Search results for "SOD1"

showing 10 items of 21 documents

Clinical characteristics of patients with familial amyotrophic lateral sclerosis carrying the pathogenic GGGGCC hexanucleotide repeat expansion of C9…

2012

A large hexanucleotide (GGGGCC) repeat expansion in the first intron of C9ORF72, a gene located on chromosome 9p21, has been recently reported to be responsible for 40% of familial amyotrophic lateral sclerosis cases of European ancestry. The aim of the current article was to describe the phenotype of amyotrophic lateral sclerosis cases carrying the expansion by providing a detailed clinical description of affected cases from representative multi-generational kindreds, and by analysing the age of onset, gender ratio and survival in a large cohort of patients with familial amyotrophic lateral sclerosis. We collected DNA and analysed phenotype data for 141 index Italian familial amyotrophic l…

MaleParentsPathologyphenotype-genotype correlationCohort Studies0302 clinical medicineC9orf72amyotrophic lateral sclerosigeneticsAmyotrophic lateral sclerosisAge of Onsetamyotrophic lateral sclerosis; familial als; C9Orf72; phenotype-genotype correlation0303 health sciencesSex CharacteristicsDNA Repeat ExpansionAdult Age of Onset Aged Amyotrophic Lateral Sclerosis; genetics/pathology Cohort Studies DNA Repeat Expansion DNA; genetics Female Humans Italy Male Middle Aged Mutation; genetics Parents Pedigree Phenotype Proteins; genetics Sex Characteristics Survival AnalysisMiddle Aged3. Good healthPedigreeSettore MED/26 - NEUROLOGIAPhenotypeItalyC9Orf72Settore MED/26 - NeurologiaFemaleFrontotemporal dementiaAdultmedicine.medical_specialtySOD1BiologyTARDBP03 medical and health sciencesInternal medicinemedicineHumans030304 developmental biologyAgedamyotrophic lateral sclerosis familial ALS C9ORF72 gene phenotype–genotype correlationC9orf72 ProteinAmyotrophic Lateral Sclerosisgenetics/pathologyProteinsOriginal ArticlesDNAmedicine.diseaseSurvival AnalysisC9orf72 ProteinSettore BIO/18 - Geneticaamyotrophic lateral sclerosis; familial ALS C9ORF72 gene; phenotype-genotype correlation;MutationNeurology (clinical)Age of onsetTrinucleotide repeat expansionfamilial al030217 neurology & neurosurgery
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Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protei…

2008

Recent studies provide evidence that wild-type Cu/Zn-superoxide dismutase (SOD1(hWT)) might be an important factor in mutant SOD1-mediated amyotrophic lateral sclerosis (ALS). In order to investigate its functional role in the pathogenesis of ALS, we designed fusion proteins of two SOD1 monomers linked by a polypeptide. We demonstrated that wild-type-like mutants, but not SOD1(G85R) homodimers, as well as mutant heterodimers including SOD1(G85R)-SOD1(hWT) display dismutase activity. Mutant homodimers showed an increased aggregation compared with the corresponding heterodimers in cell cultures and transgenic Caenorhabditis elegans, although SOD1(G85R) heterodimers are more toxic in functiona…

Cell SurvivalRecombinant Fusion Proteinsanimal diseasesSOD1MutantProtein aggregationAnimals Genetically ModifiedProtein CarbonylationSuperoxide dismutaseMicechemistry.chemical_compoundSuperoxide Dismutase-1Cell Line TumorGeneticsAnimalsHumansAmino Acid SequenceCaenorhabditis elegansMolecular BiologyGenetics (clinical)Motor NeuronsbiologySuperoxide DismutaseSuperoxideAmyotrophic Lateral SclerosisWild typenutritional and metabolic diseasesHydrogen PeroxideGeneral MedicineFusion proteinProtein Structure Tertiarynervous system diseasesCell biologyAmino Acid Substitutionnervous systemchemistryBiochemistrybiology.proteinDismutaseDimerizationHuman Molecular Genetics
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Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1

1998

Abstract A cDNA clone encoding a homolog of the yeast (Saccharomyces cerevisiae) gene Anti-oxidant 1(ATX1) has been identified from Arabidopsis. This gene, referred to as CopperCHaperone(CCH), encodes a protein that is 36% identical to the amino acid sequence of ATX1 and has a 48-amino acid extension at the C-terminal end, which is absent from ATX1 homologs identified in animals. ATX1-deficient yeast (atx1) displayed a loss of high-affinity iron uptake. Expression of CCH in the atx1 strain restored high-affinity iron uptake, demonstrating thatCCH is a functional homolog of ATX1. When overexpressed in yeast lacking the superoxide dismutase geneSOD1, both ATX1 and CCHprotected the cell from t…

endocrine systemDNA ComplementarySaccharomyces cerevisiae ProteinsPhysiologyMolecular Sequence DataSaccharomyces cerevisiaeSOD1ArabidopsisGene ExpressionSaccharomyces cerevisiaePlant ScienceFungal ProteinsGene productSuperoxide dismutaseOzoneCopper Transport ProteinsComplementary DNAArabidopsisGene expressionGeneticsHomeostasisAmino Acid SequenceCation Transport ProteinsBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsGenetic Complementation Testbiology.organism_classificationYeastOxidative StressBiochemistrybiology.proteinCarrier ProteinsCopperResearch ArticlePlant Physiology
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Wild-type Cu/Zn superoxide dismutase (SOD1) does not facilitate, but impedes the formation of protein aggregates of amyotrophic lateral sclerosis cau…

2009

Aggregation of Cu/Zn superoxide dismutase (SOD1) is a hallmark of a subset of familial amyotrophic lateral sclerosis (ALS) cases. The expression of wild-type SOD1 [SOD(hWT)] surprisingly exacerbates the phenotype of mutant SOD1 in vivo. Here we studied whether SOD1(hWT) may affect mutant SOD1 aggregation by employing fluorescence microscopy techniques combined with lifetime-based Förster resonance energy transfer (FRET). Only a very minor fraction of SOD1(hWT) was observed in aggregates induced by mutant SOD1(G37R), SOD1(G85R) or SOD1(G93C). Quite in contrast, co-expression of SOD(hWT) reduced the amount of mutant SOD1 in the aggregate fraction. Furthermore, we did not detect endogenous mou…

Protein Foldinganimal diseasesSOD1HeterodimerizationMice TransgenicEndogenyProtein aggregationCell Linelcsh:RC321-571MiceSuperoxide Dismutase-1In vivoFluorescence microscopeAnimalsHumanslcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySuperoxide DismutaseChemistryWild typenutritional and metabolic diseasesAmyotrophic lateral sclerosisPhenotypeMolecular biologynervous system diseasesFörster resonance energy transferSolubilitynervous systemNeurologyFLIM-based FRETMutationProtein MultimerizationProtein aggregationNeurobiology of Disease
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Mitochondrial and redox dysfunction in post-menopause as risk factor of neurodegenerative disease: a pilot study testing the role of a validated Japa…

2020

During the menopause women may experience increased oxidative stress and decreased antioxidant capacity and, together with the decline of neurosteroids, this represents a risk factor for Alzheimer's disease. The aim of the present study was to test a functional food (FPP-ORI, Osato Research Institute, Gifu, Japan) on redox and mitochondrial efficiency in post-menopausal women. The study population consisting of 69 untreated post-menopausal women were given supplements as follows: Group A was given a multivitamin (MV) 1c 2 times a day, and group B was given FPP 4.5 g 2 times a day. Group C consisted of 23 fertile premenopausal women as the control group. The tests carried out on entry, and a…

MDAmenopausePilot ProjectsAntioxidantsElectron Transport Complex IVFPP-ORIJapanFunctional FoodRisk FactorsMalondialdehydeBDNF; COX activity; FPP-ORI; GPx; MDA; SOD1; menopause; mitochondria; redox dysfunctionHumansGPxBrain-Derived Neurotrophic FactorNeurodegenerative DiseasesSOD1PostmenopauseCOX activitymitochondriaOxidative StressBDNFLeukocytes Mononuclearredox dysfunctioncFemaleCOX activity.Oxidation-Reductionredox dysfunction
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A longitudinal DTI and histological study of the spinal cord reveals early pathological alterations in G93A-SOD1 mouse model of amyotrophic lateral s…

2017

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by selective motor neuron degeneration in the motor cortex, brainstem and spinal cord. It is generally accepted that ALS is caused by death of motor neurons, however the exact temporal cascade of degenerative processes is not yet completely known. To identify the early pathological changes in spinal cord of G93A-SOD1 AIS mice we performed a comprehensive longitudinal analysis employing diffusion-tensor magnetic resonance imaging alongside histology and electron microscopy, in parallel with peripheral nerve histology. We showed the gradient of degeneration appearance in spinal cord white and gray matter, startin…

0301 basic medicinePathologyNeurologyTime FactorsMotor neuron diseasesSensory Receptor CellMice0302 clinical medicineImage Processing Computer-AssistedAxonAmyotrophic lateral sclerosisGray MatterAnthracenesWhite MatterMitochondriamedicine.anatomical_structureDiffusion Tensor ImagingNeurologySpinal CordG93A-SOD1 miceBrainstemHumanMotor cortexmedicine.medical_specialtyAxon degenerationTime FactorSensory Receptor CellsSOD1Mice TransgenicWhite matter03 medical and health sciencesMagnetic resonance imagingDevelopmental NeuroscienceMicroscopy Electron TransmissionmedicineElectron microscopyAnimalsHumansMotor neuron diseaseAmyotrophic lateral sclerosiAnimalbusiness.industrySuperoxide DismutaseAmyotrophic Lateral SclerosisSpinal cordmedicine.diseaseAmyotrophic lateral sclerosisMice Inbred C57BLDisease Models Animal030104 developmental biologyAnthracenebusinessNeuroscience030217 neurology & neurosurgeryExperimental neurology
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Expression of the ALS-causing variant hSOD1G93A leads to an impaired integrity and altered regulation of claudin-5 expression in an in vitro blood–sp…

2015

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by progressive paralysis due to the loss of primary and secondary motor neurons. Mutations in the Cu/Zn-superoxide dismutase (SOD1) gene are associated with familial ALS and to date numerous hypotheses for ALS pathology exist including impairment of the blood–spinal cord barrier. In transgenic mice carrying mutated SOD1 genes, a disrupted blood–spinal cord barrier as well as decreased levels of tight junction (TJ) proteins ZO-1, occludin, and claudin-5 were detected. Here, we examined TJ protein levels and barrier function of primary blood–spinal cord barrier endothelial cells of presymptomatic hSOD1G93…

SOD1FOXO1Mice TransgenicBiologyOccludinCell LineMiceGene expressionAnimalsClaudin-5ClaudinProtein kinase BBarrier functionCells CulturedTight Junction ProteinsTight junctionSuperoxide DismutaseAmyotrophic Lateral SclerosisEndothelial CellsCell biologyDisease Models AnimalNeurologyGene Expression RegulationSpinal CordImmunologyOriginal ArticleNeurology (clinical)Cardiology and Cardiovascular MedicineSignal Transduction
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Sporadic ALS is not associated with VAPB gene mutations in Southern Italy

2006

Abstract Mutations in the Cu/Zn superoxide dismutase (Sod1) gene have been reported to cause adult-onset autosomal dominant Amyotrophic Lateral Sclerosis (FALS). In sporadic cases (SALS) de novo mutations in the Sod1 gene have occasionally been observed. The recent finding of a mutation in the VAMP/synaptobrevin-associated membrane protein B (VAPB) gene as the cause of amyotrophic lateral sclerosis (ALS8), prompted us to investigate the entire coding region of this gene in SALS patients. One hundred twenty-five unrelated patients with adult-onset ALS and 150 healthy sex-age-matched subjects with the same genetic background were analyzed. Genetic analysis for all exons of the VAPB gene by DH…

AdultMaleSOD1Vesicular Transport ProteinsGlutamic AcidBiologyGene mutationmedicine.disease_causeGenetic analysisGeneral Biochemistry Genetics and Molecular BiologyPharmacology Toxicology and Pharmaceutics(all)03 medical and health sciencesExon0302 clinical medicineGene FrequencymedicineHumansCoding regionGeneral Pharmacology Toxicology and PharmaceuticsGeneAged030304 developmental biologyMedicine(all)Aged 80 and overGeneticsAspartic Acid0303 health sciencesMutationBase SequenceBiochemistry Genetics and Molecular Biology(all)Brief ReportAmyotrophic Lateral SclerosisGenetic VariationExonsGeneral MedicineMiddle AgedVAPBMolecular biologyIntrons3. Good healthAmino Acid SubstitutionItalyCase-Control StudiesMutationFemale030217 neurology & neurosurgeryJournal of Negative Results in BioMedicine
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The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease

2017

In neurons, but also in all other cells the complex proteostasis network is monitored and tightly regulated by the cellular protein quality control (PQC) system. Beyond folding of newly synthesized polypeptides and their refolding upon misfolding the PQC also manages the disposal of aberrant proteins either by the ubiquitin-proteasome machinery or by the autophagic-lysosomal system. Aggregated proteins are primarily degraded by a process termed selective macroautophagy (or aggrephagy). One such recently discovered selective macroautophagy pathway is mediated by the multifunctional HSP70 co-chaperone BAG3 (BCL-2-associated athanogene 3). Under acute stress and during cellular aging, BAG3 in …

0301 basic medicineHuntingtinSOD1AggrephagyReviewBAG3lcsh:RC321-57103 medical and health sciencesCellular and Molecular NeuroscienceUbiquitinselective macroautophagymedicineprotein quality controllcsh:Neurosciences. Biological psychiatry. NeuropsychiatryMolecular BiologyproteostasisbiologyBAG3NeurodegenerationAutophagymedicine.diseaseCell biology030104 developmental biologyProteostasisneurodegenerative disordersbiology.proteinNeuroscienceFrontiers in Molecular Neuroscience
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HFE p.H63D polymorphism does not influence ALS phenotype and survival.

2015

It has been recently reported that the p.His63Asp polymorphism of the HFE gene accelerates disease progression both in the SOD1 transgenic mouse and in amyotrophic lateral sclerosis (ALS) patients. We have evaluated the effect of HFE p.His63Asp polymorphism on the phenotype in 1351 Italian ALS patients (232 of Sardinian ancestry). Patients were genotyped for the HFE p.His63Asp polymorphism (CC, GC, and GG). All patients were also assessed for C9ORF72, TARDBP, SOD1, and FUS mutations. Of the 1351 ALS patients, 363 (29.2%) were heterozygous (GC) for the p.His63Asp polymorphism and 30 (2.2%) were homozygous for the minor allele (GG). Patients with CC, GC, and GG polymorphisms did not significa…

MaleAgingSurvivalSettore MED/03 - GENETICA MEDICAMiceSuperoxide Dismutase-1C9orf72HFE polymorphismAmyotrophic lateral sclerosisAmyotrophic lateral sclerosis; HFE polymorphisms; Phenotype; SOD1; Survival; Aged; Alleles; Amyotrophic Lateral Sclerosis; Animals; Disease Progression; Female; Hemochromatosis Protein; Histocompatibility Antigens Class I; Humans; Italy; Male; Membrane Proteins; Mice; Middle Aged; Polymorphism Genetic; Superoxide Dismutase; Superoxide Dismutase-1; Survival Rate; Genetic Association Studies; PhenotypeHFE polymorphismsMembrane ProteinAlleleAmyotrophic lateral sclerosis; HFE polymorphisms; Phenotype; SOD1; Survival; Neurology (clinical); Neuroscience (all); Aging; Developmental Biology; Geriatrics and GerontologyGeneral NeuroscienceSOD1Middle AgedPhenotypeSurvival RatePhenotypeItalyAmyotrophic lateral sclerosis; HFE polymorphisms; SOD1; phenotype; survivalDisease ProgressionFemaleHumanmedicine.medical_specialtySOD1Amyotrophic lateral sclerosis; HFE polymorphisms; Phenotype; SOD1; Survival;Genetic Association StudieBiologyTARDBPArticleGeneticInternal medicinemedicineAnimalsHumansAllelePolymorphismHemochromatosis ProteinSurvival rateAmyotrophic lateral sclerosiAllelesGenetic Association StudiesAgedNeuroscience (all)Polymorphism GeneticAnimalSuperoxide DismutaseAmyotrophic Lateral SclerosisHistocompatibility Antigens Class Inutritional and metabolic diseasesMembrane Proteinsmedicine.diseaseMinor allele frequencyEndocrinologyImmunologyNeurology (clinical)Geriatrics and GerontologyDevelopmental BiologyNeurobiology of aging
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