Search results for "Precipitin Tests"

showing 10 items of 36 documents

Calcium-Dependent Assembly of Centrin-G-Protein Complex in Photoreceptor Cells

2002

Photoexcitation of rhodopsin activates a heterotrimeric G-protein cascade leading to cyclic GMP hydrolysis in vertebrate photoreceptors. Light-induced exchanges of the visual G-protein transducin between the outer and inner segment of rod photoreceptors occur through the narrow connecting cilium. Here we demonstrate that transducin colocalizes with the Ca(2+)-binding protein centrin 1 in a specific domain of this cilium. Coimmunoprecipitation, centrifugation, centrin overlay, size exclusion chromatography, and kinetic light-scattering experiments indicate that Ca(2+)-activated centrin 1 binds with high affinity and specificity to transducin. The assembly of centrin-G-protein complex is medi…

Lightgenetic structuresChromosomal Proteins Non-HistoneMacromolecular SubstancesImmunoprecipitationG proteinCentrifugationPlasma protein bindingBiologyRetinaSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinCalcium-binding proteinAnimalsScattering RadiationTransducinMicroscopy ImmunoelectronCell Growth and DevelopmentMolecular BiologyCalcium-Binding ProteinsCell BiologyHeterotrimeric GTP-Binding ProteinsPrecipitin TestsRatsCell biologyMice Inbred C57BLMolecular WeightRhodopsinCentrinChromatography Gelbiology.proteinCalciumCattlesense organsTransducinPhotoreceptor Cells VertebrateProtein BindingSignal TransductionMolecular and Cellular Biology
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alpha 11beta 1 integrin recognizes the GFOGER sequence in interstitial collagens.

2002

The integrins alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1) are referred to as a collagen receptor subgroup of the integrin family. Recently, both alpha(1)beta(1) and alpha(2)beta(1) integrins have been shown to recognize triple-helical GFOGER (where single letter amino acid nomenclature is used, O = hydroxyproline) or GFOGER-like motifs found in collagens, despite their distinct binding specificity for various collagen subtypes. In the present study we have investigated the mechanism whereby the latest member in the integrin family, alpha(11)beta(1), recognizes collagens using C2C12 cells transfected with alpha(11) cDNA and the bacterially expressed recombinant a…

Models MolecularIntegrinsDNA ComplementaryReceptors CollagenPhenylalanineIntegrinAmino Acid MotifsPlasma protein bindingBiochemistrylaw.inventionCollagen receptorMiceProtein structurelawCell AdhesionAnimalsHumansMagnesiumMolecular BiologyBinding selectivityCells Culturedchemistry.chemical_classificationbiologyDose-Response Relationship DrugCell BiologyPrecipitin TestsRecombinant ProteinsAmino acidProtein Structure TertiaryKineticschemistryBiochemistrybiology.proteinRecombinant DNACalciumCollagenPeptidesType I collagenProtein BindingThe Journal of biological chemistry
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Deletions in the hepatitis B virus small envelope protein: effect on assembly and secretion of surface antigen particles

1992

The small envelope S protein of hepatitis B virus carrying the surface antigen has the unique property of mobilizing cellular lipids into empty envelope particles which are secreted from mammalian cells. We studied the biogenesis of such particles using site-directed mutagenesis. In this study, we describe the effect of deletions in the N-terminal hydrophobic and hydrophilic domains of the S protein. Whereas short overlapping deletions of hydrophilic sequences flanking the first hydrophobic domain were tolerated, larger deletions of the same sequences were not. Conversely, the hydrophilic region preceding the second hydrophobic domain was not permissive for even short deletions. Deletion of…

Hepatitis B virusMolecular Sequence DataImmunologyMutantMutagenesis (molecular biology technique)Biologymedicine.disease_causeMicrobiologyViral Envelope ProteinsViral envelopeVirologymedicineInterleukin 9SecretionCloning MolecularCells CulturedSecretory pathwayMutationHepatitis B Surface AntigensBase SequenceTunicamycinEndoplasmic reticulumPrecipitin TestsMolecular biologyInsect ScienceMutagenesis Site-DirectedChromosome DeletionPlasmidsResearch ArticleJournal of Virology
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In vivo studies of altered expression patterns of p53 and proliferative control genes in chronic vitamin A deficiency and hypervitaminosis

2003

Several clinical trials have revealed that individuals who were given beta-carotene and vitamin A did not have a reduced risk of cancer compared to those given placebo; rather, vitamin A could actually have caused an adverse effect in the lungs of smokers [Omenn, G.S., Goodman, G.E., Thornquist, M.D., Balmes, J., Cullen, M.R., Glass, A., Keogh, J.P., Meyskens, F.L., Valanis, B., Williams, J.H., Barnhart, S. & Hammar, S. N. Engl. J. Med (1996) 334, 1150-1155; Hennekens, C.H., Buring, J.E., Manson, J.E., Stampfer, M., Rosner, B., Cook, N.R., Belanger, C., LaMotte, F., Gaziano, J.M., Ridker, P.M., Willet, W. & Peto, R. (1996) N. Engl. J. Med. 334, 1145-1149]. Using differential display techniq…

Cyclin-Dependent Kinase Inhibitor p21VitaminRetinyl Estersmedicine.medical_specialtyMacromolecular SubstancesProto-Oncogene Proteins c-junReceptors Retinoic AcidBlotting WesternRetinoic acidBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundIn vivoCyclinsInternal medicinemedicineAnimalsHypervitaminosis ARNA MessengerRats WistarVitamin AReceptorLungDifferential displayReverse Transcriptase Polymerase Chain ReactionVitamin A DeficiencyGene Expression ProfilingDNAmedicine.diseaseHypervitaminosisPrecipitin TestsRatsVitamin A deficiencyEndocrinologyGene Expression RegulationLiverchemistryChronic DiseaseImmunologyDiterpenesTumor Suppressor Protein p53CarcinogenesisCell DivisionEuropean Journal of Biochemistry
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Establishment of Polycomb silencing requires a transient interaction between PC and ESC

2001

Two distinct types of Polycomb complexes have been identified in flies and in vertebrates, one containing ESC and one containing PC. Using LexA fusions, we show that PC and ESC can establish silencing of a reporter gene but that each requires the presence of the other. In early embryonic extracts, we find PC transiently associated with ESC in a complex that includes EZ, PHO, PH, GAGA, and RPD3 but not PSC. In older embryos, PC is found in a complex including PH, PSC, GAGA, and RPD3, whereas ESC is in a separate complex including EZ, PHO, and RPD3.

Polycomb-Group ProteinsRepressorSettore BIO/11 - Biologia MolecolarePlasma protein bindingBiologyPolycomb silencingResearch CommunicationGeneticsPolycomb-group proteinsAnimalsDrosophila ProteinsGene silencingGene Silencingreproductive and urinary physiologyPolycomb Repressive Complex 1Reporter geneurogenital systemPolycomb Repressive Complex 2PcG complexEmbryoHistone-Lysine N-MethyltransferasePrecipitin TestsEmbryonic stem cellMolecular biologyRepressor Proteinsembryonic structuresInsect ProteinsDrosophilaRepressor lexAbiological phenomena cell phenomena and immunityESC/PHOProtein BindingDevelopmental BiologyGenes & Development
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Probing human beta1- and beta2 -adrenoceptors with domain-specific fusion protein antibodies.

1997

In order to generate antibodies suitable for immunological studies on beta-adrenoceptors constitutively expressed at low levels in cells or tissues we have produced fusion proteins of the amino- and carboxy-terminus, and the second extracellular loop of the human beta 1- or beta 2-adrenoceptors with bacterial glutathione-S-transferase in E. coli. Rabbit antibodies raised against these fusion proteins strongly reacted with intact human beta 1- or beta 2-adrenoceptors in a subtype- and domain-specific manner. Antibodies directed against the second extracellular loop of the beta 1-adrenoceptor reacted stronger with non-denatured receptors and decreased the affinity of the 3H-labelled antagonis…

Recombinant Fusion ProteinsBlotting WesternEnzyme-Linked Immunosorbent AssayBiologyImmunofluorescenceProtein Structure SecondaryAntibodiesRadioligand AssayAntibody SpecificitymedicineExtracellularAnimalsHumansAvidityReceptorFluorescent Antibody Technique IndirectPharmacologymedicine.diagnostic_testMolecular biologyFusion proteinPrimary and secondary antibodiesPrecipitin TestsBlotMicroscopy FluorescenceBiochemistrybiology.proteinRabbitsReceptors Adrenergic beta-2AntibodyReceptors Adrenergic beta-1European journal of pharmacology
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Increase in Bcl-2 phosphorylation and reduced levels of BH3-only Bcl-2 family proteins in kainic acid-mediated neuronal death in the rat brain.

2003

Kainic acid induces excitotoxicity and nerve cell degeneration in vulnerable regions of rat brain, most markedly in hippocampus and amygdala. Part of the cell death following kainic acid is apoptotic as shown by caspase 3 activation and chromatin condensation. Here we have studied the regulation of pro- and anti-apoptotic proteins belonging to the Bcl-2 family in rat hippocampus and amygdala by kainic acid in relationship to ensuing neuronal death. The pro-apoptotic protein Bax was up-regulated in hippocampus 6 h after kainic acid administration. The increase in Bax was followed by the appearance of TdT-mediated dUTP nick end labelling-positive cells which were prominent at 24 h. Immunohist…

MaleTime FactorsExcitotoxicityCell Countmedicine.disease_causeSettore BIO/09 - Fisiologiachemistry.chemical_compoundPrecipitin TestExcitatory Amino Acid AgonistsSerinePhosphorylationCells CulturedNuclear Proteinbcl-2-Associated X ProteinNeuronsProto-Oncogene ProteinKainic AcidbiologyCell DeathImmunochemistryGeneral NeuroscienceBrainNuclear ProteinsImmunohistochemistryProto-Oncogene Proteins c-bcl-2Programmed cell deathKainic acidTime FactorNeuronal deathExcitatory Amino Acid AgonistBlotting WesternCaspase 3HippocampuBcl-2-associated X proteinProto-Oncogene ProteinsGlial Fibrillary Acidic ProteinmedicineIn Situ Nick-End LabelingAnimalsRats WistarProtein kinase AStaining and LabelingAnimalBcl-2 familyNeuronButylated HydroxytolueneEmbryo MammalianMolecular biologyPrecipitin Testsnervous system diseasesRatsnervous systemchemistrybiology.proteinRatNeuNBcl-2 proteinThe European journal of neuroscience
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Characterization of Cop I Coat Proteins in Plant Cells

2000

Membrane traffic in eukaryotic cells is mediated by COP (coat protein)-coated vesicles. Their existence in plant cells has not yet been unequivocally demonstrated, although coated vesicles (probably with a COP coat) can be seen by electron microscopy. At the gene level, plant cells seem to contain all the components necessary to form COP-coated vesicles. In this paper, we have used antibodies raised against mammalian COPI coat proteins to detect putative homologues in rice (Oryza sativa) cells. Using these antibodies, we have found that rice cells contain alpha-, beta-, beta'-, and gamma-COP, as well as ADP-ribosylation factor (ARF) 1 protein. In addition, we show that antibodies against ma…

ImmunoprecipitationBlotting WesternBiophysicsCoated vesicleCross ReactionsBiologyCoatomer ProteinBiochemistryAntibodiesCytosolMicrosomesAnimalsMolecular BiologyVesiclefood and beveragesBiological TransportNeomycinOryzaCell BiologyCOPIPlant cellPrecipitin TestshumanitiesRatsCell biologyMolecular WeightCytosolLiverBiochemistryCoatomerbiology.proteinADP-Ribosylation Factor 1Guanosine TriphosphateAntibodyProtein BindingBiochemical and Biophysical Research Communications
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Hepatitis B Virus Large Envelope Protein Interacts with γ2-Adaptin, a Clathrin Adaptor-Related Protein

2001

ABSTRACT For the outcome of a hepatitis B virus (HBV) infection, the viral L envelope protein with its pre-S domain performs pivotal functions by mediating attachment of HBV to liver cells, envelopment of viral capsids, release of (sub)viral particles, regulation of supercoiled DNA amplification, and transcriptional transactivation. To assess its multiple functions and host-protein assistance involved, we initiated a two-hybrid screen using the L-specific pre-S1 domain as bait. With this approach, we have identified γ2-adaptin, a putative member of the clathrin adaptor proteins responsible for protein sorting and trafficking, as a specific binding partner of L protein. Evidence for a physic…

Hepatitis B virusVesicle-associated membrane protein 8ImmunoprecipitationImmunologyGolgi ApparatusTransfectionmedicine.disease_causeMicrobiologyClathrinChromatography AffinityCytosolViral Envelope ProteinsMutant proteinYeastsVirologyProtein targetingmedicineAnimalsBinding siteAdaptor Protein Complex gamma SubunitsBinding SitesbiologyMembrane ProteinsPrecipitin TestsClathrinTransmembrane proteinVirus-Cell InteractionsCell biologyInsect ScienceCOS CellsMutationbiology.proteinClathrin adaptor proteinsProtein BindingJournal of Virology
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Complete functional C1q deficiency associated with systemic lupus erythematosus (SLE).

1993

SUMMARY A complete functional deficiency of Clq is described in a patient suffering from SLE. From reduced plasma C1 activity of the parents a hereditary trait was assumed. The defective C1q molecule was haemolytically inactive, did not bind to immune complexes, and was not recognized by the monocyte C1q receptor. C1 activity in the patient's serum could be restored by the addition of purified C1q. Analysis by gelfiltration and ultracentrifugation experiments revealed an immunoreactive molecule of about 150 kD mol. wt, corresponding to one structural subunit of the C1q macromolccule, containing two A chain-B chain dimers and a C-C chain dimer. Applying Southern blot analysis with cDNA clone…

AdultProtein subunitImmunologychemical and pharmacologic phenomenaIn Vitro TechniquesMitochondrial Proteinsimmune system diseasesComplementary DNAmedicineImmunology and AllergyHumansLupus Erythematosus SystemicReceptorskin and connective tissue diseasesSouthern blotLupus erythematosusMembrane Glycoproteinsbusiness.industryMonocyteComplement C1qDNAComplement deficiencymedicine.diseasePrecipitin TestsReceptors ComplementMolecular Weightmedicine.anatomical_structureHyaluronan ReceptorsImmunologyFemaleRestriction fragment length polymorphismbusinessCarrier ProteinsPolymorphism Restriction Fragment LengthResearch Article
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