Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P30044 (
antioxidant enzyme
)
8,037
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Protein S
-nitrosylation, the redox-based posttranslational modification of a cysteine thiol by the attachment of a nitric oxide (NO) group, is responsible for a variety of signaling effects. Dysregulation of S-nitrosylation may be directly linked to cancer apoptotic resistance and cancer therapy outcomes, emphasizing the importance of S-nitrosylation in cancer. Peroxiredoxin-2 (Prdx2), an
antioxidant enzyme
, plays an important role in the protection of cancer cells from oxidative radical damage caused by hydrogen dioxide (H
2
O
2
), which is a potential target for cancer therapy. Our studies showed that, as an endogenous NO carrier, S-nitrosoglutathione (GSNO) induced apoptosis in lung cancer cells via nitrosylating Prdx2. The nitrosylation of Prdx2 at Cys51 and Cys172 sites disrupted the formation of Prdx2 dimer and repressed the Prdx2 antioxidant activity, causing the accumulation of endogenous H
2
O
2
. H
2
O
2
activated AMPK, which then phosphorylated SIRT1 and inhibited its deacetylation activity toward p53 in A549 cells or FOXO1 in NCI-H1299 cells. Taken together, our results elucidate the roles and mechanisms of Prdx2 S-nitrosylation at Cys51 and Cys172 sites in lung cancer cells apoptosis and this finding provides an effective lung cancer treatment strategy for managing aberrant Prdx2 activity in lung cancers.
...
PMID:S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway. 3098 80
Protein S
-nitrosylation, which refers to the redox-based posttranslational modification of a cysteine thiol by the attachment of a nitric oxide (NO) group, modulates a variety of enzyme activities. Monodehydroascorbate reductase (MDHAR) is essential for ascorbic acid (AsA) regeneration, which protects plant cells against damage by detoxifying reactive oxygen species (ROS). However, the relationship between S-nitrosylation and the role of tomato MDHAR (SlMDHAR) under salt stress remains unclear. In this paper, we show that the SlMDHAR mRNA expression, enzyme activity, protein level, total S-nitrosylated proteins and S-nitrosylated SlMDHAR protein level in tomato leaves significantly increase after NaCl treatment. To further evaluate the function of SlMDHAR under salt stress, overexpressed transgenic tobacco plants were used. The germination rate and root length of the overexpressed plants under NaCl stress were significantly higher than those of wild-type (WT) plants. Meanwhile, the transgenic plants had lower ROS accumulation, higher
antioxidant enzyme
activities and AsA-DHA ratio, more proline and soluble sugar contents than those in WT plants under salt stress. With a higher expression of stress-related genes, the transgenic plants demonstrated lower Na
+
and higher K
+
accumulation compared with WT plants. The NO accumulation and S-nitrosylated MDHAR level were higher in transgenic plants than in WT plants after NaCl treatment. In contrast, virus-induced gene silencing (VIGS) of SlMDHAR tomato plants showed enhanced sensitivity to salt stress and have lower S-nitrosylated MDHAR protein. These results suggested that SlMDHAR confers salt stress tolerance by alleviating oxidative damage probably involving the S-nitrosylation of MDHAR.
...
PMID:Overexpression of SlMDHAR in transgenic tobacco increased salt stress tolerance involving S-nitrosylation regulation. 3290 Apr 47
