2. Academic Validation
  3. S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway

S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway

  • Cell Death Dis. 2019 Apr 15;10(5):329. doi: 10.1038/s41419-019-1561-x.
Yihan Zhang 1 2 3,  Changning Sun 1 2 3,  Guokai Xiao 1 2 3,  Hui Shan 1 2 3,  Luyao Tang 1 2 3,  Yujiao Yi 1 2 3,  Wengong Yu 4 5 6,  Yuchao Gu 7 8 9
Affiliations

Affiliations

  • 1 Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, 5 Yushan Road, Qingdao, 266003, China.
  • 2 Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266200, China.
  • 3 Key Laboratory of Glycoscience & Glycotechnology of Shandong Province, Qingdao, 266003, China.
  • 4 Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, 5 Yushan Road, Qingdao, 266003, China. yuwg66@ouc.edu.cn.
  • 5 Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266200, China. yuwg66@ouc.edu.cn.
  • 6 Key Laboratory of Glycoscience & Glycotechnology of Shandong Province, Qingdao, 266003, China. yuwg66@ouc.edu.cn.
  • 7 Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, 5 Yushan Road, Qingdao, 266003, China. guych@ouc.edu.cn.
  • 8 Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266200, China. guych@ouc.edu.cn.
  • 9 Key Laboratory of Glycoscience & Glycotechnology of Shandong Province, Qingdao, 266003, China. guych@ouc.edu.cn.
PMID: 30988280 DOI: 10.1038/s41419-019-1561-x
Abstract

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 (H2O2), 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 H2O2. H2O2 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.

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