Search results for "Recombinant protein"

showing 10 items of 707 documents

Autoantibody depletion ameliorates disease in murine experimental autoimmune encephalomyelitis.

2013

Much data support a role for central nervous system antigen-specific antibodies in the pathogenesis of multiple sclerosis (MS). The effects of inducing a decrease in (auto)antibody levels on MS or experimental autoimmune encephalomyelitis (EAE) through specific blockade of FcRn, however, remain unexplored. We recently developed engineered antibodies that lower endogenous IgG levels by competing for binding to FcRn. These Abdegs ("antibodies that enhance IgG degradation") can be used to directly assess the effect of decreased antibody levels in inflammatory diseases. In the current study, we show that Abdeg delivery ameliorates disease in an EAE model that is antibody dependent. Abdegs could…

Encephalomyelitis Autoimmune ExperimentalMultiple SclerosisShort CommunicationImmunologyCentral nervous systemCHO CellsReceptors FcBiologyProtein EngineeringImmunoglobulin GAntibodiesMyelin oligodendrocyte glycoproteinPathogenesisMiceCricetulusCricetinaemedicineImmunology and AllergyAnimalsHumansAutoantibodiesMultiple sclerosisExperimental autoimmune encephalomyelitisHistocompatibility Antigens Class IAutoantibodymedicine.diseaseRecombinant ProteinsMice Inbred C57BLmedicine.anatomical_structureImmunoglobulin GImmunologybiology.proteinFemaleMyelin-Oligodendrocyte GlycoproteinAntibodyProtein BindingmAbs
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Improvement in Nuclear Entry and Transgene Expression of Baculoviruses by Disintegration of Microtubules in Human Hepatocytes

2005

ABSTRACT Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV), a potent virus for mammalian cell gene delivery, possesses an ability to transduce mammalian cells without viral replication. We examined the role of the cellular cytoskeleton in the cytoplasmic trafficking of viral particles toward the nucleus in human hepatic cells. Microscopic studies showed that capsids were found in the nucleus after either viral inoculation or cytoplasmic microinjection of nucleocapsids. The presence of microtubule (MT) depolymerizing agents caused the amount of nuclear capsids to increase. Overexpression of p50/dynamitin, an inhibitor of dynein-dependent endocytic trafficking from peripheral e…

EndosomeMicrotubule-associated proteinvirusesImmunologyEndocytic cycleGenetic VectorsActive Transport Cell NucleusGene ExpressionBiologyGene deliveryMicrobiologyMicrotubulesCell Linechemistry.chemical_compoundTransduction GeneticVirologyHumansNucleocapsidCytoskeletonDynactin Complexbeta-GalactosidaseMolecular biologyNucleopolyhedrovirusesRecombinant ProteinsVirus-Cell InteractionsNocodazoleMicroscopy ElectronViral replicationchemistryLac OperonCell cultureCytoplasmInsect ScienceHepatocytesMicrotubule-Associated Proteins
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Activation of gp 130 by IL-6/soluble IL-6 receptor induces neuronal differentiation

1998

Interleukin-6 (IL-6) on target cells binds to the specific IL-6 receptor (IL-6R) and subsequently induces homodimerization of the signal-transducing protein gp130. Cells which express gp130 but no IL-6R and which therefore do not respond to IL-6 can be stimulated by the complex of IL-6 and soluble IL-6R (slL-6R). Here we show that on rat pheochromocytoma cells (PC12), the combination of IL-6 and slL-6R but not IL-6 alone induces expression of c-fos, GAP-43 and neuron-specific enolase followed by neuron-specific differentiation and formation of a neuronal network. The differentiation was dose-and time-dependent and followed the same kinetics as nerve-growth factor (NGF)-induced differentiati…

EnolaseGene ExpressionBiologyBinding CompetitivePC12 CellsAntibodiesGAP-43 ProteinAntigens CDNeutralization TestsCytokine Receptor gp130NeuritesAnimalsHumansNerve Growth FactorsReceptorNeuronsMessenger RNAMembrane GlycoproteinsInterleukin-6General NeuroscienceCell DifferentiationGlycoprotein 130Receptors Interleukin-6Molecular biologyRecombinant ProteinsRatsCell biologySolubilitynervous systemTrk receptorInterleukin-6 receptorSignal transductionProto-Oncogene Proteins c-fosTyrosine kinaseEuropean Journal of Neuroscience
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Isolation of a Putative Hydroxyacyl Enzyme Intermediate of an Epoxide Hydrolase

1994

A putative covalent, alpha-hydroxyacyl intermediate was isolated by the brief exposure of murine soluble epoxide hydrolase to its substrate. The reaction was reversed by time and blocked by competitive inhibitors. The formation of the intermediate was dependent upon the concentration of the enzyme and was increased by incubation under acidic conditions. The structure of the intermediate was supported by microchemical methods.

Epoxide HydrolasesEpoxide hydrolase 2chemistry.chemical_classificationReaction mechanismStereochemistryAcylationBiophysicsSubstrate (chemistry)Cell BiologyReaction intermediateHydrogen-Ion ConcentrationTritiumBiochemistryRecombinant ProteinsKineticsMiceEnzymechemistryBiochemistryCovalent bondAnimalsHumansEpoxide hydrolaseMolecular BiologyIncubationBiochemical and Biophysical Research Communications
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Construction of an agglutination tool: recombinant Fab fragments biotinylated in vitro.

2009

The pComb3H vector system is used for constructing and panning recombinant antibody libraries. It allows for expression of monovalent Fab fragments, either on the surface of M13 phage, or in the form of soluble proteins secreted into the periplasmic space of bacteria. We constructed a modified pComb3H vector containing cDNA encoding for a 23-amino acid fragment of the Escherichia coli biotin carboxy carrier protein (BCCP), which is an acceptor sequence for biotinylation. The vector was used to express the Fab fragment recognizing human glycophorin A. The purified Fab fragment containing this biotin acceptor sequence was effectively biotinylated in vitro using biotin ligase (BirA). The speci…

ErythrocytesBlotting WesternBioengineeringlaw.inventionchemistry.chemical_compoundImmunoglobulin Fab FragmentsBiotinlawAgglutination TestsGlycophorinHumansBiotinylationGlycophorinsMolecular BiologybiologyChemistryHemagglutinationGeneral MedicinePeriplasmic spaceAvidinMolecular biologyPrimary and secondary antibodiesRecombinant ProteinsAgglutination (biology)BiochemistryBiotinylationbiology.proteinRecombinant DNAChromatography GelElectrophoresis Polyacrylamide GelBiotechnologyAvidinProtein BindingNew biotechnology
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Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin

2013

Pyolysin (PLO) belongs to the homologous family of the cholesterol- dependent cytolysins (CDCs), which bind to cell membranes containing cholesterol to form oligomeric pores of large size. The CDC monomer structure consists of 4 domains. Among these, the C-terminal domain 4 has been implicated in membrane binding of the monomer, while the subsequent processes of oligomerization and membrane insertion have primarily been assigned to other domains of the molecule. Recombinantly expressed or proteolytic fragments that span domain 4 of the CDCs streptolysin O and perfringolysin O bind to membranes but fail to oligomerize, and they inhibit the activity of the respective wild-type toxins. We repo…

ErythrocytesMembrane bindingCellprotein bindingBiochemistryoligomerHemolysin Proteinschemistry.chemical_compoundReaction kineticsToxic materialsMonomersprotein domainRecombinant ProteinsHemolysisunclassified drugcytolysinmedicine.anatomical_structureMembraneBiochemistryStreptolysinsStreptolysinLarge sizeBacterial ToxinsBiologyCholesterol-dependent cytolysinHemolysisoligomerizationMembrane LipidsBacterial ProteinsProteolytic fragmentsEscherichia colimedicineAnimalsMonomer structuresMolecular BiologySheep Domesticcarboxy terminal sequenceC-terminal domainsCholesterolC-terminusCell MembraneHemolytic activitycholesterolCell Biologymedicine.diseaseProtein Structure TertiaryCell membranesKineticschemistryOligomersProtein MultimerizationPyolysinprotein pyolysinMembrane insertionCytology
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Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells.

1997

Staphylococcal α-toxin is a 293-residue, single-chain polypeptide that spontaneously assembles into a heptameric pore in target cell membranes. To identify the pore-forming domain, substitution mutants have been produced in which single cysteine residues were introduced throughout the toxin molecule. By attaching the environmentally sensitive dye acrylodan to the sulfhydryl groups, the environment of individual amino acid side chains could be probed. In liposomes, a single 23-amino acid sequence (residues 118–140) was found to move from a polar to a nonpolar environment, indicating that this sequence forms the walls of the pore. However, periodicity in side chain environmental polarity coul…

ErythrocytesNeutrophilsStaphylococcusT-LymphocytesBacterial ToxinsLipid BilayersBiologyHemolysin ProteinsCell membraneHemolysin ProteinsAdenosine TriphosphatePhagocytosismedicineAnimalsHumansCysteineLipid bilayerchemistry.chemical_classificationLiposomeMultidisciplinaryCell MembraneBiological SciencesFlow CytometryTransmembrane proteinRecombinant ProteinsAmino acidmedicine.anatomical_structureBeta barrelchemistryBiochemistryAmino Acid SubstitutionMutagenesis Site-DirectedPotassiumRabbitsCysteine
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Ofd1, a Human Disease Gene, Regulates the Length and Distal Structure of Centrioles

2010

SUMMARYCentrosomes and their component centrioles represent the principal microtubule organizing centers of animal cells. Here we show that the gene underlying Orofaciodigital Syndrome 1, Ofd1, is a component of the distal centriole that controls centriole length. In the absence of Ofd1, distal regions of centrioles, but not procentrioles, elongate abnormally. These long centrioles are structurally similar to normal centrioles, but contain destabilized microtubules with abnormal post-translational modifications. Ofd1 is also important for centriole distal appendage formation and centriolar recruitment of the intraflagellar transport protein Ift88. To model OFD1 Syndrome in embryonic stem ce…

G2 PhaseCentrioleMicrotubule-associated proteinMutation MissenseHUMDISEASECell Cycle ProteinsBiologyMicrotubulesModels BiologicalArticleGeneral Biochemistry Genetics and Molecular BiologyCentriole elongationCell LineMiceIntraflagellar transportCiliogenesisAnimalsHumansBasal bodyMolecular BiologyEmbryonic Stem CellsCentriolesTumor Suppressor ProteinsProteinsCell BiologyOrofaciodigital SyndromesPhosphoproteinsRecombinant ProteinsCell biologyCentrosomeCELLBIOCentriolar satelliteMicrotubule-Associated ProteinsDevelopmental Biology
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The Cell Cycle-Specific Growth-Inhibitory Factor Produced by Actinobacillus actinomycetemcomitans Is a Cytolethal Distending Toxin

1998

ABSTRACT Actinobacillus actinomycetemcomitans has been shown to produce a soluble cytotoxic factor(s) distinct from leukotoxin. We have identified in A. actinomycetemcomitans Y4 a cluster of genes encoding a cytolethal distending toxin (CDT). This new member of the CDT family is similar to the CDT produced by Haemophilus ducreyi . The CDT from A. actinomycetemcomitans was produced in Escherichia coli and was able to induce cell distension, growth arrest in G 2 /M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. The three proteins, CDTA, -B and -C, encoded by the cdt locus were all required for toxin activity. Antiserum raised against recombinant CDTC completely inhibited …

G2 PhaseCytolethal distending toxin[SDV]Life Sciences [q-bio]Bacterial ToxinsMolecular Sequence DataRestriction MappingImmunologyMitosismedicine.disease_causeAggregatibacter actinomycetemcomitansMicrobiologyVirulence factorMicrobiologyEscherichia colimedicineHumansAmino Acid SequenceCloning MolecularEscherichia coliBase SequencebiologyToxinACTIVITEAggregatibacter actinomycetemcomitansGENETIQUECell cyclebiology.organism_classificationGrowth InhibitorsRecombinant Proteins[SDV] Life Sciences [q-bio]Infectious DiseasesGenes BacterialMultigene FamilyActinobacillusMolecular and Cellular PathogenesisParasitologyHaemophilus ducreyiHeLa CellsInfection and Immunity
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Binding and/or hydrolysis of purine‐based nucleotides is not required for IM30 ring formation

2021

IM30, the inner membrane-associated protein of 30 kDa, is conserved in cyanobacteria and chloroplasts. Although its exact physiological function is still mysterious, IM30 is clearly essential for thylakoid membrane biogenesis and/or dynamics. Recently, a cryptic IM30 GTPase activity has been reported, albeit thus far no physiological function has been attributed to this. Yet, it is still possible that GTP binding/hydrolysis affects formation of the prototypical large homo-oligomeric IM30 ring and rod structures. Here, we show that the Synechocystis sp. PCC 6803 IM30 protein in fact is an NTPase that hydrolyzes GTP and ATP, but not CTP or UTP, with about identical rates. While IM30 forms lar…

GTP'Genetic VectorsBiophysicsGene ExpressionGTPaseRing (chemistry)ThylakoidsBiochemistrySubstrate Specificity03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsStructural BiologyEscherichia coliGeneticsNucleotideddc:610Cloning MolecularMolecular BiologyEnzyme Assays030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryHydrolysis030302 biochemistry & molecular biologySynechocystisSynechocystisMembrane ProteinsCell BiologyNucleoside-Triphosphatasebiology.organism_classificationRecombinant ProteinsKineticsMicroscopy ElectronThylakoidMembrane biogenesisBiophysicsGuanosine TriphosphateBiogenesisProtein BindingFEBS Letters
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