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Peer-reviewedCC BY-NC-NDActa pharmaceutica Sinica. B

Aspirin induces glycolytic reprogramming via lysine salicylation of ALDOA

  • Yanqiu Gong1
  • Li Gao2
  • Aolan Zhou2
  • Yuqi Wang2
  • Wenchen Pu3
  • Shuangyan Tan3
  • Shupan Guo2
  • Yanting He2
  • Xinyuan Wang2
  • Qinlu Peng2
  • Longlong Hu4
  • Yong Peng3
2 more authors
  • Haiyan Ren2
  • Lunzhi Dai2
4 affiliations
  1. 1Institute for Advanced Study, Chengdu University, Chengdu 610106, China
  2. 2National Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu 610041, China
  3. 3Center for Molecular Oncology, Frontiers Science Center for Disease-related Molecular Network, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu 610041, China
  4. 4Shanghai AB SCIEX Analytical Instrument Trading Co., Ltd., Shanghai 200335, China
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Abstract

Aspirin (ASA), a classical nonsteroidal anti-inflammatory drug, is known to inhibit glycolysis in cancer cells; however, the underlying mechanism remain incompletely understood. Here, we identify lysine salicylation (Ksa) as an ASA-dependent protein modification that suppresses glycolysis and proliferation in colorectal cancer cells. Specifically, ASA causes Ksa on the key glycolytic enzyme aldolase A (ALDOA), markedly reducing its enzymatic activity without altering protein level. Metabolomic analysis revealed that ASA impairs the conversion of fructose-1,6-bisphosphate (F16BP) to glyceraldehyde-3-phosphate (GAP), thereby disrupting glycolytic flux. In a xenograft mouse model, ASA administration not only inhibited tumor growth but also enhanced ALDOA Ksa level and blocked F16BP-to-GAP conversion. Besides, site-directed mutagenesis and genetic code expansion experiments confirmed that ALDOA K13sa is critical for ASA-mediated inhibition of glycolysis and cancer cell proliferation. Together, this study uncovers Ksa as an innovative mechanism by which ASA affects glycolysis and cancer cell proliferation, providing further insights into its potential role in cancer prevention and therapy.

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Cite

BibTeXRIS
BibTeX
@article{gong2026aspirin,
  title = {{Aspirin induces glycolytic reprogramming via lysine salicylation of ALDOA}},
  author = {Yanqiu Gong and Li Gao and Aolan Zhou and Yuqi Wang and Wenchen Pu and Shuangyan Tan and Shupan Guo and Yanting He and Xinyuan Wang and Qinlu Peng and Longlong Hu and Yong Peng and Haiyan Ren and Lunzhi Dai},
  journal = {Acta pharmaceutica Sinica. B},
  year = {2026},
  month = jul,
  doi = {10.1016/j.apsb.2026.07.002},
  url = {https://europepmc.org/article/PMC/PMC13729543},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - Aspirin induces glycolytic reprogramming via lysine salicylation of ALDOA
AU  - Yanqiu Gong
AU  - Li Gao
AU  - Aolan Zhou
AU  - Yuqi Wang
AU  - Wenchen Pu
AU  - Shuangyan Tan
AU  - Shupan Guo
AU  - Yanting He
AU  - Xinyuan Wang
AU  - Qinlu Peng
AU  - Longlong Hu
AU  - Yong Peng
AU  - Haiyan Ren
AU  - Lunzhi Dai
PY  - 2026
DA  - 2026/07/06
JO  - Acta pharmaceutica Sinica. B
DO  - 10.1016/j.apsb.2026.07.002
UR  - https://europepmc.org/article/PMC/PMC13729543
AB  - Aspirin (ASA), a classical nonsteroidal anti-inflammatory drug, is known to inhibit glycolysis in cancer cells; however, the underlying mechanism remain incompletely understood. Here, we identify lysine salicylation (Ksa) as an ASA-dependent protein modification that suppresses glycolysis and proliferation in colorectal cancer cells. Specifically, ASA causes Ksa on the key glycolytic enzyme aldolase A (ALDOA), markedly reducing its enzymatic activity without altering protein level. Metabolomic analysis revealed that ASA impairs the conversion of fructose-1,6-bisphosphate (F16BP) to glyceraldehyde-3-phosphate (GAP), thereby disrupting glycolytic flux. In a xenograft mouse model, ASA administration not only inhibited tumor growth but also enhanced ALDOA Ksa level and blocked F16BP-to-GAP conversion. Besides, site-directed mutagenesis and genetic code expansion experiments confirmed that ALDOA K13sa is critical for ASA-mediated inhibition of glycolysis and cancer cell proliferation. Together, this study uncovers Ksa as an innovative mechanism by which ASA affects glycolysis and cancer cell proliferation, providing further insights into its potential role in cancer prevention and therapy.
SN  - 2211-3835
SN  - 2211-3843
ER  -