Search results for "Subunit"

showing 10 items of 513 documents

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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Epigenetic control of IL-23 expression in keratinocytes is important for chronic skin inflammation

2018

The chronic skin inflammation psoriasis is crucially dependent on the IL-23/IL-17 cytokine axis. Although IL-23 is expressed by psoriatic keratinocytes and immune cells, only the immune cell-derived IL-23 is believed to be disease relevant. Here we use a genetic mouse model to show that keratinocyte-produced IL-23 is sufficient to cause a chronic skin inflammation with an IL-17 profile. Furthermore, we reveal a cell-autonomous nuclear function for the actin polymerizing molecule N-WASP, which controls IL-23 expression in keratinocytes by regulating the degradation of the histone methyltransferases G9a and GLP, and H3K9 dimethylation of the IL-23 promoter. This mechanism mediates the inducti…

KeratinocytesMale0301 basic medicinemedicine.medical_treatmentWiskott-Aldrich Syndrome Protein NeuronalGeneral Physics and AstronomyEpigenesis GeneticHistonesMice0302 clinical medicineGenes ReporterInterleukin 23Promoter Regions Geneticlcsh:ScienceSkinMice KnockoutMultidisciplinaryInterleukin-17QMiddle AgedCytokine030220 oncology & carcinogenesisHistone methyltransferaseTumor necrosis factor alphaSignal transductionmedicine.symptomSignal TransductionAdultScienceGreen Fluorescent ProteinsPrimary Cell CultureInflammationBiologyArticleGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesImmune systemPsoriasismedicineAnimalsHumansPsoriasisInflammationHistone-Lysine N-MethyltransferaseGeneral Chemistrybiochemical phenomena metabolism and nutritionmedicine.diseaseDisease Models AnimalHEK293 Cells030104 developmental biologyInterleukin-23 Subunit p19Cancer researchlcsh:QNature Communications
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Avarol inhibits TNF-a generation and NF-kB activation in human cells and in animal models

2007

Avarol is a marine sesquiterpenoid hydroquinone with interesting pharmacological properties including anti-inflammatory and antipsoriatic effects. In the present study we evaluated the pharmacological effect of avarol on some inflammatory parameters related to the pathogenesis of psoriasis. Avarol inhibited tumor necrosis factor-alpha (TNF-alpha) generation in stimulated human monocytes (IC(50) 1 microM) and TNF-alpha-induced activation of nuclear factor-kappaB (NF-kappaB)-DNA binding in keratinocytes. In the mouse air pouch model, administration of avarol produced a dose-dependent reduction of TNF-alpha generation (ED(50) 9.2 nmol/pouch) as well as of interleukin (IL)-1beta, prostaglandin …

Keratinocytesmedicine.medical_specialtymedicine.medical_treatmentAnti-Inflammatory AgentsAntineoplastic AgentsBiologyPharmacologyMonocytesGeneral Biochemistry Genetics and Molecular BiologyCell LineMicechemistry.chemical_compoundDownregulation and upregulationIn vivoInternal medicinemedicineAnimalsHumansPsoriasisGeneral Pharmacology Toxicology and PharmaceuticsPeroxidaseInflammationHyperplasiaDose-Response Relationship DrugTumor Necrosis Factor-alphaNF-kappa B p50 SubunitInterleukinNF-κBGeneral MedicineDisease Models AnimalEndocrinologymedicine.anatomical_structureEicosanoidchemistryTetradecanoylphorbol AcetateFemaleTumor necrosis factor alphaEpidermisInflammation MediatorsKeratinocyteSesquiterpenesProstaglandin E
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20P Is evaluation of phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha (PIK3CA) mutational status on circulating tumour DNA (ctD…

2021

Kinasebusiness.industryProtein subunitAlpha (ethology)HematologyMolecular biologychemistry.chemical_compoundOncologyPhosphatidylinositol 45-bisphosphatechemistryMutational statusMedicineLiquid biopsybusinessDNAAnnals of Oncology
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Insulin-dependent leptin expression in breast cancer cells.

2008

Abstract Pathologic conditions associated with hyperinsulinemia, such as obesity, metabolic syndrome, and diabetes, seem to increase the risk of breast cancer. Here, we studied molecular mechanisms by which insulin activates the expression of leptin, an obesity hormone that has been shown to promote breast cancer progression in an autocrine or paracrine way. Using MDA-MB-231 breast cancer cells, we found that (a) insulin stimulated leptin mRNA and protein expression, which was associated with increased activation of the leptin gene promoter; (b) insulin increased nuclear accumulation of transcription factors hypoxia inducible factor (HIF)-1α and Sp1 and their loading on the leptin promoter;…

LeptinTranscriptional ActivationCancer Researchmedicine.medical_specialtySmall interfering RNAChromatin ImmunoprecipitationSp1 Transcription FactorBlotting WesternFluorescent Antibody TechniqueBreast NeoplasmsEnzyme-Linked Immunosorbent AssayBiologyParacrine signallingPhosphatidylinositol 3-Kinasesbreast cancerInternal medicinemedicineHyperinsulinemiaTumor Cells CulturedHumansHypoglycemic AgentsInsulinRNA MessengerRNA Small InterferingAutocrine signallingLuciferasesPromoter Regions GeneticTranscription factorCell NucleusMitogen-Activated Protein Kinase 1Gene knockdownLeptin receptorMitogen-Activated Protein Kinase 3Reverse Transcriptase Polymerase Chain ReactionLeptinmedicine.diseaseHypoxia-Inducible Factor 1 alpha SubunitCell HypoxiaEndocrinologyOncologyCancer researchFemalehormones hormone substitutes and hormone antagonistsCancer research
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Photoaffinity Labeling and Photoaffinity Cross-Linking of Phosphofructokinase-1 from Saccharomyces cerevisiae by 8-Azidoadeninenucleotides

2001

Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of four alpha- and four beta-subunits, each of them carrying catalytic and regulatory bindings sites for MgATP. In this paper, various photoaffinity labels, such as 8-azidoadenosine 5'-triphosphate, 8-azido-1,N6-ethenoadenosine 5'-triphosphate, and 8-N3-3'(2')-O-biotinyl-8-azidoadenosine 5'-triphosphate have been used to study their interaction with the enzyme in the dark and during irradiation. All nucleotidetriphosphates function as phosphate donor forming fructose 1,6-bisphosphate from fructose 6-phosphate. However, the kinetic analysis revealed distinctly differences between them. Photolabeling causes a decrease in enzyme a…

LightPhosphofructokinase-1Blotting WesternSaccharomyces cerevisiaeBiophysicsPhotoaffinity LabelsSaccharomyces cerevisiaePhotoaffinity LabelsBiochemistryAdenosine TriphosphateFructosediphosphatesChymotrypsinMagnesiumPhosphofructokinase 1Molecular Biologychemistry.chemical_classificationGel electrophoresisBinding SitesAffinity labelingbiologyPhotoaffinity labelingFructosephosphatesDarknessbiology.organism_classificationEnzyme assayKineticsProtein SubunitsCross-Linking ReagentsEnzymechemistryBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelArchives of Biochemistry and Biophysics
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Hypoxia-inducible factor 1 alpha expression increases during colorectal carcinogenesis and tumor progression

2008

Abstract Background Hypoxia-inducible factor 1 alpha (HIF-1α) is involved in processes promoting carcinogenesis of many tumors. However, its role in the development of colorectal cancer is unknown. To investigate the significance of HIF-1α during colorectal carcinogenesis and progression we examined its expression in precursor lesions constituting the conventional and serrated pathways, as well as in non-metastatic and metastatic adenocarcinomas. Methods Immunohistochemistry and Western blot is used to analyse HIF-1α expression in normal colonic mucosa, hyperplastic polyps (HPP), sessile serrated adenomas (SSA), low-grade (TA-LGD) and high-grade (TA-HGD) traditional adenomas as well as in n…

LipopolysaccharidesCancer ResearchPathologymedicine.medical_specialtyColorectal cancerColonic PolypsMouse model of colorectal and intestinal cancermedicine.disease_causelcsh:RC254-282chemistry.chemical_compoundWestern blotCell Line TumorGeneticsMedicineHumansNeoplasm Metastasismedicine.diagnostic_testbusiness.industrymedicine.diseaseHypoxia-Inducible Factor 1 alpha Subunitlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensImmunohistochemistryVascular endothelial growth factorCell Transformation NeoplasticOncologychemistryHyperplastic PolypTumor progressionDisease ProgressionImmunohistochemistrybusinessCarcinogenesisColorectal NeoplasmsPrecancerous ConditionsResearch ArticleBMC Cancer
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