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Molecular mechanisms of lifespan extension in long-lived mitocondrial superoxide dismutase sod-2 mutants

ABSTRACT: Molecular mechanisms of lifespan extension in long-lived mitocondrial superoxide dismutase sod-2 mutants

PROVIDER: PRJNA1208437 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31940225_1.fastq.gz	Fastqsanger.gz
	SRR31940225_2.fastq.gz	Fastqsanger.gz
	SRR31940226_1.fastq.gz	Fastqsanger.gz
	SRR31940226_2.fastq.gz	Fastqsanger.gz
	SRR31940227_1.fastq.gz	Fastqsanger.gz

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Molecular mechanisms of lifespan extension in long-lived mitocondrial superoxide dismutase sod-2 mutants

Project description:To explore the molecular mechanisms of lifespan extension in sod-2 mutants in an unbiased manner, we used RNA sequencing to identify differentially expressed genes in sod-2 mutants compared to wild-type worms. We found a large number of gene expression changes at day 1 of adulthood and much fewer at day 8. Upregulated genes in sod-2 mutants included genes involved in innate immunity and cuticle development. There were many more differentially expressed genes between day 1 and day 8 of adulthood compared to differences between the genotypes.

2025-02-25 | GSE286219 | GEO

Efficient and economical iron metabolism of Aspergillus fumigatus protects its mitochondria in the absence of Mn-superoxide dismutase

Project description:The importance of manganese superoxide dismutase (Mn-SOD), an evolutionarily ancient metalloenzyme maintaining the integrity and functions of mitochondria, was studied in oxidative stress treated Aspergillus fumigatus cultures. Deletion of the Mn-SOD gene (sodB) increased both the menadione sodium bisulfite (MSB) elicited oxidative stress, and the deferiprone (DFP) induced iron limitation stress sensitivity of the strain. Moreover, DFP treatment enhanced the MSB sensitivity of both the gene deletion mutant and the reference strain. Concurring with these results, RNS sequencing data also demonstrated that deletion of sodB largely altered the MSB induced oxidative stress response. The difference between the oxidative stress responses of the two strains manifested mainly in the intensity of the response. Importantly, upregulation of “Ribosome protein”, “Iron uptake”, and Fe-S cluster assembly” genes, alterations in the transcription of “Fe-S cluster protein” genes, downregulation of “Heme binding protein” genes under MSB stress were characteristic for only the DsodB gene deletion mutant. We assume that the elevated superoxide level generated by MSB treatment may have destroyed Fe-S cluster proteins of mitochondria in the absence of SodB mediated protection. Re-synthesis of Fe-S cluster proteins enhanced translation and increased iron demand changing iron metabolism and increasing DFP sensitivity considerably.

2025-01-01 | GSE269970 | GEO

Enterocyte Superoxide Dismutase 2 Deletion Drives Hyperinsulinemia and Obesity

Project description:Enterocyte Superoxide Dismutase 2 Deletion Drives Hyperinsulinemia and Obesity

| PRJNA664402 | ENA

Bacterial Superoxide Dismutase variants, metal-loaded or apo - structural dynamics study

Project description:The proteins are a pair of closely related superoxide dismutase (SOD) enzymes from the Gram positive bacterium, Staphylococcus aureus. SodA is a Mn-specific SOD (MnSOD), which is inactive when loaded with Fe, whereas SodM is a 'cambialistic' SOD (camSOD), which is catalytically active with either Mn or Fe as a cofactor. Their sequences are 75% identical across their 199 amino acid sequences: the crystal structures of each enzyme in each metal-loaded form: Mn-loaded MnSOD SodA: PDB ID 5N56 Fe-loaded MnSOD SodA: PDB ID 6EX3 Mn-loaded camSOD SodM: PDB ID 5N57 Fe-loaded camSOD SodM: PDB ID 6EX4 The resulting structures (all to approximately 2A resolution) showed no significant differences that indicated molecular reasons for the differences in activity. Because of the differences in activity, therefore, the project aimed to compare three forms of these enzymes to determine whether there are any differences in the dynamics of regions of their structure, most notably those within the active site and the putative substrate access route(s).

2025-05-07 | PXD057066 | Pride

Redistribution of EC-SOD due to the R213G SNP reveals differential RNA-seq profile of recruited alveolar macrophages and accelerated apoptosis in response to bleomycin

Project description:A known human SNP in the matrix-binding domain of extracellular superoxide dismutase (EC-SOD), with an arginine to glycine substitution at position 213 (R213G), redistributes EC-SOD from the matrix into extracellular fluids. We reported that, following bleomycin (bleo), knock-in mice harboring the human R213G SNP (R213G mice), compared to wild-type (WT) littermates exhibit enhanced resolution of inflammation and protection against fibrosis. We tested the hypothesis that the EC-SOD R213G SNP promotes resolution via accelerated apoptosis of recruited alveolar macrophage (recAM).

2022-02-01 | GSE127345 | GEO

Differential microRNA expression of R213G extracellular superoxide dismutase mice in the setting of inflammation resolution and attenuated acute lung injury

Project description:Purpose: Oxidative stress is a key contributor to the development of dysregulated inflammation in acute lung injury (ALI). A naturally occurring single nucleotide polymorphism in the key extracellular antioxidant enzyme, extracellular superoxide dismutase (EC-SOD), results in an arginine to glycine substitution (R213G) which promotes resolution of inflammation and protection against bleomycin-induced ALI. Previously we found that mice with the R213G mutation in EC-SOD have an inflammation-resolving transcriptomic profile at 7 days post-bleomycin However, the epigenetic differences between WT and R213G EC-SOD lungs have not been examined. Therefore, we used Next Generation microRNA (miR) Sequencing of lung tissue to identify dysregulated miRs 7 days after bleomycin in wild-type (WT) and R213G mice. Methods: WT and homozygous R213G EC-SOD (rs1799895) mice received one intratracheal administration of bleomycin in phosphate-buffered saline (PBS) (100 uL at 1 U/mL) or PBS at 8-12 weeks old. Lungs were harvested and frozen. Frozen lungs were homogenized, placed in Qiazol, and RNA was isolated using the miRNeasy Mini Kit (Qiagen). Samples underwent 1x150, directional, single-end sequencing using the Illumina hiSEQ 4000 system. Results: 1424 microRNAs were detected. Up/Down regulated microRNAs were defined as havinga FC > 1.2 and p <0.05. microRNAs "unique" to a genotype were defined as meeting the prevoius criteria in only one strain, or in both with a fold change 1.5x greater in one over the other. This method identified 92 WT and 235 R213G miRs uniquely dysregulated in their respective genotypes.

2020-05-29 | GSE147138 | GEO

Switch of mitochondrial superoxide dismutase into a prooxidant peroxidase in manganese-deficient cells

Project description:Superoxide radical anion and other Reactive Oxygen Species are constantly produced during respiration. In mitochondria, the dismutation of the superoxide radical anion is accelerated by the mitochondrial superoxide dismutase 2 (SOD2), an enzyme that has been traditionally associated with antioxidant protection. However, increases in SOD2 expression promote oxidative stress, indicating that there may be a prooxidant role for SOD2. We show that SOD2, which normally binds manganese, can incorporate iron and generate an alternative isoform with peroxidase activity. The switch from manganese to iron allows FeSOD2 to utilize H2O2 to promote oxidative stress. We found that FeSOD2 is formed in cultured cells. FeSOD2 causes mitochondrial dysfunction and higher levels of oxidative stress in cultured cells. We show that formation of FeSOD2 converts an antioxidant defense into a prooxidant peroxidase that leads to cellular changes seen in multiple human diseases.

2017-12-05 | GSE106206 | GEO

Cathepsin A contributes to left ventricular remodeling by degrading the antioxidant enzyme extracellular superoxide dismutase

Project description:In the heart, the serine carboxypeptidase cathepsin A (CatA) is distributed between lysosomes and the extracellular matrix (ECM). CatA-mediated degradation of extracellular peptides may contribute to ECM-remodeling and left ventricular (LV) dysfunction. This study aimed to evaluate the effects of CatA overexpression on LV remodeling. A proteomic analysis of the secretome of adult mouse cardiac fibroblasts upon digestion by CatA identified the extracellular antioxidant enzyme superoxide dismutase (EC-SOD) as a novel substrate of CatA (5-fold decreased abundance; p=0.0001). In vitro, cardiomyocytes and cardiac fibroblasts expressed and secreted CatA protein. EC-SOD protein was expressed and secreted only by cardiac fibroblasts. Cardiomyocyte-specific over-expression of CatA and increased activity in the LV of transgenic mice (CatA-TG) reduced EC-SOD protein levels by 43% (p<0.001). Loss of EC-SOD-mediated anti-oxidative protection resulted in accumulation of superoxide radicals (WT: 4.54±1.2 vs. CatA-TG: 8.62±2.3µmol/mg tissue/min; p=0.0012), increased inflammation, myocyte hypertrophy (WT: 19.8±1.0 vs. CatA-TG: 21.9±1.8µm; p=0.024), cellular apoptosis, and elevated mRNA expression of hypertrophy-related and pro-fibrotic marker genes, without effecting intracellular detoxifying proteins. In CatA-TG mice LV interstitial fibrosis formation was enhanced by 19% (p=0.028) and type I/type III collagen ratio was shifted towards higher abundance of collagen I fibers (p=0.026). Cardiac remodeling in CatA-TG was accompanied by increased LV weight/body weight and LV enddiastolic volume (WT: 50.8±5.8 vs. CatA-TG: 61.9±6.2 µl; p=0.018). Thus, in the heart CatA-mediated reduction of EC-SOD protein contributes to increased oxidative stress, myocyte hypertrophy, ECM remodeling and inflammation. This implicates CatA as a potential therapeutic target to prevent ventricular remodeling.

2020-07-10 | PXD019895 | Pride

SOD

Project description:Oryza sativa Japonica Group SOD, Superoxide dismutase, copper/zinc binding domain containing protein, is expressed in 14 baseline experiment(s);

| Os04g0573200 | ExpressionAtlas

SOD

Project description:Oryza sativa Japonica Group SOD, Superoxide dismutase, copper/zinc binding domain containing protein, is differentially expressed in 14 experiment(s);

| Os04g0573200 | ExpressionAtlas

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