The role of S-nitrosylation of PFKM in regulation of glycolysis in ovarian cancer cells

被引：29

作者：

Gao, Wenwen ^{[1
]}

Huang, Mengqiu ^{[1
]}

Chen, Xi ^{[1
]}

Chen, Jianping ^{[1
]}

Zou, Zhiwei ^{[1
,2
]}

Li, Linlin ^{[3
]}

Ji, Kaiyuan ^{[1
]}

Nie, Zhirui ^{[4
]}

Yang, Bingsheng ^{[5
]}

Wei, Zibo ^{[1
]}

Xu, Pengfei ^{[1
]}

Jia, Junshuang ^{[1
]}

Zhang, Qianbing ^{[1
]}

Shen, Hongfen ^{[1
]}

Wang, Qianli ^{[6
]}

Li, Keyi ^{[1
]}

Zhu, Lingqun ^{[7
]}

Wang, Meng ^{[1
]}

Ye, Shuangyan ^{[1
]}

Zeng, Sisi ^{[1
]}

Lin, Ying ^{[1
]}

Rong, Zhili ^{[1
]}

Xu, Yang ^{[1
,8
]}

Zhu, Peng ^{[9
]}

Zhang, Hui ^{[10
,11
,12
]}

Hao, Bingtao ^{[1
,13
]}

Liu, Qiuzhen ^{[1
,14
]}

机构：

[1] Southern Med Univ, Sch Basic Med Sci, Canc Res Inst, Guangdong Prov Key Lab Canc Immunotherapy,Guangzh, Guangzhou 510515, Peoples R China

[2] Southern Med Univ, Southern Hosp, Zengcheng Branch, Guangzhou 528308, Peoples R China

[3] Zhengzhou Univ, Affiliated Hosp 1, Zhengzhou 450001, Henan, Peoples R China

[4] Guangzhou Panyu Cent Hosp, Guangzhou 511400, Peoples R China

[5] Southern Med Univ, Pearl River Hosp, Guangzhou 528308, Peoples R China

[6] Zhengzhou Univ, Henan Canc Hosp, Zhengzhou 450003, Henan, Peoples R China

[7] Guangzhou Concord Canc Ctr, Guangzhou 528308, Peoples R China

[8] Sun Yat Sen Univ, Affiliated Hosp 8, Shenzhen 518033, Guangdong, Peoples R China

[9] Shenzhen Pingshan Peoples Hosp, Cent Lab, Shenzhen 518118, Peoples R China

[10] Guangdong Univ Technol, Sch Biomed & Pharmaceut Sci, Guangzhou 510006, Peoples R China

[11] Sun Yat Sen Univ, Metab Innovat Ctr, Zhongshan Sch Med, Guangzhou 510080, Guangdong, Peoples R China

[12] Sun Yat Sen Univ, Ctr Precis Med, Platform Metabol, Guangzhou 510080, Guangdong, Peoples R China

[13] Zhengzhou Univ, Henan Univ, Henan Prov Peoples Hosp,Peoples Hosp, Med Genet Inst Henan Prov,Henan Prov Key Lab Gene, Guangzhou 510515, Peoples R China

[14] Southern Med Univ, Pingshan Gen Hosp, Shenzhen 518118, Peoples R China

来源：

CELL DEATH & DISEASE | 2021年 / 12卷 / 04期

基金：

中国国家自然科学基金;

关键词：

SKELETAL-MUSCLE; 6-PHOSPHOFRUCTO-1-KINASE; NITRIC-OXIDE SYNTHASE; LACTIC-ACID; METABOLISM; ACTIVATION; PHOSPHORYLATION; MECHANISMS; ENERGY; PTEN;

D O I：

10.1038/s41419-021-03681-0

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页数：14

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