Search results for "Peptidases"

showing 10 items of 319 documents

Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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Bioinformatic flowchart and database to investigate the origins and diversity of Clan AA peptidases

2009

Abstract Background Clan AA of aspartic peptidases relates the family of pepsin monomers evolutionarily with all dimeric peptidases encoded by eukaryotic LTR retroelements. Recent findings describing various pools of single-domain nonviral host peptidases, in prokaryotes and eukaryotes, indicate that the diversity of clan AA is larger than previously thought. The ensuing approach to investigate this enzyme group is by studying its phylogeny. However, clan AA is a difficult case to study due to the low similarity and different rates of evolution. This work is an ongoing attempt to investigate the different clan AA families to understand the cause of their diversity. Results In this paper, we…

Protein familySequence analysisImmunologyProtein domainMolecular Sequence DataBiologycomputer.software_genreGeneral Biochemistry Genetics and Molecular BiologyProtein Structure SecondaryPhylogeneticsSequence Analysis ProteinSoftware DesignConsensus SequenceConsensus sequenceAspartic Acid EndopeptidasesClanAmino Acid SequenceDatabases ProteinPeptide sequencelcsh:QH301-705.5Ecology Evolution Behavior and SystematicsPhylogenyDatabaseAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)Applied MathematicsResearchComputational BiologyGenetic VariationGene AnnotationTemplates GeneticMarkov ChainsProtein Structure Tertiarylcsh:Biology (General)Modeling and SimulationGeneral Agricultural and Biological SciencescomputerBiology Direct
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Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 t…

2010

Abstract The metalloproteases meprin α and β are expressed in several tissues, leukocytes, and cancer cells. In skin, meprins are located in separate layers of human epidermis indicating distinct physiological functions, supported by effects on cultured keratinocytes. Meprin β induces a dramatic change in cell morphology and a significant reduction in cell number, whereas in vitro evidence suggests a role for meprin α in basal keratinocyte proliferation. Meprins are secreted as zymogens that are activated by tryptic proteolytical processing. Here, we identify human kallikrein-related peptidases (KLKs) 4, 5, and 8 to be specific activators of meprins. KLK5 is capable of activating both metal…

Proteolysismedicine.medical_treatmentClinical BiochemistryBiologyBiochemistrySubstrate SpecificitymedicineHumansAmino Acid SequenceProtein precursorMolecular BiologySkinSerine proteaseEnzyme PrecursorsMetalloproteinaseProteasemedicine.diagnostic_testMetalloendopeptidasesKLK5Trypsinddc:Enzyme Activationmedicine.anatomical_structureBiochemistrybiology.proteinKallikreinsKeratinocytemedicine.drug
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Bioassays to monitor taspase1 function for the identification of pharmacogenetic inhibitors

2011

Background Threonine Aspartase 1 (Taspase1) mediates cleavage of the mixed lineage leukemia (MLL) protein and leukemia provoking MLL-fusions. In contrast to other proteases, the understanding of Taspase1's (patho)biological relevance and function is limited, since neither small molecule inhibitors nor cell based functional assays for Taspase1 are currently available. Methodology/Findings Efficient cell-based assays to probe Taspase1 function in vivo are presented here. These are composed of glutathione S-transferase, autofluorescent protein variants, Taspase1 cleavage sites and rational combinations of nuclear import and export signals. The biosensors localize predominantly to the cytoplasm…

ProteomicsCytoplasmHydrolasesmedicine.medical_treatmentThreonine Aspartase 1Drug Evaluation Preclinicallcsh:MedicineBiosensing TechniquesBiochemistryMiceMolecular Cell BiologyBasic Cancer Researchlcsh:ScienceMultidisciplinaryEnzyme ClassesProteomic Databases3T3 CellsSmall moleculeCellular StructuresEnzymesBiochemistryOncologyMedicineBiological AssayBiologieResearch ArticleProteasesCell SurvivalIn silicoBiologyCleavage (embryo)In vivoGenetic Mutationddc:570EndopeptidasesChemical BiologyConsensus sequencemedicineGeneticsAnimalsHumansProtease InhibitorsBiologyCell NucleusProteaselcsh:RProteinsPharmacogeneticsSmall MoleculesMutagenesislcsh:Q
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The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species

2012

The amyloid β (Aβ) peptide, which is abundantly found in the brains of patients suffering from Alzheimer disease, is central in the pathogenesis of this disease. Therefore, to understand the processing of the amyloid precursor protein (APP) is of critical importance. Recently, we demonstrated that the metalloprotease meprin β cleaves APP and liberates soluble N-terminal APP (N-APP) fragments. In this work, we present evidence that meprin β can also process APP in a manner reminiscent of β-secretase. We identified cleavage sites of meprin β in the amyloid β sequence of the wild type and Swedish mutant of APP at positions p1 and p2, thereby generating Aβ variants starting at the first or seco…

ProteomicsMolecular Sequence DataMutantPeptideBiologyHydroxamic AcidsCleavage (embryo)BiochemistryCatalysis03 medical and health sciences0302 clinical medicineAlzheimer Diseasemental disordersmedicineAmyloid precursor proteinHumansProtein IsoformsAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMetalloproteinaseAmyloid beta-PeptidesWild typeBrainMetalloendopeptidasesMolecular Bases of DiseaseCell Biologymedicine.diseaseMolecular biologyProtein Structure TertiaryKineticsHEK293 CellsEnzymechemistryBiochemistryMutationMetalloproteasesbiology.proteinAmyloid Precursor Protein SecretasesAlzheimer's diseasePeptides030217 neurology & neurosurgeryJournal of Biological Chemistry
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The Wnt-specific astacin proteinase HAS-7 restricts head organizer formation in Hydra

2021

Abstract Background The Hydra head organizer acts as a signaling center that initiates and maintains the primary body axis in steady state polyps and during budding or regeneration. Wnt/beta-Catenin signaling functions as a primary cue controlling this process, but how Wnt ligand activity is locally restricted at the protein level is poorly understood. Here we report a proteomic analysis of Hydra head tissue leading to the identification of an astacin family proteinase as a Wnt processing factor. Results Hydra astacin-7 (HAS-7) is expressed from gland cells as an apical-distal gradient in the body column, peaking close beneath the tentacle zone. HAS-7 siRNA knockdown abrogates HyWnt3 proteo…

ProteomicsPhysiologyHydraQH301-705.5XenopusPlant ScienceProteinaseGeneral Biochemistry Genetics and Molecular BiologyStructural BiologyAstacinAxis formationAnimalsRNA Small InterferingBiology (General)Wnt Signaling PathwayEcology Evolution Behavior and SystematicsActinbeta CateninBody PatterningGene knockdownBuddingbiologyRegeneration (biology)Wnt signaling pathwayMetalloendopeptidasesCell Biologybiology.organism_classificationWnt signalingCell biologyWnt ProteinsProteolysisLernaean HydraAstacinGeneral Agricultural and Biological SciencesHeadDevelopmental BiologyBiotechnologyResearch ArticleBMC Biology
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Proteomics of Galápagos Marine Iguanas Links Function of Femoral Gland Proteins to the Immune System

2020

Femoral glands secrete a wax-like substance on the inner side of lizard hind legs, which is thought to function as a mode of chemical communication. Though the minor volatile fraction is well studied, the major protein fraction remains enigmatic. Here, we use proteomics to analyze proteins in femoral gland secretions of the Galápagos marine iguana. Although we found no evidence for proteins and peptides involved in chemical communication, we found several immune-regulatory proteins which also demonstrate anti-microbial functions. Accordingly, we show that femoral gland proteins and peptides function as a barrier against microbial infection and may prevent the rapid degradation of volatile s…

ProteomicsProteomeProteomicsBiochemistryAnalytical ChemistryAnti-Infective AgentsTandem Mass Spectrometrydatabase designprotease inhibitor protein identificationLungSkin0303 health sciencesMuscles030302 biochemistry & molecular biologyBrainHigh-Throughput Nucleotide SequencingHeartBlood proteinsanimal modelsmarine iguanaBiochemistryOrgan SpecificityProteomeEcuadorBacillus subtilisPulmonary Surfactant-Associated ProteinsGalectinsAntileukoproteinaseBiologyprotease inhibitor03 medical and health sciencesproteomicsImmune systemfemoral glandsevolutionEndopeptidasesEscherichia coliAnimalsHumanstissuesMolecular Biology030304 developmental biologyGalectinInnate immune systemChemotactic FactorsResearchMyocardiumImmunity Innateimmune systemIguanasMuramidaseApoproteinsTranscriptomeFunction (biology)Molecular & Cellular Proteomics
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The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

2012

The in vivo roles of meprin metalloproteases in pathophysiological conditions remain elusive. Substrates define protease roles. Therefore, to identify natural substrates for human meprin α and β we employed TAILS (terminal amine isotopic labeling of substrates), a proteomics approach that enriches for N-terminal peptides of proteins and cleavage fragments. Of the 151 new extracellular substrates we identified, it was notable that ADAM10 (a disintegrin and metalloprotease domain-containing protein 10)—the constitutive α-secretase—is activated by meprin β through cleavage of the propeptide. To validate this cleavage event, we expressed recombinant proADAM10 and after preincubation with meprin…

Proteomicsalpha-2-HS-Glycoproteinmedicine.medical_treatmentADAM10ADAM10 ProteinMice0302 clinical medicine610 Medicine & healthMice KnockoutExtracellular Matrix Proteins0303 health sciencesMetalloproteinaseDegradomeMetalloendopeptidasesMeprinADAM10Terminal amine isotopic labeling of substratesADAM ProteinsElafinBiochemistryTAILSCytokinesMolecular MedicineElafinResearch Article610 Medicine & healthBiologyCell Line03 medical and health sciencesCellular and Molecular NeurosciencemedicineDisintegrinAnimalsHumansAmino Acid SequenceCystatin CMolecular Biology030304 developmental biologyPharmacologyProteaseMeprin; ADAM10; Metalloproteases; Proteomics; TAILS; DegradomeMembrane ProteinsCell BiologyADAM ProteinsHEK293 CellsMembrane proteinbiology.proteinMetalloproteases570 Life sciences; biologyAmyloid Precursor Protein SecretasesCaco-2 Cells030217 neurology & neurosurgery
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Reelin and CXCL12 regulate distinct migratory behaviors during the development of the dopaminergic system.

2014

The proper functioning of the dopaminergic system requires the coordinated formation of projections extending from dopaminergic neurons in the substantia nigra (SN), ventral tegmental area (VTA) and retrorubral field to a wide array of forebrain targets including the striatum, nucleus accumbens and prefrontal cortex. The mechanisms controlling the assembly of these distinct dopaminergic cell clusters are not well understood. Here, we have investigated in detail the migratory behavior of dopaminergic neurons giving rise to either the SN or the medial VTA using genetic inducible fate mapping, ultramicroscopy, time-lapse imaging, slice culture and analysis of mouse mutants. We demonstrate that…

Receptors CXCR4Cell Adhesion Molecules NeuronalDopamineEmbryonic DevelopmentSubstantia nigraNerve Tissue ProteinsStriatumBiologyNucleus accumbensLigandsModels BiologicalTime-Lapse ImagingMiceCell MovementDopaminergic CellmedicineAnimalsCell LineageReelinMolecular BiologyMice KnockoutExtracellular Matrix ProteinsDopaminergic NeuronsDopaminergicSerine EndopeptidasesVentral Tegmental AreaAnatomyChemokine CXCL12Ventral tegmental areaSubstantia NigraReelin Proteinmedicine.anatomical_structurenervous systemForebrainbiology.proteinNeuroscienceDevelopmental BiologySignal TransductionDevelopment (Cambridge, England)
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Pre- and Post-translational Regulation of Lysyl Oxidase by Transforming Growth Factor-β1 in Osteoblastic MC3T3-E1 Cells

1995

The final enzymatic step required for collagen cross-linking is the extracellular oxidative deamination of peptidyl-lysine and -hydroxylysine residues by lysyl oxidase. A cross-linked collagenous extracellular matrix is required for bone formation. The goals of this study were to compare the transforming growth factor (TGF)-beta 1 regulation of lysyl oxidase enzyme activity and steady state mRNA levels to changes in COL1A1 mRNA levels in MC3T3-E1 osteoblastic cells. TGF-beta 1 increased steady state lysyl oxidase and COL1A1 mRNA levels in a dose- and time-dependent manner. The increase in lysyl oxidase mRNA levels was transient, peaking at 12 h and 8.8 times controls in cells treated with 4…

Recombinant Fusion ProteinsLysyl oxidasemacromolecular substancesBiochemistryGene Expression Regulation EnzymologicProtein-Lysine 6-OxidaseExtracellular matrixMicechemistry.chemical_compoundTransforming Growth Factor betaEndopeptidasesTranslational regulationExtracellularAnimalsHumansRNA Messengerskin and connective tissue diseasesMolecular BiologyOsteoblastsintegumentary systembiologyOxidative deamination3T3 CellsCell BiologyMolecular biologyRecombinant ProteinsEnzyme assayKineticsHydroxylysinechemistrybiology.proteinElectrophoresis Polyacrylamide GelCollagenProtein Processing Post-TranslationalTransforming growth factorJournal of Biological Chemistry
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