Mice with Targeted Mutation of Peroxiredoxin 6 Develop Normally but Are Susceptible to Oxidative Stress

Wang, Xiaosong; Phelan, Shelley A.; Forsman‐Semb, Kristina; Taylor, Eric F.; Petros, Christina; Brown, Aaron C.; Lerner, Charles P.; Paigen, Beverly

doi:10.1074/jbc.m302706200

Cited by 294 publications

(270 citation statements)

References 50 publications

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“…PRDX6 protein expression was comparable in lenses/LECs of both groups and a similar finding has been reported by other groups. 43 Accordingly, we utilized wild-type mice and homozygous lenses/LECs throughout the study.…”

Section: Resultsmentioning

confidence: 99%

“…10 Recently, using Prdx6 À/À mouse, it has been reported that endogenously produced mouse PRDX6 functioned in vivo as an antioxidant enzyme, and its function was not redundant to other PRDXs and antioxidant enzyme. 43 Notably, the gene expression of Prdx1-5, Gpx1-4, Cat, superoxide dismutase (Sod1-3), thioredoxin (Txn1-2), and Glutaredoxin (Glrx1-2) was found similar between Prdx6 À/À and Prdx6 þ / þ mice. 43 These findings suggest that PRDX6 activities are independent of other enzymes.…”

Section: Discussionmentioning

confidence: 95%

“…Real-time PCR was carried out using specific primers. 43 (Figure 2A, e). Interestingly, these differences were evident in cells cultured with complete media, but not as distinguishable as in those cultured under serum depletion conditions ( Figure 2A, d).…”

Section: Phenotypic Changes In Prdx6 à/à Lecs Resemble Tgfb-induced Cmentioning

confidence: 98%

“…So, DCF fluorescence reflects the overall oxidative stress in cells. 43 Next, to establish whether the expression and release of bioactive TGFb is increased, we performed RT-PCR, Western analysis, and E max ELISA Assay (Promega). The culture supernatant of Prdx6 À/À LECs contained significantly higher bioactive TGFb (Figure 5c).…”

Section: Activation Of Tgfb In Prdx6-depleted Lecs Is Associated Withmentioning

confidence: 99%

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Impaired homeostasis and phenotypic abnormalities in Prdx6−/−mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFβ

et al. 2005

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PRDX6, a member of the peroxiredoxins (PRDXs) family, is a key player in the removal of reactive oxygen species (ROS). Using targeted inactivation of the Prdx6 gene, we present evidence that the corresponding protein offsets the deleterious effects of ROS on lens epithelial cells (LECs) and regulates gene expression by limiting its levels. PRDX6-depleted LECs displayed phenotypic alterations and elevated a-smooth muscle actin and big-h3 expression (markers for cataractogenesis), indistinguishable from transforming growth factor b (TGFb)-induced changes. Biochemical assays disclosed enhanced levels of ROS, as well as high expression and activation of TGFb1 in Prdx6 À/À LECs. A CAT assay revealed transcriptional repression of lens epithelium-derived growth factor (LEDGF), HSP27, and aB-crystallin promoter activities in these cells. A gel mobility shift assay demonstrated the attenuation of LEDGF binding to heat shock or stress response elements present in these genes. A supply of PRDX6 toPrdx6 À/À LECs reversed these changes. Based on the above data, we propose a rheostat role for PRDX6 in regulating gene expression by controlling the ROS level to maintain cellular homeostasis.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 95%

Section: Phenotypic Changes In Prdx6 à/à Lecs Resemble Tgfb-induced Cmentioning

confidence: 98%

Section: Activation Of Tgfb In Prdx6-depleted Lecs Is Associated Withmentioning

confidence: 99%

See 2 more Smart Citations

Impaired homeostasis and phenotypic abnormalities in Prdx6−/−mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFβ

et al. 2005

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“…The two proteins, DJ-1 and PRDX6, act against oxidative stress: DJ-1 as a quencher for ROS (Junn et al, 2005) and PRDX6 as a catalyser of the H 2 O 2 reduction (Wang et al, 2003). ROS-driven oxidative stress influences many biological processes, including cell survival and death.…”

Section: Protein Involved In Oxidative Resistancementioning

confidence: 99%

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Guillemin

Jurie

Cassar-Malek

et al. 2011

Animal

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Some proteins have been revealed as biomarkers for beef tenderness by previous studies. These markers could be used in immunological tests to predict beef tenderness, in living animals as well as in carcasses. It is well known that rearing practices modify the amounts of mRNA and proteins. Therefore, the reliability of protein tests could be affected by livestock and biological effects such as production systems, breed, muscle and animal type. This study analysed the effects of animal and muscle type on 24 proteins. The animals studied were 67 young bulls and 44 steers of the Charolais breed, and muscles were Longissimus thoracis and Semitendinosus. Protein amounts were determined by Dot blot, an immunological technique. Results showed that expressions of 20 proteins were influenced by animal and/or muscle type. These results could lead to modifications and adaptations of prediction tests according to rearing practice, bovine breed and beef cut.

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Notch3 regulates ferroptosis via ROS‐induced lipid peroxidation in NSCLC cells

Xiao

Liu

et al. 2022

FEBS Open Bio

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Ferroptosis is type of programmed cell death, which is known to be involved in certain cancers. Notch3 signaling is reported to be involved in the tumorigenesis of non‐small‐cell lung cancer (NSCLC) and regulates iron metabolism, lipid synthesis, and oxidative stress in some tissues. However, whether Notch3 signaling regulates ferroptosis is unclear. In this study, we found that ferroptosis inhibitors, ferrostatin‐1 and liproxstatin‐1, protected against cell death induced by Notch3 knockdown and that Notch3 knockdown initiated ferroptosis in NSCLC cells by increasing reactive oxygen species (ROS) levels, lipid peroxidation, and Fe2+ levels, accompanied by downregulation of glutathione peroxidase 4 (GPX4) and peroxiredoxin6 (PRDX6). Conversely, Notch3 intracellular domain overexpression suppressed erastin‐induced ferroptosis, which was synergistically enhanced by MJ33 in H1299 cells via a decrease in ROS levels and lipid peroxidation, accompanied by upregulation of GPX4 and PRDX6. Moreover, Notch3 knockdown decreased tumorigenesis in vivo with downregulation of GPX4 and PRDX6. In summary, here we have identified Notch3 as a potential negative regulator of ferroptosis in NSCLC.

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Mice with Targeted Mutation of Peroxiredoxin 6 Develop Normally but Are Susceptible to Oxidative Stress

Cited by 294 publications

References 50 publications

Impaired homeostasis and phenotypic abnormalities in Prdx6−/−mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFβ

Impaired homeostasis and phenotypic abnormalities in Prdx6−/−mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFβ

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Notch3 regulates ferroptosis via ROS‐induced lipid peroxidation in NSCLC cells

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