Search results for "Peptidases"

showing 10 items of 319 documents

A major cysteine proteinase, EPB, in germinating barley seeds: structure of two intronless genes and regulation of expression

1996

The barley cysteine proteinase B (EPB) is the main protease responsible for the degradation of endosperm storage proteins providing nitrogenous nutrients to support the growth of young seedlings. The expression of this enzyme is induced in the germinating seeds by the phytohormone, gibberellin, and suppressed by another phytohormone, abscisic acid. In situ hybridization experiments indicate that EPB is expressed in the scutellar epithelium within 24 h of seed germination, but the aleurone tissue surrounding the starchy endosperm eventually becomes the main tissue expressing this enzyme. The EPB gene family of barley consists of two very similar genes, EPB1 and EPB2, both of which have been …

Transcription GeneticMolecular Sequence DataGerminationPlant ScienceBiologyGenes PlantGene Expression Regulation EnzymologicEndospermGene Expression Regulation PlantAleuroneComplementary DNAGeneticsGene familyAmino Acid SequenceRNA MessengerPromoter Regions GeneticGeneIn Situ HybridizationPhylogenyPlant ProteinsRegulation of gene expressionReporter geneBase SequenceSequence Homology Amino AcidChromosome MappingGene Expression Regulation Developmentalfood and beveragesHordeumGeneral MedicineMolecular biologyIntronsCysteine EndopeptidasesBiochemistryRNA PlantHordeum vulgareAgronomy and Crop SciencePlant Molecular Biology
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Cross-talk between Different Enhancer Elements during Mitogenic Induction of the Human Stromelysin-1 Gene

1996

Platelet-derived growth factor (PDGF) induces the expression of human stromelysin-1, a matrix metalloproteinase involved in tumor invasion and metastasis. Here it is shown that stromelysin-1 gene induction by PDGF depends on Ras and involves three previously identified promoter elements (the stromelysin-1 PDGF-responsive element (SPRE) site, the two head-to-head polyomavirus enhancer A-binding protein-3 (PEA3) sites, and the activator protein-1 (AP-1) binding site). During mitogenic induction, these responsive elements appear to be organized in two independent transcriptional units, SPRE-AP-1 and PEA3-AP-1, which result from specific element cross-talking. Interestingly, expression of a dom…

Transcription GeneticProto-Oncogene Proteins c-junMolecular Sequence DataProtein Serine-Threonine KinasesBiologyTransfectionBiochemistryStromelysin 1Proto-Oncogene Proteins p21(ras)MiceProto-Oncogene ProteinsAnimalsHumansBinding siteEnhancerMolecular BiologyTranscription factorGeneProtein Kinase CProtein kinase CPlatelet-Derived Growth FactorBase SequenceActivator (genetics)Metalloendopeptidases3T3 CellsCell BiologyMolecular biologyRecombinant ProteinsDNA-Binding ProteinsProto-Oncogene Proteins c-rafTranscription Factor AP-1Enhancer Elements GeneticEnzyme Inductionbiology.proteinMatrix Metalloproteinase 3MitogensPlatelet-derived growth factor receptorJournal of Biological Chemistry
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Protease-mediated processing of Argonaute proteins controls small RNA association

2020

SummarySmall RNA pathways defend the germlines of animals against selfish genetic elements and help to maintain genomic integrity. At the same time, their activity needs to be well-controlled to prevent silencing of ‘self’ genes. Here, we reveal a proteolytic mechanism that controls endogenous small interfering (22G) RNA activity in the Caenorhabditis elegans germline to protect genome integrity and maintain fertility. We find that WAGO-1 and WAGO-3 Argonaute (Ago) proteins are matured through proteolytic processing of their unusually proline-rich N-termini. In the absence of DPF-3, a P-granule-localized N-terminal dipeptidase orthologous to mammalian DPP8/9, processing fails, causing a cha…

Transposable elementSmall RNAanimal structuresDNA damageBiologyDipeptidyl peptidaseSubstrate Specificity03 medical and health sciences0302 clinical medicineAnimalsGene silencingRNA MessengerRNA Small InterferingCaenorhabditis elegansCaenorhabditis elegans ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMolecular BiologyGeneCaenorhabditis elegans030304 developmental biology0303 health sciencesWild typeRNACell BiologyArgonautebiology.organism_classificationCell biologyFertilityArgonaute ProteinsProteolysisRNA HelminthProtein Processing Post-Translational030217 neurology & neurosurgery
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Keyhole Limpet Hemocyanin Type 2 (KLH2): Detection and Immunolocalization of a Labile Functional Unit h

2000

Keyhole limpet hemocyanin (KLH) is a mixture of two hemocyanin isoforms, termed KLH1 and KLH2. Within KLH1 eight oxygen-binding functional units (FUs), 1-a to 1-h, have been identified, in contrast to KLH2, which was previously thought to be organized in seven FUs (2-a to 2-g). By limited proteolysis of KLH2 subunits, isolation of the polypeptide fragments, and N-terminal sequencing, we have now identified an eighth FU of type h, with a molecular mass of 43 kDa. This is unusually small for a FU h from a gastropodan hemocyanin. It is also shown that KLH2 didecamers can be split into a stable and homogeneous population of decamers by dialysis against 50 mM Tris/HCl, pH 7.5, in the absence of …

Trismedicine.medical_treatmentProteolysisMolecular Sequence DataPopulationMegathura crenulataDivalentStructure-Activity Relationshipchemistry.chemical_compoundStructural BiologyEndopeptidasesmedicineAnimalsProtein IsoformsAmino Acid SequenceMicroscopy ImmunoelectronProtein Structure Quaternaryeducationchemistry.chemical_classificationeducation.field_of_studybiologymedicine.diagnostic_testMolecular massAntibodies MonoclonalHemocyaninbiology.organism_classificationMolecular biologyMolecular WeightchemistryMolluscaHemocyaninsbiology.proteinKeyhole limpet hemocyaninJournal of Structural Biology
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Evaluation of curcumin irreversibility

2019

Dear Editor,We would like to reply to the letter to the Editor of Steverding (2018) on our research article “Drug combination studies of curcumin and genistein against rhodesain of Trypanosoma bruc...

Trypanosoma brucei rhodesienseCurcuminCysteine EndopeptidasesGenisteinPlant SciencePharmacology01 natural sciencesBiochemistryAnalytical Chemistrychemistry.chemical_compoundMedicineResearch articlebiology010405 organic chemistrybusiness.industryOrganic ChemistryTrypanosoma brucei rhodesiensebiology.organism_classificationGenistein0104 chemical sciencesCysteine EndopeptidasesDrug Combinations010404 medicinal & biomolecular chemistrychemistryTrypanosomaCurcuminbusinessNatural Product Research
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Optimization Strategy of Novel Peptide-Based Michael Acceptors for the Treatment of Human African Trypanosomiasis

2019

This paper describes an optimization strategy of the highly active vinyl ketone 3 which was recognized as a strong inhibitor of rhodesain of Trypanosoma brucei rhodesiense, endowed with a ksecond v...

Trypanosoma brucei rhodesienseStrong inhibitorKetoneStereochemistryProtein ConformationPeptide01 natural sciences03 medical and health sciencesStructure-Activity RelationshipSUBSTRATEDrug DiscoverymedicineHumansAfrican trypanosomiasisSulfonesBIOLOGICAL EVALUATION030304 developmental biologyWARHEADchemistry.chemical_classification0303 health sciencesMolecular StructureChemistryDERIVATIVESTrypanosoma brucei rhodesienseCYSTEINE PROTEASES RHODESAIN BIOLOGICAL EVALUATION CATHEPSIN-L INHIBITORS BRUCEI PEPTIDOMIMETICS FALCIPAIN-2 DERIVATIVES SUBSTRATE WARHEADBRUCEImedicine.diseaseFALCIPAIN-2Trypanocidal Agents0104 chemical sciences010404 medicinal & biomolecular chemistryCysteine EndopeptidasesTrypanosomiasis AfricanCYSTEINE PROTEASES RHODESAINCATHEPSIN-LMolecular MedicineINHIBITORSPEPTIDOMIMETICS
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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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The tumor suppressor CYLD controls the function of murine regulatory T cells.

2012

Abstract CYLD was originally identified as a tumor suppressor gene mutated in familial cylindromatosis, an autosomal dominant predisposition to multiple benign neoplasms of the skin known as cylindromas. The CYLD protein is a deubiquitinating enzyme that acts as a negative regulator of NF-κB and JNK signaling through its interaction with NEMO and TNFR-associated factor 2. We have previously described a novel mouse strain that expresses solely and excessively a naturally occurring splice variant of CYLD (CYLDex7/8). In this study, we demonstrate that CYLD plays a critical role in Treg development and function. T cells of CYLDex7/8 mice had a hyperactive phenotype manifested by increased prod…

Tumor suppressor geneT cellImmunologyBiologyT-Lymphocytes RegulatoryDeubiquitinating Enzyme CYLDlaw.inventionProinflammatory cytokineMicelawmedicineImmunology and AllergyAnimalsCTLA-4 AntigenIL-2 receptorTumor Suppressor ProteinsInterleukin-2 Receptor alpha SubunitIntracellular Signaling Peptides and ProteinsNF-kappa BFOXP3PhenotypeMice Mutant StrainsCell biologyDeubiquitinating Enzyme CYLDCysteine Endopeptidasesmedicine.anatomical_structureGene Expression RegulationImmunologySuppressorJournal of immunology (Baltimore, Md. : 1950)
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Naturally occurring short splice variant of CYLD positively regulates dendritic cell function

2009

Abstract Deubiquitination of NF-κB members by CYLD is crucial in controlling the magnitude and nature of cell activation. The role of the naturally occurring CYLD splice variant in dendritic cell (DC) function was analyzed using CYLDex7/8 mice, which lack the full-length CYLD (flCYLD) transcript and overexpress the short splice variant (sCYLD). Bone marrow–derived DCs from CYLDex7/8 mice display a hyperactive phenotype in vitro and in vivo and have a defect in establishing tolerance with the use of DEC-205–mediated antigen targeting to resting DCs. The combination of sCYLD overexpression and lack of flCYLD in CYLDex7/8 DCs leads to enhanced NF-κB activity accompanied by an increased nuclear…

Tumor suppressor geneTransgeneImmunologyRegulatorMice TransgenicBiologyBiochemistryDeubiquitinating Enzyme CYLDMiceAnimalsAntigen-presenting cellNF-kappa BDendritic CellsCell BiologyHematologyDendritic cellDeubiquitinating Enzyme CYLDCell biologyMice Inbred C57BLAlternative SplicingCysteine EndopeptidasesPhenotypeImmunologySignal transductionCell activationSignal TransductionBlood
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