Search results for "recombinant"

showing 10 items of 1150 documents

Goodpasture antigen-binding protein, the kinase that phosphorylates the goodpasture antigen, is an alternatively spliced variant implicated in autoim…

2000

The non-collagenous C-terminal domain of the alpha(3) chain of collagen IV is the autoantigen in Goodpasture disease, an autoimmune disorder described only in humans. Specific N-terminal phosphorylation is a biological feature unique to the human domain when compared with other homologous domains lacking immunopathogenic potential. We have recently cloned from a HeLa-derived cDNA library a novel serine/threonine kinase (Goodpasture antigen-binding protein (GPBP)) that phosphorylates the N-terminal region of the human domain (Raya, A. Revert, F, Navarro, S. and Saus J. (1999) J. Biol. Chem. 274, 12642-12649). We show here that the pre-mRNA of GPBP is alternatively spliced in human tissues an…

Gene isoformCollagen Type IVMolecular Sequence DataBiologyProtein Serine-Threonine KinasesBiochemistryAutoantigensSerinePathogenesisTwo-Hybrid System TechniquesHumansAmino Acid SequencePhosphorylationMolecular BiologyCeramide Transfer ProteinBase SequenceKinasecDNA libraryCell BiologyDNACeramide transportMolecular biologyRecombinant ProteinsAlternative SplicingBiochemistryPhosphorylationCollagenThe Journal of biological chemistry
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An altered intracellular distribution of the autoantigen La/SS-B when translated from a La mRNA isoform.

1997

Abstract Transcription of the gene encoding for the nuclear autoantigen La resulted in La mRNA isoforms. A promoter switching combined with an alternative splicing pathway replaced exon 1 with exon 1′. Similar to mRNAs encoding for ribosomal proteins, exon 1′ started with a pyrimidine-rich 5′-terminus. Moreover, exon 1′ contained 5′-GC-rich regions and an oligo(U)-tail of 23 uridine residues. Exon 1′ encoded for three open reading frames upstream of the La protein reading frame. In spite of this unusual structure, exon 1′ La mRNAs were translated not only in vitro but also in transiently transfected cells. The translational efficiency of exon 1′ La mRNA was about 14% of exon 1 La mRNA using…

Gene isoformCytoplasmTranslational efficiencyDNA RecombinantBiologyTransfectionAutoantigensCell LineExonMiceExon trappingAnimalsHumansRNA MessengerGeneCell NucleusMessenger RNACell-Free SystemAlternative splicingCell Biology3T3 CellsExonsMolecular biologyOpen reading frameAlternative SplicingRibonucleoproteinsProtein BiosynthesisRabbitsExperimental cell research
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The diversity of GABAA receptors. Pharmacological and electrophysiological properties of GABAA channel subtypes.

1998

The amino acid gamma-aminobutyric-acid (GABA) prevails in the CNS as an inhibitory neurotransmitter that mediates most of its effects through fast GABA-gated Cl(-)-channels (GABAAR). Molecular biology uncovered the complex subunit architecture of this receptor channel, in which a pentameric assembly derived from five of at least 17 mammalian subunits, grouped in the six classes alpha, beta, gamma, delta, sigma and epsilon, permits a vast number of putative receptor isoforms. The subunit composition of a particular receptor determines the specific effects of allosterical modulators of the GABAARs like benzodiazepines (BZs), barbiturates, steroids, some convulsants, polyvalent cations, and et…

Gene isoformMacromolecular SubstancesProtein ConformationProtein subunitNeuroscience (miscellaneous)LoreclezoleConvulsantsBiologyInhibitory postsynaptic potentialGABAA-rho receptorSubstrate SpecificityGABA AntagonistsCellular and Molecular NeuroscienceBenzodiazepinesMiceChloride ChannelsmedicineAnimalsHumansProtein IsoformsReceptorGABA Agonistsgamma-Aminobutyric AcidAnestheticsMice KnockoutBinding SitesIon TransportGABAA receptorReceptors GABA-ARecombinant ProteinsRatsElectrophysiologyNeurologyBiochemistryBarbituratesSteroidsHeterologous expressionIon Channel Gatingmedicine.drugMolecular neurobiology
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The b1 isoform of protocadherin-gamma (Pcdhgamma) interacts with the microtubule-destabilizing protein SCG10.

2004

Due to their structural characteristics and their diversity, the 22 members of the protocadherin-gamma (Pcdhgamma) family have been suggested to contribute to the establishment of specific connections in the nervous system. Here, we focus on a single isoform, Pcdhgamma-b1. Its expression is found in different brain regions and in developing spinal cord it is restricted to scattered cells, whereas all cells are labeled using an antibody that recognizes all Pcdhgamma isoforms. As a first step to understanding the signaling mechanisms downstream of Pcdhgamma, we identify the microtubule-destabilizing protein SCG10 as a cytoplasmic interactor for Pcdhgamma-b1 and other isoforms of the Pcdhgamma…

Gene isoformNervous systemSubfamilyRecombinant Fusion ProteinsBiophysicsTwo-hybridProtocadherinCadherin Related ProteinsBiologyBiochemistryMicrotubulesMiceProtocadherinStructural BiologyMicrotubuleTwo-Hybrid System TechniquesChlorocebus aethiopsGeneticsmedicineAnimalsProtein IsoformsInteractorNerve Growth FactorsGrowth coneMolecular BiologyNeuronsProtocadherin-gammaCalcium-Binding ProteinsIntracellular Signaling Peptides and ProteinsBrainCell BiologySCGIOCadherinsMolecular biologyCell biologySCG10medicine.anatomical_structureCytoplasmCOS CellsStathminGrowth coneSignal TransductionFEBS letters
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Identification and cloning of odorant binding proteins from the scarab beetle Phyllopertha diversa.

1999

Abstract Wehave identified, cloned, and characterized two odorant binding proteins from the pale brown chafer, Phyllopertha diversa. One of the proteins (OBP1, 116 amino acids long) showed high amino acid identity (>90%) to two previously identified PBPs from scarab beetles. The second protein (OBP2) showed limited sequence similarity to lepidopteran and dipteran OBPs, but contained only 133 amino acids. Both proteins showed the occurrence of six highly conserved cysteines; electrospray mass spectral data suggested they are all bound in three disulfide bonds. During purification, OBP2 separated into several isoforms; N-terminal amino acid sequencing and electrospray ionization mass spectrom…

Gene isoformOdorant bindingElectrospray ionization1Molecular Sequence DataBiophysicsPhyllopertha diversaReceptors Odorantelectrospray mass spectrometryBiochemistryBombykolbombykolpheromonechemistry.chemical_compoundconformational changeBombyx moriAnimalsAmino Acid SequenceCloning MolecularMolecular Biologychemistry.chemical_classificationCloningbiologySequence Homology Amino Acid3H)-quinazolinedionefungi3-dimethyl-2Cell Biologybiology.organism_classificationRecombinant ProteinsjaponilureAmino acidColeopteraMolecular WeightchemistryBiochemistryOdorantsPheromone4-(1HSequence AlignmentBiochemical and biophysical research communications
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Purification and Characterization of the Soluble Interleukin-6 Receptor from Human Plasma and Identification of An Isoform Generated through Alternat…

1996

The soluble human interleukin-6 receptor (shIL6R) was purified from human plasma. In a single immunoaffinity purification step a 140000-fold enrichment with a yield of 95% was achieved. A subsequent IL-6 affinity chromatography resulted in a homogeneous receptor preparation but only in a yield of less than 5%. The biological activity of the soluble receptor was clearly demonstrated by its ability to induce the synthesis of the acute-phase protein α1-antichymotrypsin in HepG2 cells stably transfected with IL-6. Upon gel filtration, the native shIL6R showed an apparent molecular mass of 93 kDa. Analysis by SDS/PAGE revealed an apparent molecular mass of 65 kDa for the soluble receptor. Deglyc…

Gene isoformPeptideBiologyTransfectionBiochemistryChromatography AffinityAmidohydrolasesCell LineAffinity chromatographyAntigens CDTumor Cells CulturedHumansPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseRNA MessengerReceptorPeptide sequencechemistry.chemical_classificationMolecular massInterleukin-6Cell MembraneAlternative splicingReceptors InterleukinReceptors Interleukin-6Molecular biologyRecombinant ProteinsMolecular WeightAlternative SplicingBiochemistrychemistryInterleukin-6 receptorChromatography GelElectrophoresis Polyacrylamide GelEuropean Journal of Biochemistry
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The Xenopus Oocyte as an Ectopic Expression System for the Selection of Protein Isoform-Specific Antibodies

1993

A panel of Xenopus oocytes, each injected with cRNA coding for one specific isoform of the rat brain RCK family of voltage gated potassium channel proteins, was employed to screen for isoform-specific monoclonal antibodies. Several days after injection, cryosections of embedded oocytes were produced and were employed in immunohistochemical analysis of antibody binding. Of the advantageous properties of the assay, it employs the native antigen, it can be applied to homooligomeric and heterooligomeric proteins, and cryosections of the same batch can be stored frozen for later tests. The method may be advantageous also for the selection of isoform-specific antibodies of other protein families.

Gene isoformProtein isoformPotassium ChannelsProtein familymedicine.drug_classRecombinant Fusion ProteinsXenopusNerve Tissue ProteinsBiologyMonoclonal antibodyEpitopeMiceXenopus laevisAntigenAntibody SpecificitymedicineAnimalsPharmacologyMice Inbred BALB CHybridomasAntibodies Monoclonalbiology.organism_classificationMolecular biologyOocytesFemaleEctopic expressionJournal of Receptor Research
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β1-Integrin Cytoplasmic Subdomains Involved in Dominant Negative Function

1998

The beta1-integrin cytoplasmic domain consists of a membrane proximal subdomain common to the four known isoforms ("common" region) and a distal subdomain specific for each isoform ("variable" region). To investigate in detail the role of these subdomains in integrin-dependent cellular functions, we used beta1A and beta1B isoforms as well as four mutants lacking the entire cytoplasmic domain (beta1TR), the variable region (beta1COM), or the common region (beta1 deltaCOM-B and beta1 deltaCOM-A). By expressing these constructs in Chinese hamster ovary and beta1 integrin-deficient GD25 cells (Wennerberg et al., J Cell Biol 132, 227-238, 1996), we show that beta1B, beta1COM, beta1 deltaCOM-B, a…

Gene isoformTalinCytoplasmProtein ConformationIntegrinMolecular Sequence DataCHO CellsIntegrin alpha5Platelet Membrane GlycoproteinsArticleFocal adhesionchemistry.chemical_compoundMiceAntigens CDCricetinaeCell AdhesionAnimalsActininAmino Acid SequencePhosphorylationCell adhesionMolecular BiologyBinding SitesbiologyCell adhesion moleculeChinese hamster ovary cellIntegrin beta1Integrin beta3Tyrosine phosphorylationCell BiologyIntegrin alphaVProtein-Tyrosine KinasesRecombinant ProteinsCell biologyFibronectinsFibronectinchemistryFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMutationbiology.proteinCell Adhesion MoleculesSignal Transduction
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Disassembly of structurally modified viral nanoparticles: characterization by fluorescence correlation spectroscopy.

2005

Abstract Analysis of the breakdown products of engineered viral particles can give useful information on the particle structure. We used various methods to breakdown both a recombinant enveloped virus and virus-like particles (VLPs) from two non-enveloped viruses and analysed the resulting subunits by fluorescence correlation spectroscopy (FCS). Analysis of the enveloped baculovirus, Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV), displaying the green fluorescent protein (GFP) fused to its envelope protein gp64 was performed in the presence and absence of 5 mM SDS and 25 mM DTT. Without treatment, the viral particle showed a diffusion time of 3.3 ms. In the presence of SDS…

General Immunology and MicrobiologyChemistryvirusesRecombinant Fusion ProteinsGreen Fluorescent ProteinsTrimerFluorescence correlation spectroscopyGeneral MedicineMothsSpodopteraFluorescenceMolecular biologyGeneral Biochemistry Genetics and Molecular BiologyGreen fluorescent proteinCell LineKineticsViral ProteinsVirus-like particleViral envelopeCapsidParticleAnimalsGeneral Agricultural and Biological SciencesBaculoviridaeComptes rendus biologies
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Baculoviral display of functional scFv and synthetic IgG-binding domains.

2000

Viral vectors displaying specific ligand binding moities such as scFv fragments or intact antibodies hold promise for the development of targeted gene therapy vectors. In this report we describe baculoviral vectors displaying either functional scFv fragments or the synthetic Z/ZZ IgG binding domain derived from protein A. Display on the baculovirus surface was achieved via fusion of the scFv fragment or Z/ZZ domain to the N-terminus of gp64, the major envelope protein of the Autographa californica nuclear polyhedrosis virus, AcNPV. As examples of scFv fragments we have used a murine scFv specific for the hapten 2-phenyloxazolone and a human scFv specific for carcinoembryonic antigen. In pri…

Genetic enhancementvirusesRecombinant Fusion ProteinsBlotting WesternBiophysicschemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayVectors in gene therapySpodopteraBiochemistryViral vector03 medical and health sciencesMice0302 clinical medicineAntibody SpecificityPeptide LibraryAnimalsHumansMolecular BiologyImmunoglobulin FragmentsCells Cultured030304 developmental biology0303 health sciencesbiologyOxazoloneNuclear Polyhedrosis VirusCell Biologyrespiratory systembiology.organism_classificationMolecular biology3. Good healthCarcinoembryonic AntigenAutographa californicaIgG binding030220 oncology & carcinogenesisImmunoglobulin Gbiology.proteinBinding Sites AntibodyAntibodyHaptenBaculoviridaeHaptensViral Fusion ProteinsBiochemical and biophysical research communications
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