The role of S-nitrosylation of PFKM in regulation of glycolysis in ovarian cancer cells
| Autor: | Lingqun Zhu, Peng Zhu, Pengfei Xu, Yang Xu, Mengqiu Huang, Hongfen Shen, Zhili Rong, Xi Chen, Keyi Li, Li Linlin, Hui Zhang, Kaiyuan Ji, Sisi Zeng, Shuangyan Ye, Zhiwei Zou, Jianping Chen, Bingtao Hao, Ying Lin, Wenwen Gao, Qianbing Zhang, Zibo Wei, Bingsheng Yang, Zhirui Nie, Meng Wang, Qiuzhen Liu, Qianli Wang, Jun-Shuang Jia |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Cancer Research Phosphofructokinase-1 Immunology Oncology and Carcinogenesis Carcinoma Ovarian Epithelial Article Malignant transformation Cell Line 03 medical and health sciences Cellular and Molecular Neuroscience Mice 0302 clinical medicine Rare Diseases Phosphofructokinase-1 Muscle Type Ovarian Epithelial Cell Line Tumor 2.1 Biological and endogenous factors Animals Humans Glycolysis Aetiology Cancer Tumor QH573-671 Chemistry Animal Nitrosylation Carcinoma Muscle Type Cell Biology Cancer metabolism Cell biology Ovarian Cancer Disease Models Animal 030104 developmental biology PFKM Tumor progression 030220 oncology & carcinogenesis Cancer cell Disease Models Female Biochemistry and Cell Biology Cytology Reprogramming Phosphofructokinase |
| Zdroj: | Cell Death & Disease Cell Death and Disease, Vol 12, Iss 4, Pp 1-14 (2021) Cell death & disease, vol 12, iss 4 |
| ISSN: | 2041-4889 |
| Popis: | One of the malignant transformation hallmarks is metabolism reprogramming, which plays a critical role in the biosynthetic needs of unchecked proliferation, abrogating cell death programs, and immunologic escape. However, the mechanism of the metabolic switch is not fully understood. Here, we found that the S-nitrosoproteomic profile of endogenous nitrogen oxide in ovarian cancer cells targeted multiple components in metabolism processes. Phosphofructokinase (PFKM), one of the most important regulatory enzymes of glycolysis, was S-nitrosylated by nitric oxide synthase NOS1 at Cys351. S-nitrosylation at Cys351 stabilized the tetramer of PFKM, leading to resist negative feedback of downstream metabolic intermediates. The PFKM-C351S mutation decreased the proliferation rate of cultured cancer cells, and reduced tumor growth and metastasis in the mouse xenograft model. These findings indicated that S-nitrosylation at Cys351 of PFKM by NOS1 contributes to the metabolic reprogramming of ovarian cancer cells, highlighting a critical role of endogenous nitrogen oxide on metabolism regulations in tumor progression. |
| Databáze: | OpenAIRE |
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