2. Academic Validation
  3. Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth

Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth

  • Cancer Cell. 2012 Nov 13;22(5):585-600. doi: 10.1016/j.ccr.2012.09.020.
Taro Hitosugi 1,  Lu Zhou,  Shannon Elf,  Jun Fan,  Hee-Bum Kang,  Jae Ho Seo,  Changliang Shan,  Qing Dai,  Liang Zhang,  Jianxin Xie,  Ting-Lei Gu,  Peng Jin,  Masa Alečković,  Gary LeRoy,  Yibin Kang,  Jessica A Sudderth,  Ralph J DeBerardinis,  Chi-Hao Luan,  Georgia Z Chen,  Susan Muller,  Dong M Shin,  Taofeek K Owonikoko,  Sagar Lonial,  Martha L Arellano,  Hanna J Khoury,  Fadlo R Khuri,  Benjamin H Lee,  Keqiang Ye,  Titus J Boggon,  Sumin Kang,  Chuan He,  Jing Chen
Affiliations

Affiliation

  • 1 Department of Hematology and Medical Oncology, Winship Cancer Institute, Emory University School of Medicine, Atlanta, GA 30322, USA.
PMID: 23153533 DOI: 10.1016/j.ccr.2012.09.020
Abstract

It is unclear how Cancer cells coordinate glycolysis and biosynthesis to support rapidly growing tumors. We found that the glycolytic Enzyme phosphoglycerate mutase 1 (PGAM1), commonly upregulated in human cancers due to loss of TP53, contributes to biosynthesis regulation in part by controlling intracellular levels of its substrate, 3-phosphoglycerate (3-PG), and product, 2-phosphoglycerate (2-PG). 3-PG binds to and inhibits 6-phosphogluconate dehydrogenase in the oxidative pentose phosphate pathway (PPP), while 2-PG activates 3-phosphoglycerate dehydrogenase to provide feedback control of 3-PG levels. Inhibition of PGAM1 by shRNA or a small molecule inhibitor PGMI-004A results in increased 3-PG and decreased 2-PG levels in Cancer cells, leading to significantly decreased glycolysis, PPP flux and biosynthesis, as well as attenuated cell proliferation and tumor growth.

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