HCSGD entry for SOD2
1. General information
| Official gene symbol | SOD2 |
|---|---|
| Entrez ID | 6648 |
| Gene full name | superoxide dismutase 2, mitochondrial |
| Other gene symbols | IPOB MNSOD MVCD6 |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000303 | Response to superoxide | IMP | biological_process |
| GO:0001306 | Age-dependent response to oxidative stress | IEA | biological_process |
| GO:0001315 | Age-dependent response to reactive oxygen species | IMP | biological_process |
| GO:0001666 | Response to hypoxia | IEA | biological_process |
| GO:0001836 | Release of cytochrome c from mitochondria | IEA ISS | biological_process |
| GO:0001889 | Liver development | IEA | biological_process |
| GO:0003032 | Detection of oxygen | IEA | biological_process |
| GO:0003069 | Vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure | IEA ISS | biological_process |
| GO:0003677 | DNA binding | IEA | molecular_function |
| GO:0004784 | Superoxide dismutase activity | IDA IEA | molecular_function |
| GO:0005739 | Mitochondrion | IDA | cellular_component |
| GO:0005743 | Mitochondrial inner membrane | IEA | cellular_component |
| GO:0005759 | Mitochondrial matrix | TAS | cellular_component |
| GO:0006357 | Regulation of transcription from RNA polymerase II promoter | IMP | biological_process |
| GO:0006749 | Glutathione metabolic process | IEA | biological_process |
| GO:0006801 | Superoxide metabolic process | IDA IEA | biological_process |
| GO:0007507 | Heart development | IEA | biological_process |
| GO:0007626 | Locomotory behavior | IEA | biological_process |
| GO:0008217 | Regulation of blood pressure | ISS | biological_process |
| GO:0008285 | Negative regulation of cell proliferation | IMP | biological_process |
| GO:0008630 | Intrinsic apoptotic signaling pathway in response to DNA damage | IEA | biological_process |
| GO:0008631 | Intrinsic apoptotic signaling pathway in response to oxidative stress | IEA | biological_process |
| GO:0009791 | Post-embryonic development | IEA | biological_process |
| GO:0010042 | Response to manganese ion | IEA | biological_process |
| GO:0010043 | Response to zinc ion | IEA | biological_process |
| GO:0010269 | Response to selenium ion | IEA | biological_process |
| GO:0010332 | Response to gamma radiation | IEA | biological_process |
| GO:0014823 | Response to activity | IEA | biological_process |
| GO:0019430 | Removal of superoxide radicals | IEA IMP | biological_process |
| GO:0019825 | Oxygen binding | IEA | molecular_function |
| GO:0022904 | Respiratory electron transport chain | IEA | biological_process |
| GO:0030097 | Hemopoiesis | IEA | biological_process |
| GO:0030145 | Manganese ion binding | IDA TAS | molecular_function |
| GO:0032364 | Oxygen homeostasis | IMP | biological_process |
| GO:0032496 | Response to lipopolysaccharide | IEA | biological_process |
| GO:0033591 | Response to L-ascorbic acid | IEA | biological_process |
| GO:0034021 | Response to silicon dioxide | IEA | biological_process |
| GO:0042493 | Response to drug | IEA | biological_process |
| GO:0042542 | Response to hydrogen peroxide | IEA | biological_process |
| GO:0042554 | Superoxide anion generation | IEA | biological_process |
| GO:0042645 | Mitochondrial nucleoid | IEA | cellular_component |
| GO:0042802 | Identical protein binding | IEA IPI | molecular_function |
| GO:0043066 | Negative regulation of apoptotic process | IEA | biological_process |
| GO:0043524 | Negative regulation of neuron apoptotic process | IGI | biological_process |
| GO:0045429 | Positive regulation of nitric oxide biosynthetic process | IEA | biological_process |
| GO:0045599 | Negative regulation of fat cell differentiation | IEA | biological_process |
| GO:0046686 | Response to cadmium ion | IEA | biological_process |
| GO:0046872 | Metal ion binding | IEA | molecular_function |
| GO:0048147 | Negative regulation of fibroblast proliferation | IEA | biological_process |
| GO:0048666 | Neuron development | IEA | biological_process |
| GO:0048678 | Response to axon injury | IEA | biological_process |
| GO:0048773 | Erythrophore differentiation | IEA | biological_process |
| GO:0050665 | Hydrogen peroxide biosynthetic process | IEA | biological_process |
| GO:0050790 | Regulation of catalytic activity | IEA | biological_process |
| GO:0051260 | Protein homooligomerization | IEA | biological_process |
| GO:0051289 | Protein homotetramerization | IPI | biological_process |
| GO:0051602 | Response to electrical stimulus | IEA | biological_process |
| GO:0051881 | Regulation of mitochondrial membrane potential | IEA | biological_process |
| GO:0055072 | Iron ion homeostasis | IEA | biological_process |
| GO:0055093 | Response to hyperoxia | IEA | biological_process |
| GO:0071361 | Cellular response to ethanol | IEA | biological_process |
| GO:1902176 | Negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress | IMP | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.0063185061 | 0.9784261388 | 0.2105182278 | 1.0000000000 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
| Data source | Up or down | Log fold change |
|---|---|---|
| GSE11954 | Up | 0.2170964566 |
| GSE13712_SHEAR | Up | 0.7933988762 |
| GSE13712_STATIC | Up | 0.2325681580 |
| GSE19018 | Down | -0.3451742054 |
| GSE19899_A1 | Up | 0.8905385210 |
| GSE19899_A2 | Up | 0.5185558159 |
| PubMed_21979375_A1 | Up | 1.2515529169 |
| PubMed_21979375_A2 | Up | 0.6633023753 |
| GSE35957 | Up | 1.1739461847 |
| GSE36640 | Up | 0.4403826922 |
| GSE54402 | Down | -0.0877059631 |
| GSE9593 | Up | 1.1859483168 |
| GSE43922 | - | - |
| GSE24585 | - | - |
| GSE37065 | - | - |
| GSE28863_A1 | - | - |
| GSE28863_A2 | - | - |
| GSE28863_A3 | - | - |
| GSE28863_A4 | - | - |
| GSE48662 | Up | 0.0810132600 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-222-3p | MIMAT0000279 | MIRT000135 | Flow//Luciferase reporter assay//Microarray//qRT-PCR//Western blot | Functional MTI | 19487542 |
| hsa-miR-377-3p | MIMAT0000730 | MIRT000993 | Luciferase reporter assay//Western blot | Functional MTI | 18716028 |
| hsa-miR-17-3p | MIMAT0000071 | MIRT005745 | Luciferase reporter assay//Quantitative proteomic approach//Western blot | Functional MTI | 21203553 |
| hsa-miR-30a-5p | MIMAT0000087 | MIRT028409 | Proteomics | Functional MTI (Weak) | 18668040 |
| hsa-miR-769-3p | MIMAT0003887 | MIRT039083 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-342-3p | MIMAT0000753 | MIRT043729 | CLASH | Functional MTI (Weak) | 23622248 |
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- mirRecord
MicroRNA name | mirBase ID | Target site number | MiRNA mature ID | Test method inter | MiRNA regulation site | Reporter target site | Pubmed ID |
|---|---|---|---|---|---|---|---|
| hsa-miR-222-3p | MIMAT0000279 | 1 | hsa-miR-222 | {Western blot} | {overexpression by miRNA mimics tranfection} | 19487542 |
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6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 35 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 27212182 | The kinetics of the effect of manganese supplementation on SOD2 activity in senescent human fibroblasts |
| 27212182 | OBJECTIVE: To investigate the effect of increasing Mn+2 concentrations on superoxide dismutase 2 (SOD2) activity in pre-senescent and senescent cultured fibroblasts, and to determine the Km Mn+2 values required to achieve maximal SOD2 activities in such cells |
| 27212182 | MATERIALS AND METHODS: SOD2 activities, and superoxide anion (SOA) generation rates, were assayed in mitochondrial sonicates of young passage 5 fibroblasts sub-cultured in routine growth medium (MEM 1), and in an accurately identified senescent passage 20, 25 and 30 subcultures incubated with media containing supplemental Mn+2 increments equal to 60, 90, 120, 150 and 180 nM (MEM 2, 3, 4, 5 and 6 respectively) |
| 27212182 | RESULTS: Whereas SOD2 activity did not significantly change in any of the cells sub-cultured in MEM 1, the enzyme underwent progressive significant increases in early senescent passage 20 cells and senescent passage 25 and 30 cells |
| 27212182 | The computed Km values of Mn+2 with respect to SOD2 in senescent passage 20, 25 and 30 cells equalled 19 |
| 27212182 | 4 nM respectively with corresponding SOD2 Vmax values of 37 |
| 27212182 | CONCLUSIONS: Senescent cells near the end of their replicative life span utilise more Mn+2 and achieve maximal SOD2 activities suggesting that the use of supplementary Mn+2 can help in combating oxidative stress |
| 26731545 | TE increased the mRNA expression of collagen-I, elastin, superoxide dismutase (SOD-2), aquaporin-3 (AQP-3), filaggrin, involucrin, transglutaminase in HDF or HaCaT cells, and decreased the mRNA levels of tyrosinase in B16F10 cells |
| 26696133 | SOD II levels increased gradually, whereas the SOD I and III levels were biphasic during the experimental periods after PPKO treatment |
| 26443543 | ERK5/HDAC5-mediated, resveratrol-, and pterostilbene-induced expression of MnSOD in human endothelial cells |
| 26443543 | Manganese superoxide dismutase (MnSOD) is an important antioxidant enzyme in mitochondria |
| 26443543 | Although polyphenols can induce the expression of MnSOD, their corresponding mechanisms remains unclear |
| 26443543 | In this study, we tested the hypothesis that resveratrol and pterostilbene can activate the expression of MnSOD through an AMPK-ERK5/HDAC5-KLF2 pathway |
| 26443543 | METHODS AND RESULTS: Our results revealed that two stilbenes reduced mitochondrial superoxide-free radicals, and endothelial cell senescence, and increased the mRNA expression of several genes related to mitochondrial function, including MnSOD |
| 26443543 | Moreover, two stilbenes upregulated the activation of human MnSOD promoter luciferase reporter gene and protein level in human umbilical vein endothelial cells |
| 26443543 | Furthermore, using a chromatin immunoprecipitation-PCR detection method, we found that resveratrol and pterostilbene promoted KLF2 binding to CACCC sites of the human MnSOD promoter |
| 26443543 | CONCLUSION: Resveratrol and pterostilbene can activate MnSOD expression through ERK5/HDAC5 pathway, thus alleviating mitochondrial oxidative stress in endothelial cells that relates to cardiovascular disease |
| 26240345 | We developed a mouse model, Tg(KRT14-cre/Esr1) (20Efu/J) x Sod2 (tm1Smel) , that generates mitochondrial oxidative stress in keratin 14-expressing epidermal stem/progenitor cells in a temporally controlled manner owing to deletion of Sod2, a nuclear gene that encodes the mitochondrial antioxidant enzyme superoxide dismutase 2 (Sod2) |
| 26240345 | Epidermal Sod2 loss induced cellular senescence, which irreversibly arrested proliferation in a fraction of keratinocytes |
| 26240345 | Surprisingly, in young mice, Sod2 deficiency accelerated wound closure, increasing epidermal differentiation and reepithelialization, despite the reduced proliferation |
| 26240345 | In contrast, at older ages, Sod2 deficiency delayed wound closure and reduced epidermal thickness, accompanied by epidermal stem cell exhaustion |
| 26240345 | In young mice, Sod2 deficiency accelerated epidermal thinning in response to the tumor promoter 12-O-tetradecanoylphorbol-13-acetate, phenocopying the reduced regeneration of older Sod2-deficient skin |
| 26159917 | Additionally, the cellular senescence phenotypes were manifested at the molecular level by a significant increase in p21 and p53 expression, a decrease in SOD2 expression, and a decrease in expression of some key autophagy-related genes such as Atg5, Atg7, Atg12, and Beclin 1 |
| 26141949 | Cells expressing Thr150Ala/Ser159Ala-mutant SIRT3 show a reduction in mitochondrial protein lysine deacetylation, Deltapsim, MnSOD activity, and mitochondrial ATP generation |
| 26121691 | Overexpression of SIRT3 promoted cell proliferation and enhanced ATP generation, glucose uptake, glycogen formation, MnSOD activity and lactate production, which were inhibited by SIRT3 knockdown, indicating that SIRT3 plays a role in reprogramming the bioenergetics in gastric tumor cells |
| 26089914 | For each early passage BM-MSC sample (5th or 6th passages), the normalized protein expression levels of senescence-associated markers p16(INK4A), p21(WAF1), SOD2, and rpS6(S240/244); the concentration of IL6 and IL8 in cell culture supernatants; and the normalized gene expression levels of pluripotency markers OCT4, NANOG, and SOX2 were correlated with final population doubling (PD) number |
| 25852816 | Using cultured fibroblasts with trisomy 21 (T21F), this study aimed to ascertain whether an imbalance exists in activities, mRNA, and protein expression of the antioxidant enzymes SOD1, SOD2, glutathione-peroxidase, and catalase during the cell replication process in vitro |
| 25536029 | Chronic CI inhibition did not increase mitochondrial superoxide levels or cellular lipid peroxidation and was paralleled by a specific increase in SOD2/GR, whereas SOD1/CAT/Gpx1/Gpx2/Gpx5 levels remained unchanged |
| 25360110 | Interestingly, markers indicating cellular senescence or oxidative stress (SNCA, CASP3, CAT, SOD2, and TERT) were largely unchanged within the ENS |
| 25344604 | E2F1 attenuates FOXO3-mediated expression of MnSOD and Catalase without affecting FOXO3 protein stability, subcellular localization, or phosphorylation by Akt |
| 24984152 | METHODS AND RESULTS: Treatment of human EPCs with HKa for 72h stimulated JNK phosphorylation at Thr183/Tyr185, and FOXO4 phosphorylation at Thr451, Concomitantly, upregulated the expression of MnSOD at protein and mRNA levels in a concentration-dependent manner |
| 24984152 | Moreover, HC at 50 nM increased FOXO4 phosphorylation at Thr451 and the protein level of MnSOD in EPCs |
| 24204728 | CONCLUSIONS: Bradykinin, acting through BK B2 receptor induced NO release, upregulated antioxidant Cu/Zn-SOD and Mn-SOD activity and expression while downregulating NADPH oxidase activity and subsequently inhibited ROS production, and finally protected against cardiomyocytes senescence induced by oxidative stress |
| 23997094 | Transcriptional and phenotypic changes in aorta and aortic valve with aging and MnSOD deficiency in mice |
| 23997094 | Wild-type (MnSOD(+/+)) and manganese SOD heterozygous haploinsufficient (MnSOD(+/-)) mice were studied at 3 and 18 mo of age |
| 23997094 | Haploinsufficiency of MnSOD did not alter antioxidant expression in aorta, but increased expression of Nox2 |
| 23997094 | When compared with that of aorta, age-associated reductions in antioxidant expression were larger in aortic valves from wild-type and MnSOD haploinsufficient mice, although Nox2 expression was unchanged |
| 23997094 | Expression of p16(ink4a), a marker of cellular senescence, was profoundly increased in both aorta and aortic valve from MnSOD(+/+) and MnSOD(+/-) mice |
| 23997094 | Functionally, we observed comparable age-associated reductions in endothelial function in aorta from both MnSOD(+/+) and MnSOD(+/-) mice |
| 23997094 | Interestingly, inhibition of NAD(P)H oxidase with apocynin or gp91ds-tat improved endothelial function in MnSOD(+/+) mice but significantly impaired endothelial function in MnSOD(+/-) mice at both ages |
| 23997094 | Aortic valve function was not impaired by aging or MnSOD haploinsufficiency |
| 23997094 | Furthermore, although MnSOD does not result in overt cardiovascular dysfunction with aging, compensatory transcriptional responses to MnSOD deficiency appear to be tissue specific |
| 23742046 | The alteration in regulation and synthesis of Forkhead box O3a (FoxO3a) family of transcription factors as well as major antioxidant enzymes (manganese superoxide dismutase, catalase) are also seen in aging |
| 23494737 | We have demonstrated that overexpression of SIRT3 under high glucose conditions reduces FOXO1 acetylation, suggesting that deacetylation of FOXO1 by SIRT3 elevates the expression of the FOXO1 target genes, catalase, and manganese superoxide dismutase (MnSOD) while decreasing senescence phenotypes |
| 23494737 | The data showed that shRNA-SIRT3 accelerated senescence phenotypes and acetylation of FOXO1; the expression level of catalase and MnSOD decreased compared with the control group |
| 23488583 | Forced expression of SIRT3, which activates the reactive oxygen species (ROS) scavenger superoxide dismutase 2 (SOD2) by de-acetylation to reduce oxidative stress, functionally rejuvenates mouse HSCs |
| 22958932 | This protective effect of rapamycin is mediated by the increase in expression of mitochondrial superoxide dismutase (MnSOD), and the consequent inhibition of ROS formation and oxidative stress |
| 22958927 | In normal tissues, rapamycin prevents epithelial stem cell senescence by reducing oxidative stress through increased MnSOD |
| 22907303 | Western blot was used to analyze the expression levels of xanthine oxidase (XOD), manganese-superoxide dismutase (Mn-SOD) and the subunits p67(phox) of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase in the HUVECs |
| 22907303 | Compared with the young group, the old group showed increased expression levels of XOD and p67(phox), as well as lower Mn-SOD expression level |
| 22907303 | With the pretreatment of NaHS, the up-regulations of XOD and p67(phox) levels and down-regulation of Mn-SOD level were inhibited |
| 22744176 | Moreover, manganese superoxide dismutase expression (MnSOD) was significantly downregulated in the aortas of diabetic WT mice, but was preserved in diabetic SIRT1-Tg mice |
| 22278880 | Mitochondrial oxidative stress caused by Sod2 deficiency promotes cellular senescence and aging phenotypes in the skin |
| 22278880 | Using a mouse model of genetic Sod2 deficiency, we show that failure to express this important mitochondrial anti-oxidant enzyme also impairs mitochondrial complex II activity, causes nuclear DNA damage, and induces cellular senescence but not apoptosis in the epidermis |
| 22278880 | Sod2 deficiency also reduced the number of cells and thickness of the epidermis, while increasing terminal differentiation |
| 21538411 | The specific activities of zinc/copper (Zn/Cu)-superoxide dismutase (SOD-1) and manganese (Mn)-superoxide dismutase (SOD-2) were assayed in young passage 5 fibroblasts and in serially subcultured cells that were characterized as senescent at passages 15-35 |
| 21538411 | SOD-1 and SOD-2 activities did not significantly change in senescent and young cells cultured in either routine medium [minimum essential medium 1 (MEM1)], or in Zn, Cu and Mn supplemented medium (MEM2) containing normal human plasma levels of the cations |
| 21538411 | SOD-1 and SOD-2 activities, however, underwent parallel progressive significant activity increases in senescent passage 20 and 25 cells, which peaked in value in passage 30 and 35 cells subcultured in supplemented medium (MEM3) containing triple human plasma levels of the cations |
| 21538411 | We infer that it was only possible to significantly stimulate SOD-1 and SOD-2 activities in senescent MEM3 cultured cells enabling them to combat oxidative stress |
| 20473639 | Manganese-containing superoxide dismutase (MnSOD) activity was unaffected by oxygen tension, but was elevated in young confluent cultures as compared with cultures in log-phase growth |
| 20473639 | MnSOD activity was significantly higher in senescent cultures than in early passage cultures and was also responsive to increased oxygen tension in senescent cultures |
| 20195488 | Sod2 haploinsufficiency does not accelerate aging of telomere dysfunctional mice |
| 20195488 | We therefore have analysed whether an increase in mitochondrial derived oxidative stress in response to heterozygous deletion of superoxide dismutase (Sod2(+/-)) would exacerbate aging phenotypes in telomere dysfunctional (mTerc(-/-)) mice |
| 20195488 | Heterozygous deletion of Sod2 resulted in reduced SOD2 protein levels and increased oxidative stress in aging telomere dysfunctional mice, but this did not lead to an increase in basal levels of oxidative nuclear DNA damage, an accumulation of nuclear DNA breaks, or an increased rate of telomere shortening in the mice |
| 20195488 | Moreover, heterozygous deletion of Sod2 did not accelerate the depletion of stem cells and the impairment in organ maintenance in aging mTerc(-/-) mice |
| 20195488 | In agreement with these observations, Sod2 haploinsufficiency did not lead to a further reduction in lifespan of mTerc(-/-) mice |
| 19126595 | MnSOD expression was significantly (P<0 |
| 17023572 | O(2)(-) produced by the mitochondria is converted to hydrogen peroxide by mitochondrial superoxide dismutase (SOD2) |
| 17023572 | Mice with complete SOD2 deficiency (SOD2(-/-)) exhibit dilated cardiomyopathy and fatty liver leading to neonatal mortality, whereas mice with partial SOD2 deficiency (SOD2(+/-)) show evidence of O(2)(-)-induced mitochondrial damage resembling cell senescence |
| 17023572 | Since earlier studies have provided compelling evidence for the role of oxidative stress and tubulointerstitial inflammation in the pathogenesis of hypertension, we tested the hypothesis that partial SOD2 deficiency may result in hypertension |
| 17023572 | Wild-type (SOD2(+/+)) and partial SOD2-deficient (SOD2(+/-)) mice had similar blood pressures at 6-7 mo of age, but at 2 yr SOD2(+/-) mice had higher blood pressure |
| 17023572 | Oxidative stress, renal interstitial T-cell and macrophage infiltration, tubular damage, and glomerular sclerosis were all significantly increased in 2-yr-old SOD2(+/-) mice |
| 17023572 | In conclusion, partial SOD2 deficiency results in oxidative stress and renal interstitial inflammation, changes compatible with accelerated renal senescence and salt-sensitive hypertension |
| 16304208 | To begin to test this hypothesis, we compared the activities and steady-state mRNA and protein levels of the antioxidant enzymes copper zinc (CuZn) superoxide dismutase (CuZnSOD, SOD1), manganese (Mn) superoxide dismutase (MnSOD, SOD2), and glutathione peroxidase (GPx) and the levels of reduced and oxidized glutathione in Leydig cells isolated from the testes of young (4-month-old) and aged (20-month-old) Brown Norway rats |
| 16304208 | CuZnSOD and MnSOD mRNA levels decreased with aging, though the magnitude of the decreases were considerably lower than the respective decreases in enzyme activities |
| 16304208 | MnSOD protein expression declined with age, and to a lesser extent, CuZnSOD did as well |
| 16189290 | Thus major antioxidants, MnSOD, glutathione peroxidase I, and glutathione reductase, were also evaluated |
| 16189290 | MnSOD expression was elevated in female vs |
| 16107721 | Manganese superoxide dismutase induces p53-dependent senescence in colorectal cancer cells |
| 16107721 | The mitochondrial enzyme manganese superoxide dismutase (MnSOD) is known to suppress cell growth in different tumor cell lines |
| 16107721 | Here we show that overexpression of MnSOD slows down growth of HCT116 human colorectal cancer cells by induction of cellular senescence |
| 16107721 | MnSOD overexpression causes up-regulation of p53 and its transcriptional target, the cyclin-dependent kinase inhibitor p21 |
| 16107721 | Accordingly, the overexpression of MnSOD in HCTp53(-/-) cells does not lead to senescence, whereas in HCTp21(-/-) cells we found induction of senescence by forced expression of MnSOD |
| 16107721 | Our data indicate that uncoupling of the electrochemical gradient by increased MnSOD activity gives rise to p53 up-regulation and induction of senescence |
| 11382788 | In the present study, the steady-state expression of manganese-containing superoxide dismutase, copper- and zinc-containing superoxide dismutase, catalase, and glutathione peroxidase was assessed in primary hepatocytes isolated from young and senescent rats and cultured in MATRIGEL: There was no change in steady-state superoxide dismutase protein or activity levels in cells collected from young animals and cultured for 7 days |
| 7520270 | All the immortalized clones had two common regions of deletion involving bands 6q21-22 and the SOD2 gene in 6q25 |
| 7520270 | The SOD2 deletion confirms recent data on the role of the Mn-dependent superoxide dismutase in inhibition of proliferation |
| 8262134 | This occurred despite the TNF-dependent induction of such proliferation-independent genes as manganese superoxide dismutase and interleukin-6 in senescent and quiescent cells |
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