Search results for "proteolysis"

showing 10 items of 119 documents

Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells

1994

AbstractExocytosis of secretory granules by adrenal chromaffin cells is blocked by the tetanus toxin light chain in a zinc specific manner. Here we show that cellular synaptobrevin is almost completely degraded by the tetanus toxin light chain within 15 min. We used highly purified adrenal secretory granules to show that synaptobrevin, which can be cleaved by the tetanus toxin light chain, is localized in the vesicular membrane. Proteolysis of synaptobrevin in cells and in secretory granules is reversibly inhibited by the zinc chelating agent dipicolinic acid. Moreover, cleavage of synaptobrevin present in secretory granules by the tetanus toxin light chain is blocked by the zinc peptidase …

SynaptobrevinProteolysismedicine.medical_treatmentMolecular Sequence DataBiophysicsSynaptobrevinNerve Tissue ProteinsIn Vitro Techniquesmedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosisExocytosisR-SNARE ProteinsStructural BiologyGeneticsmedicineAnimalsChromaffin GranulesAmino Acid SequenceMolecular BiologySecretory granuleR-SNARE ProteinsAdrenal medullaProteasemedicine.diagnostic_testChemistryToxinMembrane ProteinsCell BiologyPeptide FragmentsTetanus toxinmedicine.anatomical_structureBiochemistryCattleAdrenal medullaFEBS Letters
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Taspase1: a 'misunderstood' protease with translational cancer relevance

2015

Proteolysis is not only a critical requirement for life, but the executing enzymes also play important roles in numerous pathological conditions, including cancer. Therefore, targeting proteases is clearly relevant for improving cancer patient care. However, to effectively control proteases, a profound knowledge of their mechanistic function as well as their regulation and downstream signalling in health and disease is required. The highly conserved protease Threonine Aspartase1 (Taspase1) is overexpressed in numerous liquid and solid malignancies and was characterized as a 'non-oncogene addiction' protease. Although Taspase1 was shown to cleave various regulatory proteins in humans as well…

Threonine0301 basic medicineCancer ResearchProteasesmedicine.medical_treatmentProteolysisComputational biologyDiseaseBiologyBioinformaticsmedicine.disease_causeAspartate Ammonia-LyaseGene Expression Regulation EnzymologicTranslational Research Biomedical03 medical and health sciencesNeoplasmsEndopeptidasesGeneticsmedicineHumansEnzyme InhibitorsMolecular BiologyProteaseMolecular Structuremedicine.diagnostic_testCancermedicine.diseaseGene Expression Regulation Neoplastic030104 developmental biologyProteasomeCarcinogenesisBiologieFunction (biology)Oncogene
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Coordinated Sumoylation and Ubiquitination Modulate EGF Induced EGR1 Expression and Stability

2011

Background Human early growth response-1 (EGR1) is a member of the zing-finger family of transcription factors induced by a range of molecular and environmental stimuli including epidermal growth factor (EGF). In a recently published paper we demonstrated that integrin/EGFR cross-talk was required for Egr1 expression through activation of the Erk1/2 and PI3K/Akt/Forkhead pathways. EGR1 activity and stability can be influenced by many different post-translational modifications such as acetylation, phosphorylation, ubiquitination and the recently discovered sumoylation. The aim of this work was to assess the influence of sumoylation on EGF induced Egr1 expression and/or stability. Methods We …

Time FactorsTranscription GeneticSUMO proteinlcsh:MedicineUbiquitin-conjugating enzymeBiochemistrychemistry.chemical_compoundEpidermal growth factorMG132protein 1lcsh:ScienceMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3MultidisciplinaryProtein translationProtein Stabilitygene expression regulationCell biologyepidermal growth factorResearch Articlemedicine.drugProteasome Endopeptidase Complexendocrine systemkinase 1SUMO-1 ProteinBiologyDNA-binding proteinsGeneticsmedicineHumansBiologySettore BIO/10 - BIOCHIMICAProtein kinase BPI3K/AKT/mTOR pathwayEarly Growth Response Protein 1lcsh:RMitogen-activated proteinProteinsSumoylationRegulatory proteinsenzyme activationRNA stabilityMolecular biologychemistryProteolysisUbiquitin-Conjugating EnzymesProteasome inhibitorlcsh:QEarly growth responseGene expressionCell linePLoS ONE
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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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Paenibacillus larvae Chitin-Degrading Protein PlCBP49 Is a Key Virulence Factor in American Foulbrood of Honey Bees

2014

Paenibacillus larvae, the etiological agent of the globally occurring epizootic American Foulbrood (AFB) of honey bees, causes intestinal infections in honey bee larvae which develop into systemic infections inevitably leading to larval death. Massive brood mortality might eventually lead to collapse of the entire colony. Molecular mechanisms of host-microbe interactions in this system and of differences in virulence between P. larvae genotypes are poorly understood. Recently, it was demonstrated that the degradation of the peritrophic matrix lining the midgut epithelium is a key step in pathogenesis of P. larvae infections. Here, we present the isolation and identification of PlCBP49, a mo…

Veterinary MicrobiologyChitinPathogenesisPathology and Laboratory MedicineVirulence factorchemistry.chemical_compoundMedicine and Health SciencesPeritrophic matrixlcsh:QH301-705.5biologyVirulenceGram Positive BacteriaBeesVeterinary BacteriologyBacterial PathogensVeterinary DiseasesMedical MicrobiologyLarvaHost-Pathogen InteractionsPaenibacillusResearch Articlelcsh:Immunologic diseases. Allergy570American foulbroodVirulence FactorsImmunologyMolecular Sequence DataVirulenceMicrobiologyMicrobiologyChitinBacterial ProteinsVirologyGeneticsAnimalsAmino Acid SequenceMolecular BiologyMicrobial PathogensGram-Positive Bacterial InfectionsSequence Homology Amino AcidfungiBiology and Life SciencesMidgutBacteriologyHoney beebiology.organism_classificationlcsh:Biology (General)chemistryProteolysisParasitologyVeterinary Sciencelcsh:RC581-607BacteriaPLoS Pathogens
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Diversity and technological potential of lactic acid bacteria of wheat flours

2013

Abstract Lactic acid bacteria (LAB) were analysed from wheat flours used in traditional bread making throughout Sicily (southern Italy). Plate counts, carried out in three different media commonly used to detect food and sourdough LAB, revealed a maximal LAB concentration of approximately 4.75 Log CFU g−1. Colonies representing various morphological appearances were isolated and differentiated based on phenotypic characteristics and genetic analysis by randomly amplified polymorphic DNA (RAPD)-PCR. Fifty unique strains were identified. Analysis by 16S rRNA gene sequencing grouped the strains into 11 LAB species, which belonged to six genera: Enterococcus, Lactobacillus, Lactococcus, Leucono…

WeissellaLactococcusFlourLeuconostoc pseudomesenteroidesmedicine.disease_causeMicrobiologyMicrobiologyAcidificationWheat flourIndustrial MicrobiologyBacterial ProteinsLeuconostoc citreumLactobacillusmedicineLactic acid bacteriaLeuconostocLactic AcidWeissella cibariaProteolysiAcidification; Lactic acid bacteria; Proteolysis; Sourdough; Volatile organic compounds; Wheat flourPhylogenyTriticumbiologyfood and beveragesBiodiversitySettore AGR/15 - Scienze E Tecnologie AlimentariVolatile organic compoundbiology.organism_classificationLactobacillaceaeSourdoughPediococcusAcidsPeptide HydrolasesFood ScienceSettore AGR/16 - Microbiologia Agraria
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Review : Compounds involved in the flavor of surface mold-ripened cheeses : Origins and properties

1996

Abstract Cheese flavor is obtained through a series of chemical changes that occur in the curd during the early stages of ripening. Lipid hydrolysis leads to FFA, which serve as substrates for further reactions. Peptides and amino acids, which results from proteolysis, also lead to aroma compounds through enzymic and chemical reactions. This paper is a review of the current knowledge about the compounds that contribute to flavor in mold-ripened cheeses, especially Camembert-type cheese. Discussed are the pathway of formation, the sensory properties (odorous notes and perception thresholds), and the quantities of the main volatile compounds encountered in these types of cheeses.

[SDV.SA]Life Sciences [q-bio]/Agricultural sciencesCheese FlavorProteolysisOrganolepticCheese ripeningHydrolysis0404 agricultural biotechnologyGeneticsmedicineOrganic chemistryFood scienceAromaFlavor[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesmedicine.diagnostic_testbiologyChemistry0402 animal and dairy sciencefood and beveragesRipening04 agricultural and veterinary sciencesbiology.organism_classification040401 food science040201 dairy & animal science3. Good healthAnimal Science and ZoologyFood Science
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Potential anticarcinogenic peptides from bovine milk.

2012

Bovine milk possesses a protein system constituted by two major families of proteins: caseins (insoluble) and whey proteins (soluble). Caseins (αS1,αS2,β, andκ) are the predominant phosphoproteins in the milk of ruminants, accounting for about 80% of total protein, while the whey proteins, representing approximately 20% of milk protein fraction, includeβ-lactoglobulin,α-lactalbumin, immunoglobulins, bovine serum albumin, bovine lactoferrin, and lactoperoxidase, together with other minor components. Different bioactivities have been associated with these proteins. In many cases, caseins and whey proteins act as precursors of bioactive peptides that are released, in the body, by enzymatic pro…

animal structuresAntioxidantmedicine.medical_treatmentProteolysisReview ArticleBiochemistryfluids and secretionsmedicineFood scienceBovine serum albuminMolecular Biologychemistry.chemical_classificationbiologymedicine.diagnostic_testbusiness.industryLactoperoxidasefood and beveragesBiological activityGeneral MedicineAntimicrobialEnzymechemistryBiochemistrybiology.proteinAntibodybusiness
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IDENTIFICATION OF A CALMODULIN-BINDING SITE WITHIN THE DOMAIN I OF BACILLUS THURINGIENSISCry3Aa TOXIN

2012

Bacillus thuringiensis Cry3Aa toxin is a coleopteran specific toxin highly active against Colorado Potato Beetle (CPB).We have recently shown that Cry3Aa toxin is proteolytically cleaved by CPB midgut membrane associated metalloproteases and that this cleavage is inhibited by ADAM metalloprotease inhibitors. In the present study, we investigated whether the Cry3Aa toxin is a calmodulin (CaM) binding protein, as it is the case of several different ADAM shedding substrates. In pull-down assays using agarose beads conjugated with CaM, we demonstrated that Cry3Aa toxin specifically binds to CaM in a calcium-independent manner. Furthermore, we used gel shift assays and (1)H NMR spectra to demons…

chemistry.chemical_classificationCalmodulinmedicine.diagnostic_testPhysiologyToxinBinding proteinProteolysisPeptideGeneral MedicineTrifluoperazineBiologymedicine.disease_causebiology.organism_classificationBiochemistryMolecular biologychemistryBiochemistryInsect ScienceBacillus thuringiensismedicinebiology.proteinBinding sitemedicine.drugArchives of Insect Biochemistry and Physiology
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