoisomeraseRetinoblastomaSodium butyrateDrug SynergismGeneral Medicinemedicine.diseaseeye diseasesEnzyme ActivationButyrateschemistryBiochemistryProto-Oncogene Proteins c-bcl-2CaspasesCancer researchbiology.proteinCamptothecinTopoisomerase I InhibitorsTumor Suppressor Protein p53CamptothecinTopoisomerase inhibitormedicine.drugTumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine
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Dipeptidyl Enoates As Potent Rhodesain Inhibitors That Display a Dual Mode of Action

2015

Dipeptidyl enoates were prepared through a high-yielding two-step synthetic route. They have a dipeptidic structure with a 4-oxoenoate moiety as a warhead with multiple reactive sites. Dipeptidyl enoates were screened against rhodesain and human cathepsins B and L, and were found to be potent and selective inhibitors of rhodesain. Among them (S,E)-ethyl 5-((S)-2-{[(benzyloxy)carbonyl]amino}-3-phenylpropanamido)-7-methyl-4-oxooct-2-enoate (6) was the most potent, with an IC50 value of 16.4 nm and kinact/Ki=1.6×106 m−1 s−1 against rhodesain. These dipeptidyl enoates display a reversible mode of inhibition at very low concentrations and an irreversible mode at higher concentrations. Inhibition…

trypanosomiasisStereochemistrysleeping sicknessCathepsin LDrug Evaluation PreclinicalChemistry Techniques SyntheticInhibition kineticsCysteine Proteinase InhibitorsBiochemistryCathepsin BInhibitory Concentration 50Structure-Activity RelationshipinhibitorsDrug DiscoveryHumansMoietyMolecular Targeted TherapyGeneral Pharmacology Toxicology and PharmaceuticsIC50Volume concentrationrhodesainPharmacologyChemistryOrganic ChemistryDual modeDipeptidesTrypanocidal AgentsCombinatorial chemistryMolecular Docking SimulationCysteine EndopeptidasesKineticsdipeptidyl enoatesTrypanosomiasis AfricanDocking (molecular)Molecular MedicineCysteine thiolateChemMedChem
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