Search results for "Precipitin Tests"

showing 10 items of 36 documents

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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Kinin receptor status in normal and inflammed gastric mucosa

1997

No documented studies have been reported on the presence of B1 and B2 kinin receptors in the mammalian gastric mucosa. This first study aimed to immunolocalise sites of B1 and B2 kinin receptors in the human pyloric gastric mucosa and to evaluate its role in gastritis. Biopsies were obtained from patients with dyspepsia during endoscopic examination of the patient. The diagnosis and grading of the gastritis was performed on histological examination. Sections were immunostained for both B1 and B2 receptors using rabbit anti-human B1 and B2 kinin receptor antibodies. Control tissue was obtained from partial gastrectomy specimens, following surgical excision of the antrum for duodenal ulcers. …

AdultReceptor StatusPathologymedicine.medical_specialtyReceptor Bradykinin B2Molecular Sequence DataInflammationBiologyReceptor Bradykinin B1EpitheliumAntibody SpecificityGastroscopyPyloric AntrummedicineGastric mucosaAnimalsHumansAmino Acid SequenceDyspepsiaReceptorAntrumBradykinin Receptor AntagonistsPharmacologyReceptors BradykininBiopsy NeedleKininImmunohistochemistryPrecipitin TestsEpitheliummedicine.anatomical_structureGastric MucosaGastritisRabbitsmedicine.symptomGastritisFluorescein-5-isothiocyanateImmunopharmacology
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Embryonic neural cell adhesion molecules on human natural killer cells

1989

The neural cell adhesion molecules (NCAM) are surface glycoproteins that were first described in brain tissue. NCAM mediate adhesion in a variety of cell-cell interactions. In the present study we show that the so-called "embryonic" NCAM, i.e., the highly polysialylated forms of these proteins, are expressed on natural killer cells and some CD3+ cells in man. Homotypic binding of NCAM, believed to be of importance for cell-cell adhesion in neural tissues, appears not to be essential for NK cell-mediated killing. Yet, NCAM might be involved in NK cell migration, homing or related functions.

Antigens Differentiation T-LymphocyteCD3 ComplexCell Adhesion Molecules NeuronalT-LymphocytesCD3Blotting WesternImmunologyReceptors Antigen T-CellChromatography AffinityNatural killer cellCell–cell interactionmedicineHumansImmunology and AllergybiologyCell adhesion moleculeAntibodies MonoclonalCell migrationFlow CytometryPrecipitin TestsMolecular biologyEmbryonic stem cellCell biologyKiller Cells Naturalmedicine.anatomical_structurenervous systembiology.proteinNeural cell adhesion moleculeHoming (hematopoietic)European Journal of Immunology
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Cloning and characterization of Scavidin, a fusion protein for the targeted delivery of biotinylated molecules.

2001

We have constructed a novel fusion protein "Scavidin" consisting of the macrophage scavenger receptor class A and avidin. The Scavidin fusion protein is transported to plasma membranes where the avidin portion of the fusion protein binds biotin with high affinity and forms the basis for the targeted delivery of biotinylated molecules. Subcellular fractionation analysis, immunostaining, and electron microscopy demonstrated endosomal localization of the fusion protein. According to pulse-labeling and cross-linking studies Scavidin is found as monomers (55 kDa), dimers, and multimers, of which the 220-kDa form was the most abundant. The biotin binding capacity and active endocytosis of the bio…

Biotin bindingRecombinant Fusion ProteinsBlotting WesternGenetic VectorsPlasma protein bindingBiologyEndocytosisLigandsBiochemistrychemistry.chemical_compoundProtein structureBiotinTransduction GeneticTumor Cells CulturedAnimalsBiotinylationCloning MolecularReceptors ImmunologicMicroscopy ImmunoelectronMolecular BiologyReceptors ScavengerModels GeneticCell MembraneGene Transfer TechniquesScavenger Receptors Class ACell BiologyGliomaAvidinBlotting NorthernFusion proteinImmunohistochemistryPrecipitin TestsEndocytosisProtein Structure TertiaryRatsCross-Linking ReagentsRetroviridaeBiochemistrychemistryMicroscopy FluorescenceBiotinylationbiology.proteinDimerizationAvidinProtein BindingThe Journal of biological chemistry
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Identifying human platelet glycoproteins IIb and IIIa by capillary electrophoresis.

1998

Glanzmann thrombasthenia (GT) is an inherited hemorrhagic defect due to a failure of the platelet membrane glycoprotein (GP) IIb–IIIa complex. Capillary electrophoresis (CE) analysis of solubilized platelet membranes from normal individuals showed the presence of two peaks with a migration time of 27 and 29 min, respectively. An excellent run-to-run and day-to-day reproducibility of the technique (< 1% variation of the retention time) was documented. Using an automated Ferguson method, the apparent molecular masses were 100.0 kDa and 138.5 kDa, respectively. Immunoprecipitation with monoclonal antibodies anti-GP IIIa (B59.2.1) and anti-IIb (61.9.1.3) showed the two peaks as IIIa and IIb, re…

Blood PlateletsMaleClinical BiochemistryPlatelet Glycoprotein GPIIb-IIIa ComplexPlatelet membrane glycoproteinBiochemistryAnalytical ChemistryCapillary electrophoresisThrombastheniamedicineHumansPlateletChildPolyacrylamide gel electrophoresischemistry.chemical_classificationMembrane GlycoproteinsGlanzmann's thrombastheniaCell MembraneElectrophoresis Capillarymedicine.diseaseFlow CytometryMolecular biologyPrecipitin TestsPlatelet Glycoprotein GPIIb-IIIa ComplexchemistryGlycoproteinThrombastheniaElectrophoresis
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Shortstop Recruits EB1/APC1 and Promotes Microtubule Assembly at the Muscle-Tendon Junction

2003

Abstract Background: Shot (previously named Kakapo), is a Drosophila Plakin family member containing both Actin binding and microtubule binding domains. In Drosophila , it is required for a wide range of processes, including axon extension, dendrite formation, axonal terminal arborization at the neuromuscular junction, tendon cell development, and adhesion of wing epithelium. Results: To address how Shot exerts its activity at the molecular level, we investigated the molecular interactions of Shot with candidate proteins in mature larval tendon cells. We show that Shot colocalizes with EB1/APC1 and with a compact microtubule array extending between the muscle-tendon junction and the cuticle…

Blotting WesternFluorescent Antibody TechniqueBiologyTransfectionMicrotubulesCell junctionGeneral Biochemistry Genetics and Molecular BiologyTendonsTendon cellMicrotubuleAnimalsDrosophila ProteinsCytoskeletonActinPlakinAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)MusclesAxon extensionMicrofilament ProteinsfungiPrecipitin TestsCell biologyCytoskeletal ProteinsIntercellular JunctionsLarvaMuscle tendon junctionDrosophilaGeneral Agricultural and Biological SciencesCurrent Biology
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In BCR-ABL-positive cells, STAT-5 tyrosine-phosphorylation integrates signals induced by imatinib mesylate and Ara-C.

2003

In BCR-ABL-positive cells, the transcription factor STAT-5 is constitutively activated by tyrosine phosphorylation. STAT-5 activation results in upregulation of bcl-X(L) and increased resistance to induction of apoptosis. Here, we investigated the effects of imatinib mesylate and cytosine arabinoside (Ara-C) on STAT-5 tyrosine-phosphorylation, cellular proliferation and induction of apoptosis in cell lines and primary hematopoietic cells. Imatinib mesylate treatment strongly suppressed STAT-5 tyrosine-phosphorylation in K562 and primary CML blasts. In contrast to JAK-2 and PI-3-kinase inhibition, exposure of K562 cells to imatinib mesylate resulted in obvious suppression of proliferation. R…

Cancer ResearchProgrammed cell deathBlotting WesternFusion Proteins bcr-ablDown-RegulationAntineoplastic AgentsApoptosisBiologyPiperazineschemistry.chemical_compoundDownregulation and upregulationhemic and lymphatic diseasesLeukemia Myelogenous Chronic BCR-ABL PositivemedicineIn Situ Nick-End LabelingSTAT5 Transcription FactorHumansEnzyme InhibitorsPhosphorylationCell growthCytarabineImatinibTyrosine phosphorylationDrug SynergismHematologyDNAU937 CellsProtein-Tyrosine KinasesMilk ProteinsPrecipitin TestsDNA-Binding ProteinsImatinib mesylatePyrimidinesOncologychemistryApoptosisCaspasesBenzamidesCancer researchImatinib MesylateTrans-ActivatorsTyrosinePoly(ADP-ribose) PolymerasesK562 CellsCell Divisionmedicine.drugK562 cellsSignal TransductionLeukemia
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Nuclear insulin receptor substrate 1 interacts with estrogen receptor alpha at ERE promoters.

2004

Insulin receptor substrate 1 (IRS-1) is a major signaling molecule activated by the insulin and insulin-like growth factor I receptors. Recent data obtained in different cell models suggested that in addition to its conventional role as a cytoplasmic signal transducer, IRS-1 has a function in the nuclear compartment. However, the role of nuclear IRS-1 in breast cancer has never been addressed. Here we report that in estrogen receptor alpha (ERalpha)-positive MCF-7 cells, (1) a fraction of IRS-1 was translocated to the nucleus upon 17-beta-estradiol (E2) treatment; (2) E2-dependent nuclear translocation of IRS-1 was blocked with the antiestrogen ICI 182,780; (3) nuclear IRS-1 colocalized and…

Cancer Researchmedicine.medical_specialtyTranscription Geneticmedicine.medical_treatmentBlotting WesternEstrogen receptorBiologyInsulin-like growth factorInternal medicineCell Line TumorGeneticsmedicineAnimalsHumansReceptorPromoter Regions GeneticMolecular BiologyNuclear receptor co-repressor 1DNA PrimersBase SequenceReverse Transcriptase Polymerase Chain ReactionEstrogen Receptor alphaPromoterAntiestrogenPhosphoproteinsPrecipitin TestsIRS1Cell biologyProtein TransportEndocrinologyNuclear receptorReceptors EstrogenInsulin Receptor Substrate ProteinsProtein BindingOncogene
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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Calmodulin binds to p21(Cip1) and is involved in the regulation of its nuclear localization.

1999

p21(Cip1), first described as an inhibitor of cyclin-dependent kinases, has recently been shown to have a function in the formation of cyclin D-Cdk4 complexes and in their nuclear translocation. The dual behavior of p21(Cip1) may be due to its association with other proteins. Different evidence presented here indicate an in vitro and in vivo interaction of p21(Cip1) with calmodulin: 1) purified p21(Cip1) is able to bind to calmodulin-Sepharose in a Ca(2+)-dependent manner, and this binding is inhibited by the calmodulin-binding domain of calmodulin-dependent kinase II; 2) both molecules coimmunoprecipitate when extracted from cellular lysates; and 3) colocalization of calmodulin and p21(Cip…

Cyclin-Dependent Kinase Inhibitor p21CalmodulinMolecular Sequence DataBiologyBiochemistryCell LineCalmodulinIn vivoCyclinsProto-Oncogene ProteinsmedicineAnimalsCyclin D1Amino Acid SequencePhosphorylationMolecular BiologyCyclinCell NucleusSulfonamidesKinaseColocalizationCyclin-Dependent Kinase 4Cell BiologyImmunogold labellingPrecipitin TestsCyclin-Dependent KinasesCell biologyRatsEnzyme ActivationCell nucleusMicroscopy Electronmedicine.anatomical_structurebiology.proteinNuclear localization sequenceProtein BindingThe Journal of biological chemistry
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