Search results for "proteinas"

showing 10 items of 416 documents

Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics

2015

Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we present an in vitro and in silico characterization of native neuroserpin and its dysfunctional conformation isoforms: the proteolytically cleaved conformer, the inactive latent conformer, and the polymeric species. Based on circular dichroism and fluorescence spectroscopy, we present an experimental validation of the latent model and highlight the main structural features of the different conformers. In particular, emission spectra of aromatic res…

Protein FoldingCircular dichroismSerine Proteinase InhibitorsProtein ConformationStereochemistryNeuroserpinBiophysicsEpilepsies MyoclonicMolecular Dynamics SimulationSerpinMolecular DynamicsBiochemistryProtein Structure SecondaryArticleFluorescenceAnalytical ChemistryMolecular dynamicsProtein structureNeuroserpinmedicineHumansProtein IsoformsFluorescence emission spectra; circular dichroism; neuroserpin latent conformationneuroserpin latent conformationFamilial encephalopathy with neuroserpin inclusion bodiesMolecular BiologyConformational isomerismSerpinsFluorescence emission spectraSerpinChemistryCircular DichroismConformational diseaseNeuropeptidesHydrogen Bondingmedicine.diseaseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Heredodegenerative Disorders Nervous SystemProtein foldingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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The production of 85 kDa N-terminal fragment of apolipoprotein B in mutant HepG2 cells generated by targeted modification of apoB gene occurs by ALLN…

2010

Abstract To study the mechanism of low levels of full length and truncated apoB in individuals heterozygous for apoB truncation, a non-sense mutation was introduced in one of the three alleles of apob gene of HepG2 cells by homologous recombination. Despite very low levels of apoB-82 (1–2%) in the media, a prominent N-terminal apoB protein of 85 kDa (apoB-15) was secreted that fractionated at d > 1.065 in density gradient ultracentrifugation. The mechanism of production of this short protein was studied by 35S-methionine pulse–chase experiment. Oleate prevented presecretory degradation of apoB-100 in the cell and resulted in increased secretion of newly synthesized apoB-100 with decreases i…

Protein FoldingHepG2Apolipoprotein BLeupeptinsmedicine.medical_treatmentMutantBiophysicsBiologyCysteine Proteinase Inhibitorsdigestive systemBiochemistry85 kDa N-terminalCysteine ProteasesapoBmedicineHumansSecretionMolecular BiologyApolipoproteins BProteasenutritional and metabolic diseasesCell BiologyHep G2 CellsCysteine proteaseMolecular biologyTransmembrane proteinProtein TransportCodon NonsenseHypobetalipoproteinemia Familial Apolipoprotein Bbiology.proteinlipids (amino acids peptides and proteins)Density gradient ultracentrifugationIntracellular
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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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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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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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Integrated multi-omics investigations of metalloproteinases in colon cancer: Focus on MMP2 and MMP9

2021

Colorectal cancer (CRC) develops by genetic and epigenetic alterations. However, the molecular mechanisms underlying metastatic dissemination remain unclear and could benefit from multi-omics investigations of specific protein families. Matrix metalloproteinases (MMPs) are proteolytic enzymes involved in ECM remodeling and the processing of bioactive molecules. Increased MMP expression promotes the hallmarks of tumor progression, including angiogenesis, invasion, and metastasis, and is correlated with a shortened survival. Nevertheless, the collective role and the possible coordination of MMP members in CRC are poorly investigated. Here, we performed a multi-omics analysis of MMP expression…

ProteomicsMMP2Epithelial-Mesenchymal TransitionQH301-705.5Colorectal cancerBioinformaticsKaplan-Meier EstimateBiologyMatrix metalloproteinaseMMP9ArticleCatalysisEpigenesis GeneticMetastasisCohort StudiesInorganic ChemistryLymphocytes Tumor-InfiltratingmedicineHumansEpithelial–mesenchymal transitionBiology (General)Physical and Theoretical ChemistrySettore BIO/06 - Anatomia Comparata E CitologiaQD1-999Molecular BiologySpectroscopyTissue Inhibitor of Metalloproteinase-2Functional analysisMMP9Organic ChemistryProteolytic enzymesGeneral Medicinemedicine.diseasePrognosisComputer Science ApplicationsColon cancerExtracellular MatrixGene Expression Regulation NeoplasticChemistryMatrix metalloproteinasesMatrix Metalloproteinase 9Tumor progressionCase-Control StudiesColonic NeoplasmsCancer researchMatrix Metalloproteinase 2Gene expressionMMP2
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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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