Search results for "acrylamide"

showing 10 items of 485 documents

µ-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptos…

2011

Anti-apoptotic Bfl-1 and pro-apoptotic Bax, two members of the Bcl-2 family sharing a similar structural fold, are classically viewed as antagonist regulators of apoptosis. However, both proteins were reported to be death inducers following cleavage by the cysteine protease µ-calpain. Here we demonstrate that calpain-mediated cleavage of full-length Bfl-1 induces the release of C-terminal membrane active α-helices that are responsible for its conversion into a pro-apoptotic factor. A careful comparison of the different membrane-active regions present in the Bfl-1 truncated fragments with homologous domains of Bax show that helix α5, but not α6, of Bfl-1 induces cell death and cytochrome c r…

Programmed cell deathProtein StructureCancer Treatmentlcsh:MedicineApoptosisMitochondrionCleavage (embryo)BiochemistryProtein Structure SecondaryMinor Histocompatibility AntigensMiceCell Line TumorMolecular Cell BiologyAnimalsHumanslcsh:ScienceProtein InteractionsBiologyMultidisciplinaryMicroscopy ConfocalbiologyCell DeathCalpainCytochrome clcsh:RCytochromes cProteinsCalpainCysteine proteaseCell biologyMitochondriaProto-Oncogene Proteins c-bcl-2OncologyApoptosisbiology.proteinMedicinelcsh:QElectrophoresis Polyacrylamide GelGlobular ProteinsBCL2-related protein A1Research ArticlePloS one
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Macrophage-mediated clearance of cells undergoing caspase-3-independent death

2003

Little is known of the functions of caspases in mediating the surface changes required for phagocytosis of dying cells. Here we investigate the role played by the effector caspase, caspase-3 in this process using the caspase-3-defective MCF-7 breast carcinoma line and derived caspase-3-expressing transfectants. Our results indicate that, while certain typical features of apoptosis induced by etoposide - namely classical morphological changes and the ability to degrade DNA into oligonucleosomal fragments - are caspase-3-dependent, loss of cell adhesion to plastic and the capacity to interact with, and to be phagocytosed by, human monocyte-derived macrophages - both by CD14-dependent and CD14…

Programmed cell deathTime FactorsBlotting WesternGreen Fluorescent ProteinsLipopolysaccharide ReceptorsApoptosisCaspase 3PhosphatidylserinesDNA FragmentationTransfectionCaspase 7Proinflammatory cytokinePhagocytosisCell Line TumorSettore BIO/10 - BiochimicaHumansMacrophageAnnexin A5Cell adhesionCytokineMolecular BiologyCells CulturedCaspaseEtoposideCaspase 7InflammationCell DeathbiologyCaspase 3MacrophagesDNACell BiologyCaspaseCell biologyEnzyme ActivationLuminescent ProteinsApoptosisCaspasesbiology.proteinCytokinesElectrophoresis Polyacrylamide GelCell Death & Differentiation
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Secretion of haemolysins and proteases by Aeromonas hydrophila EO63: separation and characterization of the serine protease (caseinase) and the metal…

2004

C . E S T E V E A N D T . H . B I R K B E C K . 2004. Aims: To determine the haemolysins and proteases excreted by the virulent strain EO63 of Aeromonas hydrophila grown in complex media and to then fractionate and characterize them, in particular those with elastolytic activity. Methods and Results: The amount of haemolytic and proteolytic activity in EO63 culture supernatants was dependent on the culture media used. In all media, haemolysins appeared during the phase of active growth and haemolytic activity decreased quickly thereafter, as previously described for aerolysin. In contrast, proteases were mainly released during the stationary phase. Serine protease activity in EO63 culture s…

ProteasesAerolysinBiologyApplied Microbiology and BiotechnologyMicrobiologySerineHemolysin ProteinsCaseinaseEndopeptidasesSerine proteaseSerine EndopeptidasesElastaseCaseinsHemolysinGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationAeromonas hydrophilaCulture MediaElastinAeromonas hydrophilaBiochemistryMetalloproteasesbiology.proteinElectrophoresis Polyacrylamide GelIsoelectric FocusingBiotechnologyJournal of Applied Microbiology
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Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity

2008

International audience; Extracellular proteins from Oenococcus oeni. a wine-making bacterium, were isolated during growth on media differing by their nitrogen content. Analysis by two-dimensional electrophoresis revealed a low number of protein signals. Among the main spots, one signal corresponded to a single protein, which contained a lysine repeat domain characteristic of cell-wall hydrolases. We demonstrated that this major protein, named EprA, was able to hydrolyse several proteins. The heterologous production of this protein in Escherichia coli confirmed the protease activity of EprA. With a MW of 21.3 kDa and a pl of 5.3, EprA presents optimal activity at pH 7.0 and 45 degrees C. Thi…

ProteasesHydrolyzed proteinNitrogenmedicine.medical_treatmentWinemedicine.disease_causeMicrobiology[ CHIM ] Chemical SciencesMicrobiology03 medical and health sciencesBacterial Proteinsmedicine[CHIM]Chemical SciencesElectrophoresis Gel Two-DimensionalPolyacrylamide gel electrophoresisEscherichia coli030304 developmental biologyOenococcus oenichemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyTemperatureGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationCulture MediaMolecular WeightEnzymeBiochemistrychemistryFermentationFood MicrobiologyElectrophoresis Polyacrylamide GelOenococcusLeuconostocFood SciencePeptide Hydrolases
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The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen I provides a quantitative explanation for functional diffe…

2006

The procollagen C-proteinase (PCP) is a zinc peptidase of the astacin family and the metzincin superfamily. The enzyme removes the C-terminal propeptides of fibrillar procollagens and activates other matrix proteins. Besides its catalytic protease domain, the procollagen C-proteinase contains several C-terminal CUB modules (named after complement factors C1r and C1s, the sea urchin UEGF protein, and BMP-1) and EGF-like domains. The two major splice forms of the C-proteinase differ in their overall domain composition. The longer variant, termed mammalian tolloid (mTld, i.e., PCP-2), has the protease- CUB1-CUB2-EGF1-CUB3-EGF2-CUB4-CUB5 composition, whereas the shorter form termed bone morphog…

ProteasesProtein FoldingTolloid-Like Metalloproteinasesmedicine.medical_treatmentRNA SplicingBiologyAntiparallel (biochemistry)BiochemistryBone morphogenetic protein 1law.inventionBone Morphogenetic Protein 1lawmedicineAnimalsProtein precursorDNA PrimersProteaseBase SequenceCircular DichroismMetalloendopeptidasesSurface Plasmon ResonanceRecombinant ProteinsProcollagen peptidaseSpectrometry FluorescenceBiochemistryBone Morphogenetic ProteinsRecombinant DNAMetalloproteasesElectrophoresis Polyacrylamide GelAstacinProcollagenBiochemistry
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Crystallization and preliminary X-ray studies of oligandrin, a sterol-carrier elicitor fromPythium oligandrum

2000

Oligandrin is a 10 kDa acidic protein produced by the fungus micromycete Pythium oligandrum and is a member of the alpha-elicitin group, with sterol- and lipid-carrier properties. Oligandrin has been crystallized at 290 K using PEG 4000 as a precipitant. A cholesterol complex was obtained under the same conditions. The space group of the crystals at low temperature (100 K) is C222, with unit-cell parameters a = 94.0, b = 171.1, c = 55.3 A. Four molecules are present in the asymmetric unit. Data from the free and cholesterol-complexed forms were recorded at synchrotron sources to resolutions of 2.4 (uncomplexed) and 1.9 A (complexed), respectively.

Protein ConformationPythiumElicitinGeneral MedicineBiologyCrystallography X-Raybiology.organism_classificationSterolElicitorlaw.inventionFungal ProteinsSterolsCrystallographyCholesterolSterol carrier proteinStructural BiologylawPEG ratioIntercellular Signaling Peptides and ProteinsMoleculeElectrophoresis Polyacrylamide GelCrystallizationCarrier ProteinsCrystallizationPythium oligandrumActa Crystallographica Section D Biological Crystallography
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Two amino acid residues determine the low substrate affinity of human cationic amino acid transporter-2A.

2003

Mammalian cationic amino acid transporters (CAT) differ in their substrate affinity and sensitivity to trans-stimulation. The apparent Km values for cationic amino acids and the sensitivity to trans-stimulation of CAT-1, -2B, and -3 are characteristic of system y+. In contrast, CAT-2A exhibits a 10-fold lower substrate affinity and is largely independent of substrate at the trans-side of the membrane. CAT-2A and -2B demonstrate such divergent transport properties, even though their amino acid sequences differ only in a stretch of 42 amino acids. Here, we identify two amino acid residues within this 42-amino acid domain of the human CAT-2A protein that are responsible for the apparent low af…

Protein ConformationRecombinant Fusion ProteinsBlotting WesternGreen Fluorescent ProteinsMolecular Sequence DataGene ExpressionArginineTransfectionBiochemistryStructure-Activity RelationshipXenopus laevisExtracellularAnimalsHumansBiotinylationAmino acid transporterAmino Acid SequenceAmino AcidsCationic Amino Acid Transporter 2Molecular BiologyGlutathione Transferasechemistry.chemical_classificationBinding SitesSubstrate (chemistry)Biological TransportCell BiologyPhoto-reactive amino acid analogAmino acidTransmembrane domainLuminescent ProteinsS-tagchemistryBiochemistryMutagenesis Site-DirectedOocytesElectrophoresis Polyacrylamide GelFemaleIntracellularThe Journal of biological chemistry
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Subunits composition and allosteric control in Carcinus aestuarii hemocyanin

1998

Carcinus aestuarii hemocyanin (Hc) exists in two aggregation forms at pH 7.5 and 20 mM Ca2+: 24S accounting for 90% of total hemocyanin and 16S accounting for 10%. Removal of metal cations by EDTA at neutral pH causes the complete dissociation of 24S hemocyanin into two different 16S. At pH 9.2, 24S hemocyanin dissociates into a pH stable 16S and a 5S component. The 5S component consists of three monomeric fractions named CaeSS1 (10%), CaeSS2 (50%) and CaeSS3 (40%); the latter fraction consisting of two isoforms. The fractions CaeSS1, CaeSS2 and CaeSS3 have been studied as far as their reassociation properties to form hexamers are concerned. We investigated the oxygen-binding properties of …

Protein ConformationStereochemistrymedicine.medical_treatmentProtein subunitAllosteric regulationHemocyaninBiochemistryAllosteric interactionchemistry.chemical_compoundProtein structureOxygen bindingAllosteric RegulationCrustaceaMetalloproteinsmedicineMetalloproteinAnimalschemistry.chemical_classificationHemocyanin; Oxygen binding; Allosteric interaction; OxygenbiologyHemocyaninHydrogen-Ion Concentrationbiology.organism_classificationOxygenCarcinus aestuariiMonomerBiochemistrychemistryHemocyaninsChromatography GelElectrophoresis Polyacrylamide GelOxygen bindingProtein Binding
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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

2005

AbstractThe principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix–helix association and/or d…

Protein FoldingRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataBiophysicsBiochemistryMicelleHydrophobic mismatchHydrophobic mismatchStructural BiologyLeucineHelix packingGeneticsGlycophorinAnimalsHumansAmino Acid SequenceGlycophorinsMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationbiologyChemistryGlycophorin AProteïnes de membranaMembrane ProteinsMembrane protein associationCell BiologyTransmembrane proteinAmino acidTransmembrane domainBiochemistryMembrane proteinMutationTransmembrane helixBiophysicsbiology.proteinPeptidesDimerizationHydrophobic and Hydrophilic Interactions
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Metaproteomic analysis of atmospheric aerosol samples.

2016

Metaproteomic analysis of air particulate matter provides information about the abundance and properties of bioaerosols in the atmosphere and their influence on climate and public health. We developed and applied efficient methods for the extraction and analysis of proteins from glass fiber filter samples of total, coarse, and fine particulate matter. Size exclusion chromatography was applied to remove matrix components, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was applied for protein fractionation according to molecular size, followed by in-gel digestion and LC-MS/MS analysis of peptides using a hybrid Quadrupole-Orbitrap MS. Maxquant software and the Swiss-…

Proteomics010504 meteorology & atmospheric sciencesSize-exclusion chromatographyIndoor bioaerosolFractionation010501 environmental sciences01 natural sciencesBiochemistryAnalytical ChemistryMatrix (chemical analysis)Fungal ProteinsBacterial ProteinsMetaproteomicsTandem Mass SpectrometryDatabases ProteinChromatography High Pressure Liquid0105 earth and related environmental sciencesPlant ProteinsAerosolsFungal proteinAir PollutantsChromatographyMass spectrometryChemistryAtmosphereProteinsParticulatesAllergensAtmospheric aerosolsAerosolEnvironmental chemistryBioanalytical methodsParticleElectrophoresis Polyacrylamide GelParticulate MatterHPLCResearch PaperAnalytical and bioanalytical chemistry
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