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Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN5777061
Luchinat, Barbieri, Rubino, Kozyreva, Cantini, Banci: In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants. in Nature communications 2014
The crystal structures of BmSod1 in both holo and Cu-deficient forms, are reported.
These results show that secosterol aldehydes are increased in plasma of symptomatic amyotrophic lateral sclerosis rats, overexpressing multiple copies (~8 copies) of G93A mutant human SOD1, and represent a class of aldehydes that can potentially modify SOD1 enhancing its propensity to aggregate.
Study results in transgenic mice carrying human SOD1 gene and analysis of cerebrospinal fluid as well as the spinal cord homogenate amyotrophic lateral sclerosis (ALS) patients suggest that metal-deficiency in mutant SOD1 at its copper-binding site is one of the earliest pathological features in SOD1-ALS.
A stable core of the SOD2 that unfolds last and refolds first, and directly observe several distinct misfolded states that branch off from the native folding pathways at specific points after the formation of the stable core.
The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis.
the introduction of SOD1(G93A) and TDP43(A315T), established Amyotrophic lateral sclerosis (ALS)-related mutations, changed the subcellular expression and localization of RNAs within the neurons, showing a spatial specificity to either the soma or the axon. Altogether, we provide here the first combined inclusive profile of mRNA and miRNA expression in two ALS models at the subcellular level.
Shorter activated partial thromboplastin time and increased SOD levels might be useful hemostatic markers in patients with type 2 diabetes mellitus.
In this study we demonstrate dynamic changes in the number of calretinin- (CR) and neuropeptide Y-expressing (NPY) interneurons in the motor cortex of the familial hSOD1(G93A) ALS mouse model, suggesting their potential involvement in motor neuron circuitry defects
Our results suggest that SOD1 mutation is the most common cause of amyotrophic lateral sclerosis(ALS) in Chinese populations and that the mutation spectrum of ALS varies among different ethnic populations
Weak significance was observed for a protective effect of the TT genotype of rs1041740 in the SOD1 gene relative to Type 1 Diabetes development (OR 0.318, 95% CI 0.092-0.959, p = 0.056).
SOD1 is S-acetylated in spinal cord homogenates from ALS and non-ALS subjects. The degree of S-acylation is highest for SOD1-CCS heterodimers and lowest for SOD1 monomers.
Study suggests that endoplasmic reticulum stress increases the susceptibility of SOD1WT to aggregate during aging, operating as a possible risk factor for developing amyotrophic lateral sclerosis.
Metallation and oxidation of SOD1 stabilize the native, mature conformation and decrease the number of detected excited conformational states.
results thus shed light on the role of local unfolding and conformational dynamics in aggregation of SOD1
Certain SOD1 mutants, viz. His80Arg and Asp83Gly, were recognized that were more damaging to the Zn binding loop than all other mutants, leading to a loss of Zn binding with altered coordination of the Zn ion. Furthermore, the conformational stability, compactness, and secondary structural alteration of the His80Arg and Asp83Gly mutants were monitored using distinct parameters.
describe here two cases of apparently sporadic amyotrophic lateral sclerosis associated with mutations, respectively, in SOD1 and TARDP genes
that global changes in DNA methylation might contribute to the ALS phenotype in carriers of not fully penetrant SOD1 mutations
The present study indicating that although the Ins/Del polymorphism of SOD1 is associated with the SOD1 expression levels, this polymorphism is not associated with the risk of dependency to heroin.
The mutant human SOD1-G93A protein induced axonal and myelin degeneration during the progression of Amyotrophic Lateral Sclerosis in a mouse model and participated in axon remyelination and regeneration in response to injury.
SOD1 oligomer and not the mature form of aggregated fibril is critical for the neurotoxic effects in the model of amyotrophic lateral sclerosis.
Data suggest that serum SOD1 levels are decreased in patients with controlled or uncontrolled acromegaly as compared to healthy subjects; in acromegaly, SOD1 levels are not associated with MnSOD/SOD2 polymorphisms.
the cytosolic SOD-null syndrome is largely consistent across sex and genetic background, but also significantly influenced by both.
The functional SOD1 and SOD2 genes knockout and their overexpression in neurons and glial tissue increase the sensitivity of Drosophila melanogaster to oxidative stress conditions.
Expression of zinc-deficient human superoxide dismutase in Drosophila neurons produces a locomotor defect linked to mitochondrial dysfunction.
curcumin increases mean lifespan of Drosophila via regulating gene expression of the key enzyme SOD and reducing accumulation of MDA and lipid peroxidation.
The activity of carbohydrate metabolizing enzymes, lipid and triglyceride concentration, and steady state NADPH:NADP(+) in SOD1-null and control transgenic rescue flies, was analysed.
Overexpression of Cu,ZnSOD and MnSOD in transgenic Drosophila.
survey of DNA sequence polymorphisms
Effects of overexpression of copper-zinc and manganese superoxide dismutases, catalase, and thioredoxin reductase genes on longevity.
SOD1 and SOD2 provide independent protection to compartment-specific protein iron-sulfur clusters against attack by superoxide generated under oxidative stress
A 1140 base pair region, composed of the single sod1 intron along with exon 2, was found to be essential for permitting spatial and temporal expression patterns that approximate normal endogenous expression.
Cu/Zn superoxide dismutase has a role in preventing spontaneous DNA damage
Instability of superoxide dismutase 1 of Drosophila in mutants deficient for its cognate copper chaperone
switching SOD1-deficient flies from normoxia into hypoxia fails to alter their mortality
These findings suggest unexpected specificity, mediated by both the primary protein pathology and cellular context, in the induced "secondary aggregation" of a mutant form of SOD1 that could be viewed as a reporter of proteostatic function
Presence of mutated SOD1 protein affects the MHC class I molecules expression and is associated with facial injured motoneurons.
DKO mice spontaneously develop severe liver failure at a relatively young stage, they have the potential for use as a model for hepatic disorders and for testing other potential treatments.
These results suggest that overexpression of SQSTM1 in SOD1 (H46R) mice accelerates disease onset by compromising the protein degradation pathways.
Results support the concept that impaired redox signaling, rather than oxidative damage, in peripheral nerve plays a key role in muscle loss in Sod1(-/-) mice and potentially sarcopenia during aging
This evidence favours mutant SOD1-containing astrocytes releasing destructive species that alter the biology of adjacent astrocytes
Given the close association of stress granules and TDP-43, we wondered whether internalisation of SOD1 aggregates stimulated TDP-43 cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 to the cytoplasm where it was still accumulated after 48 h.
Distinct roles for motor neuron autophagy early and late in the SOD1(G93A) mouse model of ALS.
It was observed that global AQP4 expression increased in the spinal cord of SOD1G93A mice as the disease progressed. However, AQP4 polarization decreased as the disease progressed, and AQP4 polarized localization at the endfeet of astrocytes was decreased in the spinal ventral horn of SOD1G93A mice at the disease onset and end stages.
Superoxide dismutase 1 mutation is associated with amyotrophic lateral sclerosis.
Restrictive Lung Disease in the Cu/Zn Superoxide-Dismutase 1 G93A Amyotrophic Lateral Sclerosis Mouse Model.
Endogenous MIF reduces the accumulation and toxicity of misfolded SOD1 in a mouse model of amyotrophic lateral sclerosis.
This study indicates that axonal and neuromuscular junction degeneration in the SOD1 model of amyotrophic lateral sclerosis is a complex and evolving sequence of events
In this newborn mouse lung hypoxia-reoxygenation model, we found downregulation of genes of mediators of inflammation, an antiapoptotic gene expression pattern, and downregulation of DNA glycosylases. Sod1 and Il1b were significantly differentially expressed when comparing reoxygenation using 60% O2 with air.
the senescence associated secretory phenotype was also increased significantly in the kidney of Sod1(-/)(-) mice compared to WT mice as measured by the expression of transcripts for IL-6 and IL-1b
Our study provides the first direct evidence that Abeta, an AD-linked factor, is associated to the pathogenesis of ALS and provides molecular clues to understand common aggregation mechanisms in the pathogenesis of neurodegenerative diseases.
deletion-rescue experiments show that a respiration-defective mutant of SOD1 is also impaired in its ability to rescue cells from toxicity caused by SOD1 deletion
These findings indicate that a loss of Sig1R function is causative for juvenile amyotrophic lateral sclerosis (ALS16), and collapse of the mitochondria-associated membrane is a common pathomechanism in both Sig1R- and SOD1-linked ALS.
the aberrant mutant SOD1-G3BP1 interaction affects stress granule dynamics
the absence of IP3R2 led to increased innate immunity, which may contribute to the decreased survival of the SOD1(G93A) mice.our data indicate that IP3R2 protects against the negative effects of inflammation, suggesting that the increase in IP3R2 expression in ALS patients is a protective response.
The results showed that 60-min ischemia of the porcine uterus conducted at the mid-secretory estrous phase caused decreased HIF-1alpha and increased SOD-2 gene expression.
Sequence comparison between sows with high and low estimated breeding value (EBV) for litter size, revealed a total of eight single nucleotide polymorphisms (SNPs) in the noncoding sequence and no SNPs in the coding region.
CuZnSOD mRNA is a broad-spectrum expression gene, which was detected in brain, heart, spleen, liver, kidney, lung, large intestine, small intestine, spinal cord, muscle, backfat, and stomach
Results indicate that variants of the PRLH and SOD1 genes are associated with heat tolerance in Chinese cattle.
The three-dimensional structure of bSOD1 reveals the imidazole ring of His19 localized within 5A from the alpha-carbon of Gly31 providing a structural basis that copper ion, most likely coordinated by His19, catalyzes the specific cleavage reaction
SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability
antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase, which show the changes in their expression during improper placental release
Results sugget thet Copper/Zinc superoxide dismutase (SOD1) may play a role in controlling intraluteal prostaglandin F2alph and reactive oxygen species action during functional and structural luteolysis.
ALOX5AP, CPNE3, IL1R2, IL6, TLR2, TLR4, and THY1 were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows.
Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced by PGF during functional luteolysis.
At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase.
Capillary electrophoresis and mass spectrometry to study the different structures of bovine SOD-1. In both cases, an average molecular mass corresponding to the apo-monomer SOD-1 was calculated.
flexibility of the metal sites involved in present a single-crystal X-ray diffraction study of Cu,Zn superoxide dismutase in space group P212121 at 0.57 GPa. The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution.
expression profile in follicles: oocytes (SOD1 throughout ooplasm & nucleoplasm); cumulus cells (no SOD1 detected); granulosa cells (expressed SOD1); follicular fluid (small follicles show increased amounts of SOD1 in comparison with large follicles)
Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions.
Raman spectrum analysis strongly suggests that the His41-mediated hydrogen bond bridge of Cu-Zn superoxide dismutase plays a crucial role in keeping the protein structure suitable for highly efficient catalytic reactions.
HCO(3)(-)-derived oxidant does not alter significantly the Cu(II) active site geometry and histidine coordination to Cu(II) in SOD1 as does H(2)O(2) alone
copper- and carbonate radical anion-mediated oxidations have roles in hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation
SOD1 mutants gain fatty acid binding abilities based on their structural instability and form cytotoxic granular aggregates
The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing 10(-4) M EDTA.
Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH).
communication between the two monomers of SOD1 such that the binding of one zinc ion per homodimer has a more profound effect on the homodimeric protein structure than the binding of subsequent metal ions
DNA accelerates the formation of SOD1 aggregates and is incorporated into SOD1 aggregates. SOD1 association with DNA, driven by electrostatic interactions, can restrict the orientation of SOD1 molecules and increase a SOD1 population along DNA strands.
amyloid and oxidative stress-related disease proteins like SOD 1 is increased in expression and form localized accumulations in diabetic muscle in this rabbit model of diabetes.
We found that guanylyl cyclases GCY-5 and GCY-22 and neuropeptide receptor NPR-1 act antagonistically to regulate SOD-1 expression in the gustatory neuron ASER.
These data suggest that SOD1 mutants are removed from the nucleus by CRM1 as a defense mechanism against proteotoxicity of misfolded SOD1 in the nucleus.
a post-translational modification to the inactive enzyme during hypoxia
the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on the copper chaperone CCS for activation
although several long-lived mutants of Caenorhabditis elegans have increased SOD levels, this phenomenon does not correlate with life span or growth rate.
SOD isoforms play no role in lifespan in ad lib or dietary restricted conditions, but mutational inactivation of SOD-1 reduces life extension by cold.
the ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans
this suggests that the activity of SOD-1, which so far has been thought to act mainly in cytoplasm, helps to control the detoxification of *O2- also in the mitochondria.
fenofibrate almost completely abolished GM-induced reactive oxygen species generation, which seemed to be mediated at least in part by the restoration of the expression of PPARalphadependent antioxidant enzymes, including catalase and superoxide dismutase (SOD)-1.
The earliest event in the pathophysiology of amyotrohic lateral sclerosis in the mutant sod1 zebrafish model involves neuronal stress in inhibitory interneurons, resulting from mutant Sod1 expression.
A hierarchic gene expression of copper homeostatic genes was demonstrated between atp7a, sp1 and sod1 in zebrafish.
depresses cathepsin L activity stimulated by free radicals and prevents otic complications associated with bone erosion
This isoform, when expressed in PC-12 cells affects t-butylhydroperoxide-induced apoptosis differentially from its isoenzyme.
Copper/zinc superoxide dismutase was cloned from the zebrafish ( Danio rerio). Evidence is presented that SOD protects against paraquat toxicity in fish.
Glia maturation factor-null cells ahow a concurrent decrease in CuZnSOD astrocytes.
The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene.
, Cu/Zn superoxide dismutase
, SOD, soluble
, indophenoloxidase A
, superoxide dismutase [Cu-Zn]
, superoxide dismutase, cystolic
, Cu, Zn superoxide dismutase
, Cu-Zn superoxide dismutase
, Cu/Zn-Superoxide dismutase
, CuZn superoxide dismutase
, CuZn-superoxide dismutase
, CuZn-superoxide dismutase (SOD)1
, Cu[2+] Zn[2+] superoxide dismutase
, Cu[2+]Zn[2+] superoxide dismutase
, Mn superoxide dismutase
, complementation group G
, copper and zinc SOD
, copper-zinc superoxide
, copper-zinc superoxide dismutase
, cytoplasmic Cu/ZnSOD
, super oxide dismutase
, superoxidase dismutase
, superoxide dismutase
, superoxide dismutase 1
, superoxide dismutatase
, superoxido dismutase
, tetrazolium oxidase
, tetrazolium oxidase-1
, superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))
, superoxide dismutase 1 soluble
, Cu(2+)-Zn2+ superoxide dismutase
, Cu-Zn-superoxide dismutase
, Cu,Zn-superoxide dismutase
, Cu,Zn superoxide dismutase
, superoxide dismutase [Cu-Zn] B