Search results for "Protein subunit"

showing 10 items of 243 documents

Expression and developmental regulation of the cystine/glutamate exchanger (xc-) in the rat.

2007

The cystine/glutamate exchanger (antiporter x c − ) is a membrane transporter involved in the uptake of cystine, the rate-limiting amino acid in the synthesis of glutathione. Recent studies suggest that the antiporter plays a role in the slow oxidative excitotoxity and in the pathological effects of β-N-oxalylamino-l-alanine, the molecule responsible for neurolathyrism, a neurotoxic upper motor neuron disease. The mouse cystine/glutamate exchanger has been cloned and showed to be composed of two distinct proteins, one of which being a novel protein, named xCT, of 502 amino acids and 12 putative trans-membrane domains. We have generated and purified a polyclonal antibody to mouse xCT and stu…

MaleAmino Acid Transport SystemsAntiporterProtein subunitBlotting WesternImmunoblottingCystineGlutamic AcidBiologyBiochemistryRats Sprague-DawleyCellular and Molecular Neurosciencechemistry.chemical_compoundMiceWestern blotChlorocebus aethiopsmedicineAnimalsHumansCystine/glutamate exchanger Protein expression Cell cultures Developmenchemistry.chemical_classificationCerebral CortexNeuronsmedicine.diagnostic_testGlutamate receptorGene Expression Regulation DevelopmentalGeneral MedicineGlutathioneFibroblastsImmunohistochemistryAmino acidRatsBiochemistrychemistryAstrocytesCOS CellsCystineSettore MED/26 - NeurologiaElectrophoresis Polyacrylamide GelCell fractionationSubcellular FractionsNeurochemical research
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Altered receptor subtypes in the forebrain of GABAA receptor δ subunit-deficient mice: recruitment of γ2 subunits

2002

A GABA(A) receptor delta subunit-deficient mouse line was created by homologous recombination in embryonic stem cells to investigate the role of the subunit in the brain GABA(A) receptors. High-affinity [(3)H]muscimol binding to GABA sites as studied by ligand autoradiography was reduced in various brain regions of delta(-/-) animals. [(3)H]Ro 15-4513 binding to benzodiazepine sites was increased in delta(-/-) animals, partly due to an increment of diazepam-insensitive receptors, indicating an augmented forebrain assembly of gamma 2 subunits with alpha 4 subunits. In the western blots of forebrain membranes of delta(-/-) animals, the level of gamma 2 subunit was increased and that of alpha …

MaleAzidesProtein subunitBiologyTritiumSynaptic TransmissionIon ChannelsGABAA-rho receptorInterleukin 10 receptor alpha subunitBenzodiazepinesMiceRadioligand Assaychemistry.chemical_compoundAnimalsReceptorGABA Agonistsgamma-Aminobutyric AcidMice KnockoutNeuronsBinding SitesMuscimolGABAA receptorGeneral NeuroscienceBrainAffinity LabelsNeural InhibitionReceptors GABA-AMolecular biologynervous systemMuscimolchemistryMutationForebrainFemaleCys-loop receptorsNeuroscience
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Morphological studies on CLN2

2001

Electron microscopic, fluorescence microscopic, and immunohistochemical studies earlier performed on archivalcerebral tissue from Max Bielchowsky's original three patients revealed curvilinear bodies rich in subunit C of mitochondrial ATP synthase (SCMAS). Recent progress in the elucidation of CLN2, i.e. identification of the defective lysosomal enzyme tripeptidyl-peptidase I (TPP-I) and mutations in the CLN2 gene have further corroborated earlier data. Immunohistochemically the absence of the TPP-I protein could be confirmed in the archival tissues using pathological controls. Unlike biochemistry, immunohistochemistry enables examination of these archival tissues elucidating the causative …

MaleCell typePathologymedicine.medical_specialtyProtein subunitEncephalopathyBiologymedicine.disease_causeAminopeptidasesNeuronal Ceroid-LipofuscinosesChloroquineEndopeptidasesmedicineHumansChildDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMyopathyGeneMutationTripeptidyl-Peptidase 1BrainGeneral MedicineMitochondrial Proton-Translocating ATPasesmedicine.diseaseImmunohistochemistryProton-Translocating ATPasesMutationPediatrics Perinatology and Child HealthImmunohistochemistryFemaleNeurology (clinical)Serine Proteasesmedicine.symptomPeptide Hydrolasesmedicine.drugEuropean Journal of Paediatric Neurology
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A discoidal lipoprotein from the coelomic fluid of the polychaete Nereis virens.

2005

A discoidal lipoprotein was isolated from the coelomic fluid of the polychaete, Nereis virens, by density gradient centrifugation. The lipoprotein was present in both sexes and moved as a uniform band in an agarose gel. The average diameter of the lipoprotein particles determined by electron microscopy was 42 nm with a thickness of 10 nm. SDS electrophoresis showed two apoprotein subunits with molecular masses of 247 and 85 kDa, respectively. In lectin blots, both apoproteins were reactive with Concanavalin A indicating the presence of N-glycans. The small subunit was also reactive with peanut lectin, indicating additional O-glycosylation. The total lipid content was 48% and consisted mainl…

MaleEmbryo NonmammalianGlycosylationPhysiologyLipoproteinsBiologyIn Vitro TechniquesBiochemistrychemistry.chemical_compoundPolysaccharidesAnimalsParticle SizeMolecular BiologyDifferential centrifugationMolecular massLectinPolychaetaLipidsThin-layer chromatographyBody FluidsMolecular WeightElectrophoresisProtein SubunitschemistryBiochemistryConcanavalin Abiology.proteinAgaroselipids (amino acids peptides and proteins)FemaleLipoproteinComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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A novel pyruvate kinase (PK-S) from boar spermatozoa is localized at the fibrous sheath and the acrosome

2007

Boar spermatozoa contain a novel pyruvate kinase (PK-S) that is tightly bound at the acrosome of the sperm head and at the fibrous sheath in the principal piece of the flagellum, while the midpiece contains a soluble pyruvate kinase (PK). PK-S could not be solubilized by detergents, but by trypsin with no loss of activity. Purified PK-S as well as PK-S still bound to cell structures and soluble sperm PK have all kinetics similar to those of rabbit muscle PK-M1. The PK-S subunit had a relative molecular mass of 64 ± 1 × 103(n= 3), i.e. slightly higher than that of PK-M1, and carried an N-terminal extension (NH2-TSEAM-COOH) that is lacking in native PK-M1. Evidence is provided that PK-S is en…

MaleEmbryologyErythrocytesSwineProtein subunitBlotting WesternMolecular Sequence DataPyruvate KinaseBiologyEndocrinologySpecies SpecificitymedicineAnimalsAmino Acid SequenceAcrosomeSequence Homology Amino AcidMolecular massAntibodies MonoclonalObstetrics and GynecologyCell BiologyImmunogold labellingTrypsinSpermatozoaSpermReproductive MedicineBiochemistryPolyclonal antibodiesSperm Tailbiology.proteinElectrophoresis Polyacrylamide GelRabbitsSperm MidpieceAcrosomePyruvate kinasemedicine.drugReproduction
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Key features and clinical variability of COG6-CDG

2015

The conserved oligomeric Golgi (COG) complex consists of eight subunits and plays a crucial role in Golgi trafficking and positioning of glycosylation enzymes. Mutations in all COG subunits, except subunit 3, have been detected in patients with congenital disorders of glycosylation (CDG) of variable severity. So far, 3 families with a total of 10 individuals with biallelic COG6 mutations have been described, showing a broad clinical spectrum. Here we present 7 additional patients with 4 novel COG6 mutations. In spite of clinical variability, we delineate the core features of COG6-CDG i.e. liver involvement (9/10), microcephaly (8/10), developmental disability (8/10), recurrent infections (7…

MaleMicrocephalyGlycosylationAdolescentEndocrinology Diabetes and MetabolismProtein subunitHyperkeratosisMolecular Sequence DataGolgi ApparatusCase ReportsResearch SupportBiochemistryConserved oligomeric Golgi complexYoung AdultEndocrinologyCogCongenital Disorders of GlycosylationGeneticsJournal ArticleMedicineHumansNon-U.S. Gov'tChildMolecular BiologyExome sequencingGenetic Association StudiesGeneticsbusiness.industryConserved oligomeric Golgi complexResearch Support Non-U.S. Gov'tHigh-Throughput Nucleotide SequencingInfantCongenital disorder of glycosylationmedicine.diseasePhenotypeAdaptor Proteins Vesicular TransportPhenotypeCOG6MutationMicrocephalyFemaleCDGbusinessCongenital disorder of glycosylation
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The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase

2003

The mammalian soluble epoxide hydrolase (sEH) is an enzyme with multiple functions, being implicated in detoxification of xenobiotic epoxides as well as in regulation of physiological processes such as blood pressure. The enzyme is a homodimer, in which each subunit is composed of two domains. The 35-kDa C-terminal domain has an α/β hydrolase fold and harbors the catalytic center for the EH activity. The 25-kDa N-terminal domain has a different α/β fold and belongs to the haloacid dehalogenase superfamily of enzymes. The catalytic properties of the enzyme reported so far can all be explained by the action of the C-terminal domain alone. The function of the N-terminal domain, other than in …

MaleModels MolecularEpoxide hydrolase 2HydrolasesStereochemistryProtein subunitMolecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthDephosphorylationHydrolaseAnimalsHumansAmino Acid SequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classification1000 MultidisciplinaryMultidisciplinaryBase SequenceSequence Homology Amino AcidbiologyChemistryActive siteBiological SciencesPhosphoric Monoester HydrolasesRats Inbred F344Recombinant ProteinsRatsAmino acidEnzymeSolubilityBiochemistryMutagenesis Site-Directedbiology.protein570 Life sciences; biologyProceedings of the National Academy of Sciences
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Low Density Lipoprotein Receptor-related Protein 1 (LRP1) Modulates N-Methyl-d-aspartate (NMDA) Receptor-dependent Intracellular Signaling and NMDA-i…

2013

The lipoprotein receptor LRP1 is essential in neurons of the central nervous system, as was revealed by the analysis of conditional Lrp1-deficient mouse models. The molecular basis of its neuronal functions, however, is still incompletely understood. Here we show by immunocytochemistry, electron microscopy, and postsynaptic density preparation that LRP1 is located postsynaptically. Basal and NMDA-induced phosphorylation of the transcription factor cAMP-response element-binding protein (CREB) as well as NMDA target gene transcription are reduced in LRP1-deficient neurons. In control neurons, NMDA promotes γ-secretase-dependent release of the LRP1 intracellular domain (LRP1-ICD). However, pul…

MaleN-MethylaspartateCell SurvivalBlotting WesternGene ExpressionMice Transgenicmacromolecular substancesAMPA receptorBiologyCREBReceptors N-Methyl-D-AspartateBiochemistryMiceNeurobiologyPostsynaptic potentialAnimalsMolecular BiologyCells CulturedMice KnockoutNeuronsReverse Transcriptase Polymerase Chain Reactionmusculoskeletal neural and ocular physiologyTumor Suppressor ProteinsMembrane ProteinsCell BiologyEmbryo MammalianLRP1Cell biologyProtein SubunitsReceptors LDLnervous systemSynapsesLDL receptorbiology.proteinNMDA receptorFemaleAmyloid Precursor Protein SecretasesSignal transductionDisks Large Homolog 4 ProteinGuanylate KinasesPostsynaptic densityLow Density Lipoprotein Receptor-Related Protein-1Protein BindingSignal TransductionSynaptosomesJournal of Biological Chemistry
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Androglobin: a chimeric globin in metazoans that is preferentially expressed in mammalian testes

2012

Abstract: Comparative genomic studies have led to the recent identification of several novel globin types in the Metazoa. They have revealed a surprising evolutionary diversity of functions beyond the familiar O2 supply roles of hemoglobin and myoglobin. Here we report the discovery of a hitherto unrecognized family of proteins with a unique modular architecture, possessing an N-terminal calpain-like domain, an internal, circular permuted globin domain, and an IQ calmodulin-binding motif. Putative orthologs are present in the genomes of many metazoan taxa, including vertebrates. The calpain-like region is homologous to the catalytic domain II of the large subunit of human calpain-7. The glo…

MaleProtein subunitAmino Acid MotifsMolecular Sequence DataProtein domain610 Medicine & healthBiologyGenome10052 Institute of PhysiologyEvolution MolecularMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicine1311 GeneticsTestisGene expressionGenetics1312 Molecular BiologyAnimalsHumansGene familyAmino Acid SequenceGlobinBiologyMolecular BiologyGenePhylogenyEcology Evolution Behavior and Systematics030304 developmental biologyGenetics0303 health sciencesCalpainRecombinant ProteinsGlobinsProtein Structure TertiaryChemistry1105 Ecology Evolution Behavior and SystematicsMyoglobinchemistryMultigene Family10076 Center for Integrative Human Physiology570 Life sciences; biologyCalmodulin-Binding ProteinsHuman medicineSequence Alignment030217 neurology & neurosurgeryResearch Article
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New Hyperekplexia Mutations Provide Insight into Glycine Receptor Assembly, Trafficking, and Activation Mechanisms*

2013

Hyperekplexia is a syndrome of readily provoked startle responses, alongside episodic and generalized hypertonia, that presents within the first month of life. Inhibitory glycine receptors are pentameric ligand-gated ion channels with a definitive and clinically well stratified linkage to hyperekplexia. Most hyperekplexia cases are caused by mutations in the α1 subunit of the human glycine receptor (hGlyR) gene (GLRA1). Here we analyzed 68 new unrelated hyperekplexia probands for GLRA1 mutations and identified 19 mutations, of which 9 were novel. Electrophysiological analysis demonstrated that the dominant mutations p.Q226E, p.V280M, and p.R414H induced spontaneous channel activity, indicat…

MaleProtein subunitMutation MissenseBiologyBiochemistryProtein Structure SecondaryReceptors GlycinemedicineHumansHyperekplexiaReceptorMolecular BiologyGlycine receptorIon channelGeneticsWild typeMolecular Bases of DiseaseCell BiologyMuscle RigidityProtein Structure TertiaryAmino Acid SubstitutionGene Expression RegulationFemalemedicine.symptomIon channel linked receptorsCys-loop receptors
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