Search results for "Protein subunit"

showing 10 items of 243 documents

Cutting Edge: IL-23 Cross-Regulates IL-12 Production in T Cell-Dependent Experimental Colitis

2006

Abstract Although IL-12 and IL-23 share the common p40 subunit, IL-23, rather than IL-12, seems to drive the pathogenesis of experimental autoimmune encephalomyelitis and arthritis, because IL-23/p19 knockout mice are protected from disease. In contrast, we describe in this study that newly created LacZ knockin mice deficient for IL-23 p19 were highly susceptible for the development of experimental T cell-mediated TNBS colitis and showed even more severe colitis than wild-type mice by endoscopic and histologic criteria. Subsequent studies revealed that dendritic cells from p19-deficient mice produce elevated levels of IL-12, and that IL-23 down-regulates IL-12 expression upon TLR ligation. …

T-LymphocytesTransgeneT cellImmunologyDown-RegulationMice TransgenicInterleukin-23PathogenesisMiceInterleukin 23AnimalsImmunology and AllergyMedicineColitisCells Culturedbusiness.industryInterleukinsExperimental autoimmune encephalomyelitisColitismedicine.diseaseInterleukin-12Survival RateDisease Models AnimalProtein Subunitsmedicine.anatomical_structureImmunologyKnockout mouseInterleukin-23 Subunit p19Interleukin 12Disease SusceptibilitybusinessThe Journal of Immunology
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Pigment organization and energy transfer dynamics in isolated photosystem I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K, P…

2002

Abstract Green plant photosystem I (PSI) consists of at least 18 different protein subunits. The roles of some of these protein subunits are not well known, in particular those that do not occur in the well characterized PSI complexes from cyanobacteria. We investigated the spectroscopic properties and excited-state dynamics of isolated PSI-200 particles from wild-type and mutant Arabidopsis thaliana plants devoid of the PSI-G, PSI-K, PSI-L, or PSI-N subunit. Pigment analysis and a comparison of the 5K absorption spectra of the various particles suggests that the PSI-L and PSI-H subunits together bind approximately five chlorophyll a molecules with absorption maxima near 688 and 667nm, that…

Time FactorsAbsorption spectroscopyProtein subunitPhotosynthetic Reaction Center Complex ProteinsArabidopsisLight-Harvesting Protein ComplexesBiophysicsBiologyPhotosystem Ichemistry.chemical_compoundPhase (matter)MoleculePlant ProteinsQuantitative Biology::BiomoleculesPhotosystem I Protein ComplexTemperaturePigments Biologicalbeta CaroteneFluorescenceKineticsCrystallographySpectrometry FluorescenceEnergy TransferchemistryChlorophyllThermodynamicsHigh Energy Physics::ExperimentAbsorption (chemistry)Research Article
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Erythropoietin mediates tissue protection through an erythropoietin and common beta-subunit heteroreceptor

2004

The cytokine erythropoietin (Epo) is tissue-protective in preclinical models of ischemic, traumatic, toxic, and inflammatory injuries. We have recently characterized Epo derivatives that do not bind to the Epo receptor (EpoR) yet are tissue-protective. For example, carbamylated Epo (CEpo) does not stimulate erythropoiesis, yet it prevents tissue injury in a wide variety ofin vivoandin vitromodels. These observations suggest that another receptor is responsible for the tissue-protective actions of Epo. Notably, prior investigation suggests that EpoR physically interacts with the common β receptor (βcR), the signal-transducing subunit shared by the granulocyte-macrophage colony stimulating fa…

Time FactorsBiologyMotor ActivityHeteroreceptorNeuroprotectionCell LineMicemedicineReceptors ErythropoietinAnimalsVentricular Functionerythropoietin receptor; common beta receptor; tissue injury; CytokinesReceptorErythropoietinAortaCells CulturedSpinal Cord InjuriesMice KnockoutMultidisciplinaryCell MembraneBiological SciencesErythropoietin Erythropoietin receptor neuroprotectionErythropoietin receptorCell biologyMice Inbred C57BLProtein SubunitsErythrocyte maturationErythropoietinKnockout mouseImmunologyErythropoiesismedicine.drug
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Short‐term hypoxia promotes vascularization in co‐culture system consisting of primary human osteoblasts and outgrowth endothelial cells

2019

Prevascularization of tissue constructs before implantation has been developed as a novel and promising concept for successful implantation. Since hypoxia might induce angiogenesis, we have investigated the effects of hypoxic treatment on vascularization by using co-cultures of primary human osteoblasts (POBs) and outgrowth endothelial cells. Our results show that: (a) repeated short-term hypoxia (2% O2 for 8 hr), not long-term hypoxia (2% O2 for 24 hr), over 1 or 2 weeks, significantly enhances microvessel formation in co-cultures; (b) sustained hypoxia, not short-term or long-term hypoxia, causes cytotoxicity in mono- and co-cultures; (c) the expression of some angiogenic and inflammatory…

Time FactorsMaterials scienceCell SurvivalAngiogenesisProtein subunitmedicine.medical_treatment0206 medical engineeringBiomedical EngineeringNeovascularization Physiologic02 engineering and technologyBone tissueBiomaterialschemistry.chemical_compoundmedicineHumansRNA MessengerCytotoxicityMicrovesselCells CulturedOsteoblastsCell DeathGrowth factorMetals and AlloysEndothelial CellsHypoxia (medical)021001 nanoscience & nanotechnology020601 biomedical engineeringCell HypoxiaCoculture TechniquesUp-RegulationVascular endothelial growth factormedicine.anatomical_structurechemistryCeramics and CompositesCancer researchInflammation Mediatorsmedicine.symptom0210 nano-technologyJournal of Biomedical Materials Research Part A
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α-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines

2004

α-Synuclein (α-syn) is a small protein of unknown function that is found aggregated in Lewy bodies, the histopathological hallmark of sporadic Parkinson disease and other synucleinopathies. Mutations in the α-syn gene and a triplication of its gene locus have been identified in early onset familial Parkinson disease. α-Syn turnover can be mediated by the proteasome pathway. A survey of published data may lead to the suggestion that overexpression of α-syn wild type, and/or their variants (A53T and A30P), may produce a decrease in proteasome activity and function, contributing to α-syn aggregation. To investigate the relationship between synuclein expression and proteasome function we have s…

Time Factorsanimal diseasesmedicine.disease_causePC12 CellsBiochemistryMicechemistry.chemical_compoundTransgenesPromoter Regions GeneticMice KnockoutGeneticsMutationInnervationBrainParkinson DiseaseProteasome complexAmyloidosisCell biologyInnervacióalpha-SynucleinAdditions and CorrectionsPèptidsPlasmidsProteasome Endopeptidase ComplexPrionsProtein subunitBlotting WesternImmunoblottingSynucleinsMice TransgenicNerve Tissue ProteinsBiologyTransfectionBacterial ProteinsMultienzyme ComplexesmedicineAnimalsImmunoprecipitationMolecular BiologyAlpha-synucleinSynucleinopathiesEpilepsyWild typeGenetic VariationCell BiologyAxonsRatsnervous system diseasesMice Inbred C57BLEpilèpsiaDisease Models AnimalLuminescent ProteinschemistryProteasomenervous systemSinapsiMutationSynapsesSynucleinAmiloïdosiPeptides
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Proteasome comprising a beta1 inducible subunit acts as a negative regulator of NADPH oxidase during elicitation of plant defense reactions.

2005

Elicitation of defense reactions in tobacco by cryptogein, triggered a production of active oxygen species (AOS) via the NADPH oxidase, NtrbohD, and an accumulation of beta1din, a defense induced beta-type subunit of 20S proteasome. The proteasome inhibitor, MG132, stimulated this AOS production. Tobacco cells transformed with sense constructs of beta1din showed an inhibition of the AOS production following elicitin treatment, whereas the antisense transformed cells showed a strongly enhanced AOS production. In cells transformed with sense construct of beta1din, the NtrbohD transcripts failed to be induced by cryptogein as observed in control and antisense transformed cells. Conversely, in …

Tobacco BY-2 cellsHypersensitive responseProteasome Endopeptidase ComplexLeupeptinsBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyCysteine Proteinase InhibitorsBiochemistrychemistry.chemical_compoundStructural BiologyMG132Sense (molecular biology)TobaccoGeneticsmedicineNADPH OXIDASEPROTEASOMEMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSPlant ProteinsCRYPTOGEINNADPH oxidaseTOBACCO BY-2 CELLSNADPH OxidasesElicitinCell BiologyOligonucleotides AntisenseProtein SubunitsProteasomechemistryBiochemistryProteasome inhibitorbiology.proteinPLANT DEFENSEAOS PRODUCTIONReactive Oxygen SpeciesProteasome Inhibitorsmedicine.drugFEBS letters
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Developmental dynamics of PAFAH1B subunits during mouse brain development.

2012

Platelet-activating factor (PAF) mediates an array of biological processes in the mammalian central nervous system as a bioactive lipid messenger in synaptic function and dysfunction (plasticity, memory, and neurodegeneration). The intracellular enzyme that deacetylates the PAF (PAFAH1B) is composed of a tetramer of two catalytic subunits, ALPHA1 (PAFAH1B3) and ALPHA2 (PAFAH1B2), and a regulatory dimer of LIS1 (PAFAH1B1). We have investigated the mouse PAFAH1B subunit genes during brain development in normal mice and in mice with a hypomorphic allele for Lis1 (Lis1/sLis1; Cahana et al. [2001] Proc Natl Acad Sci U S A 98:6429–6434). We have analyzed quantitatively (by means of real-time poly…

Transcription GeneticProtein subunitNeurogenesisCentral nervous systemHindbrainIn situ hybridizationBiologyReal-Time Polymerase Chain Reaction03 medical and health sciencesMice0302 clinical medicineGene expressionmedicineAnimalsIn Situ Hybridization030304 developmental biologyRegulation of gene expression0303 health sciencesCerebrumGeneral NeuroscienceBrainGene Expression Regulation DevelopmentalMolecular biologyImmunohistochemistry3. Good healthMice Inbred C57BLProtein Subunitsmedicine.anatomical_structureForebrain1-Alkyl-2-acetylglycerophosphocholine EsteraseTranscriptomeMicrotubule-Associated Proteins030217 neurology & neurosurgery
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The yeast Aft1 transcription factor activates ribonucleotide reductase catalytic subunit RNR1 in response to iron deficiency

2020

Eukaryotic ribonucleotide reductases are iron-dependent enzymes that catalyze the rate-limiting step in the de novo synthesis of deoxyribonucleotides. Multiple mechanisms regulate the activity of ribonucleotide reductases in response to genotoxic stresses and iron deficiency. Upon iron starvation, the Saccharomyces cerevisiae Aft1 transcription factor specifically binds to iron-responsive cis elements within the promoter of a group of genes, known as the iron regulon, activating their transcription. Members of the iron regulon participate in iron acquisition, mobilization and recycling, and trigger a genome-wide metabolic remodeling of iron-dependent pathways. Here, we describe a mechanism …

Transcriptional ActivationRibonucleotideSaccharomyces cerevisiae ProteinsProtein subunitIronSaccharomyces cerevisiaeDeoxyribonucleotidesBiophysicsSaccharomyces cerevisiaeResponse ElementsBiochemistry03 medical and health sciencesStructural BiologyTranscription (biology)Gene Expression Regulation FungalRibonucleotide ReductasesGeneticsMolecular BiologyTranscription factorRibonucleotide reductase030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryIron deficiency030302 biochemistry & molecular biologyHigh Mobility Group ProteinsIron Deficienciesbiology.organism_classificationCell biologyDNA-Binding ProteinsRibonucleotide reductaseRegulonEnzymeYeast/TranscriptionProtein BindingTranscription Factors
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Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans

2021

AbstractPiwi-interacting RNAs (piRNAs) constitute a class of small RNAs that bind PIWI proteins and are essential to repress transposable elements in the animal germline, thereby promoting genome stability and maintaining fertility. C. elegans piRNAs (21U RNAs) are transcribed individually from minigenes as precursors that require 5’ and 3’ processing. This process depends on the PETISCO complex, consisting of four proteins: IFE-3, TOFU-6, PID-3, and ERH-2. We employ biochemical and structural biology approaches to characterize the PETISCO architecture and its interaction with RNA, together with its effector proteins TOST-1 and PID-1. These two proteins define different PETISCO functions: P…

Transposable elementStructural biologyChemistryEffectorProtein subunitGeneticsPiwi-interacting RNARNABiologyBinding siteBiogenesisDevelopmental BiologyCell biologyGenes & Development
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Philogenetics of Sea Urchin Tripneustes gratilla using Cytochrome Oxidase Subunit 1 Gene

2021

Sea urchin Tripneustes gratilla is multifunction organism that can be used as potential food source because of its high nutrient content. This organism can also be utilized bioindicator of sea waters and as a modal of organism for studying biology’s purposes. The purposes of this research is studying Filogenetic of sea urchin T. gratilla from waters of Wasior and Serui. The research has been doing at the Biotechnology Laboratory of the state of University of Papua on November to December 2009. The sample was extracted by using Chelex 10 % and was amplified with PCR technic (polymerase chain reaction). Sequencing of CO I gens (cythocrome oxidase subunit I) was done using sequencher ABI 377 (…

Tripneustes gratillaProtein subunitZoologyBiologyMega-law.inventionlawbiology.animalbiology.proteinCytochrome c oxidaseGeneSea urchinBioindicatorPolymerase chain reactionJURNAL SUMBERDAYA AKUATIK INDOPASIFIK
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