Search results for " Subunit"

showing 10 items of 502 documents

Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide

2011

DAPIT (Diabetes Associated Protein in Insulin-sensitive Tissues) is a small, phylogenetically conserved, 58 amino acid peptide that was previously shown to be down-regulated at mRNA level in insulin-sensitive tissues of type 1 diabetes rats. In this study we characterize a custom made antibody against DAPIT and confirm the mitochondrial presence of DAPIT on cellular level. We also show that DAPIT is localized in lysosomes of HUVEC and HEK 293T cells. In addition, we describe the histological expression of DAPIT in several tissues of rat and man and show that it is highly expressed especially in cells with high aerobic metabolism and epithelial cells related to active transport of nutrients …

HistologyCellular respirationProtein subunitBiophysicsPeptideV-ATPaseBiologyMitochondrionAntibodiesMitochondrial ProteinsHuman Umbilical Vein Endothelial CellsV-ATPaseAnimalsHumansmitochondrionta315lcsh:QH301-705.5PhylogenyDAPIT mitochondrion V-ATPase type 1 diabeteschemistry.chemical_classificationRegulation of gene expressionOriginal Papertype 1 diabetes.HEK 293 cellsMembrane ProteinsCell BiologyProton PumpsCell biologyMitochondriaRatsHEK293 CellsMembrane proteinchemistryBiochemistryGene Expression Regulationlcsh:Biology (General)Organ SpecificityLysosomesDAPITEuropean Journal of Histochemistry
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Cryptogein affects expression of alpha3, alpha6 and beta1 20S proteasome subunits encoding genes in tobacco.

2001

Twelve a and b 20S proteasome subunits cDNAs showing 70–82% identity with the corresponding genes in Arabidopsis or rice, and features of eukaryotic proteasome subunits were cloned in tobacco. Only b1-tcI 7, a3 and a6, 20S proteasome subunits encoding genes were up-regulated by cryptogein, a proteinaceous elicitor of plant defence reactions. These results led to the hypothesis that the activation of b1-tcI 7, a3 and a6 could induce a specific proteolysis involved in the hypersensitive response and systemic acquired resistance monitored by cryptogein. In eukaryotes, the 26S proteasome is the central multicatalytic proteinase complex comprising two subcomplexes: the 20S core particle that per…

Hypersensitive responseProteasome Endopeptidase ComplexPhysiologyProtein subunitProteolysisMolecular Sequence DataPlant ScienceGenes PlantGene Expression Regulation EnzymologicFungal ProteinsGene Expression Regulation PlantMultienzyme ComplexesArabidopsisGene expressionTobaccomedicineAmino Acid SequenceGenePlant Diseasesbiologymedicine.diagnostic_testAlgal Proteinsbiology.organism_classificationPlants Genetically ModifiedCysteine EndopeptidasesProteasomeBiochemistryProtein foldingJournal of experimental botany
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Structural Determinants for the Mode of Action of Imidazopyridine DS2 at δ-Containing γ-Aminobutyric Acid Type A Receptors

2021

Despite the therapeutic relevance of δ-containing γ-aminobutyric acid type A receptors (GABAARs) and the need for δ-selective compounds, the structural determinants for the mode and molecular site of action of δ-selective positive allosteric modulator imidazo[1,2-a]pyridine DS2 remain elusive. To guide the quest for insight, we synthesized a series of DS2 analogues guided by a structural receptor model. Using a fluorescence-based fluorometric imaging plate reader membrane potential assay, we found that the δ-selectivity and the pharmacological profile are severely affected by substituents in the 5-position of the imidazopyridine core scaffold. Interestingly, the 5-methyl, 5-bromo, and 5-chl…

ImidazopyridineAllosteric modulatorPyridinesStereochemistryAllosteric regulationLigands01 natural sciencesAminobutyric acidStructure-Activity Relationship03 medical and health sciencesAllosteric RegulationDrug DiscoveryHumansPotencyReceptor030304 developmental biologyMembrane potential0303 health sciencesBinding SitesChemistryReceptors GABA-A0104 chemical sciencesMolecular Docking SimulationProtein Subunits010404 medicinal & biomolecular chemistryHEK293 CellsDrug DesignMolecular MedicinePlate readerJournal of Medicinal Chemistry
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Cytoskeletal stabilization of inhibitory interactions in immunologic synapses of mature human dendritic cells with natural killer cells

2011

Abstract Human mature dendritic cells (DCs) can efficiently stimulate natural killer (NK)–cell responses without being targeted by their cytotoxicity. To understand this important regulatory crosstalk, we characterized the development of the immunologic synapse between mature DCs and resting NK cells. Conjugates between these 2 innate leukocyte populations formed rapidly, persisted for prolonged time periods and matured with DC-derived f-actin polymerization at the synapse. Polarization of IL-12 and IL-12R to the synapse coincided with f-actin polymerization, while other activating and inhibitory molecules were enriched at the interface between DCs and NK cells earlier. Functional assays re…

Immunological SynapsesImmunologyCell Communicationmacromolecular substancesBiochemistryImmunological synapseNatural killer cell03 medical and health sciences0302 clinical medicineInterleukin-15 Receptor alpha SubunitMicroscopy Electron TransmissionReceptors KIRMHC class ImedicineHumansAntigen-presenting cellCells CulturedCytoskeleton030304 developmental biology0303 health sciencesMicroscopy ConfocalbiologyReceptors Interleukin-12Dendritic CellsCell BiologyHematologyDendritic cellFlow CytometryInterleukin-12Immunological SynapsesActinsCoculture Techniques3. Good healthCell biologyKiller Cells Naturalmedicine.anatomical_structureMicroscopy Fluorescencebiology.proteinInterleukin 12RNA InterferenceK562 CellsMicrotubule-Organizing CenterWiskott-Aldrich Syndrome Protein030215 immunologyK562 cellsBlood
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CD4-mediated functional activation of human CD4+CD25+ regulatory T cells

2007

Naturally occurring CD4(+)CD25(+)FoxP3(+) regulatory T cells (CD25(+) Tregs) constitute a specialized population of T cells that is essential for the maintenance of peripheral self-tolerance. The immune regulatory function of CD25(+) Tregs depends upon their activation. We found that anti-CD4 antibodies activate the suppressive function of human CD25(+) Tregs in a dose-dependent manner. We demonstrate that CD4-activated CD25(+) Tregs suppress the proliferation of CD4(+) and CD8(+) T cells, their IL-2 and IFN-gamma production as well as the capacity of CD8(+) T cells to re-express CD25. By contrast, anti-CD4 stimulation did not induce suppressive activity in conventional CD4(+) T cells. Thes…

ImmunologyInterleukin-2 Receptor alpha SubunitAntibodies MonoclonalFOXP3hemic and immune systemschemical and pharmacologic phenomenaCD8-Positive T-LymphocytesBiologyFlow CytometryLymphocyte ActivationT-Lymphocytes RegulatoryCoculture TechniquesImmune toleranceCell biologyInterleukin 21Immune systemCD4 AntigensImmunologyImmune ToleranceHumansImmunology and AllergyCytotoxic T cellIL-2 receptorCell activationCD8European Journal of Immunology
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Functional characterization of two human olfactory receptors expressed in the baculovirus Sf9 insect cell system

2005

Olfactory receptors (ORs) are the largest member of the G-protein-coupled receptors which mediate early olfactory perception in discriminating among thousands of odorant molecules. Assigning odorous ligands to ORs is a prerequisite to gaining an understanding of the mechanisms of odorant recognition. The functional expression of ORs represents a critical step in addressing this issue. Due to limitations in heterologous expression, very few mammal ORs have been characterized, and so far only one is from human origin. Consequently, OR function still remains poorly understood, especially in humans, whose genome encodes a restricted chemosensory repertoire compared with most mammal species. In …

InsectaPhysiologyG protein[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringSf9BiologyOlfactory Receptor NeuronsCell LineReceptors G-Protein-Coupled03 medical and health sciencesBehavioral Neuroscience0302 clinical medicineCalcium imagingPhysiology (medical)[SDV.IDA]Life Sciences [q-bio]/Food engineeringmedicineAnimalsHumans[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringReceptorComputingMilieux_MISCELLANEOUS030304 developmental biologyG protein-coupled receptorOrphan receptor0303 health sciencesMicroscopy ConfocalOlfactory receptorGenomics[SDV.IDA] Life Sciences [q-bio]/Food engineeringGTP-Binding Protein alpha SubunitsSensory SystemsCell biologyINSECTEmedicine.anatomical_structureOdorantsImmunologyCalcium[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Heterologous expressionBaculoviridae030217 neurology & neurosurgery
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Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthro…

1992

Arylphorin was purified from larvae of the blowfly Calliphora vicina and studied in its oligomeric form and after dissociation at pH 9.6 into native subunits. In accordance with earlier literature, it was electrophoretically shown to be a 500 kDa hexamer (1 x 6) consisting of 78 kDa polypeptides (= subunits). Electron micrographs of negatively stained hexamers show a characteristic curvilinear, equilateral triangle of 12 nm in diameter (top view) and a rectangle measuring 10 x 12 nm (side view). Alternatively, particles in the top view orientation exhibit a roughly circular shape 12 nm in diameter. Crossed immunoelectrophoresis revealed the presence of a major subunit type; the nature of a …

Insectaanimal structuresCalliphora vicinaProtein ConformationPhysiologyStereochemistryProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiologyRandom hexamerBiochemistryCalliphoraEndocrinologyHemolymphmedicineAnimalsAmino Acid SequenceEcology Evolution Behavior and SystematicsGlycoproteinsSequence Homology Amino AcidProtein primary structureSpidersHemocyaninbiology.organism_classificationNephropidaeMicroscopy ElectronBiochemistryInsect HormonesLarvaHemocyaninsInsect ProteinsElectrophoresis Polyacrylamide GelAnimal Science and ZoologyProtein quaternary structureJournal of Comparative Physiology B
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On the origin of Metazoan adhesion receptors: cloning of integrin alpha subunit from the sponge Geodia cydonium

1997

Integrins are prominent receptors known from vertebrates and the higher phyla of invertebrates. Until now, no evidence has been provided for the existence of integrins in the lowest Metazoa, the sponges (Porifera). We have isolated and characterized a cDNA clone encoding the alpha subunit of integrin from the marine sponge Geodia cydonium (GCINTEG). The open reading frame encodes a polypeptide of 1,086 residues (118 kDa). The intracellular domain features the sequence Tyr-Phe-x-Gly-Phe-Phe-x-Arg, which is different in one residue from the characteristic consensus pattern for integrin alpha subunits. We conclude that sponges, the oldest multicellular animal phylum, already utilize the struct…

IntegrinsDNA ComplementaryMolecular Sequence DataIntegrinExtracellular matrixGeneticsAnimalsCloning MolecularReceptorMolecular BiologyEcology Evolution Behavior and SystematicsG alpha subunitCloningMembrane GlycoproteinsBase SequenceSequence Homology Amino AcidbiologyMembrane Proteinsbiology.organism_classificationPoriferaCell biologySuberites domunculaOpen reading frameSpongePlatelet Glycoprotein GPIb-IX Complexbiology.proteinMolecular Biology and Evolution
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The Selective Regulation of αVβ1 Integrin Expression Is Based on the Hierarchical Formation of αV-containing Heterodimers

2002

The integrin beta1 subunit can form a heterodimer with 12 different alpha subunits. According to the present model, the expression level of any alphabeta complex is regulated by the availability of the specific alpha subunit, whereas beta1 subunit is constantly present in a large excess. The expression of several heterodimers containing the alphaV subunit seems to be regulated by an identical mechanism. The fact that many cells express alphaVbeta1 heterodimer, and that this fibronectin/vitronectin receptor may be selectively regulated, compromises the present model of the regulation of beta1 and alphaV integrins. We have tried to solve this problem by assuming that distinct alphabeta hetero…

IntegrinsProtein subunitCellIntegrinBiologyModels BiologicalBiochemistryAntigens CDComplementary DNATumor Cells CulturedmedicineHumansReceptors VitronectinMelanomaMolecular BiologyCell MembraneCell BiologyTransfectionIntegrin alphaVFibronectinsCell biologyGene Expression Regulation NeoplasticFibronectinmedicine.anatomical_structurebiology.proteinVitronectinCollagenDimerizationIntracellularProtein BindingJournal of Biological Chemistry
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Interleukin-12 and -23 Control Plasticity of CD127(+) Group 1 and Group 3 Innate Lymphoid Cells in the Intestinal Lamina Propria.

2015

Human group 1 ILCs consist of at least three phenotypically distinct subsets, including NK cells, CD127(+) ILC1, and intraepithelial CD103(+) ILC1. In inflamed intestinal tissues from Crohn's disease patients, numbers of CD127(+) ILC1 increased at the cost of ILC3. Here we found that differentiation of ILC3 to CD127(+) ILC1 is reversible in vitro and in vivo. CD127(+) ILC1 differentiated to ILC3 in the presence of interleukin-2 (IL-2), IL-23, and IL-1β dependent on the transcription factor RORγt, and this process was enhanced in the presence of retinoic acid. Furthermore, we observed in resection specimen from Crohn's disease patients a higher proportion of CD14(+) dendritic cells (DC), whi…

Interleukin 2Receptors Retinoic AcidCellular differentiationCD14ImmunologyInterleukin-1betaRetinoic acidLipopolysaccharide Receptorschemical and pharmacologic phenomenaTretinoinMice SCIDBiologyInterleukin-12 Subunit p35Interleukin-7 Receptor alpha Subunitchemistry.chemical_compoundMiceIntestinal mucosaCrohn DiseaseMice Inbred NODmedicineImmunology and AllergyAnimalsHumansRetinoid X Receptor gammaLymphocytesIntestinal MucosaInterleukin-7 receptorCells CulturedMice KnockoutRetinoic Acid Receptor alphaInnate lymphoid cellvirus diseaseshemic and immune systemsCell DifferentiationDendritic CellsNuclear Receptor Subfamily 1 Group F Member 3Molecular biologyKiller Cells NaturalMice Inbred C57BLInfectious DiseaseschemistryLymphocyte TransfusionImmunologyInterleukin 12Interleukin-23 Subunit p19Interleukin-2medicine.drugImmunity
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