@article{88181,
  keywords = {Animals, Models, Molecular, Humans, Cell Proliferation, Enzyme Activation, Mice, Cell Line, Tumor, Glycolysis, Neoplasms, Gene Knockdown Techniques, Binding, Competitive, Mice, Nude, Glyceric Acids, Phosphoglycerate Mutase, Gluconates, Glucosephosphate Dehydrogenase},
  author = {Taro Hitosugi and Lu Zhou and Shannon Elf and Jun Fan and Hee-Bum Kang and Jae Ho Seo and Changliang Shan and Qing Dai and Liang Zhang and Jianxin Xie and Ting-Lei Gu and Peng Jin and Masa Ale{\v c}kovi{\'c} and Gary LeRoy and Yibin Kang and Jessica Sudderth and Ralph DeBerardinis and Chi-Hao Luan and Georgia Chen and Susan Muller and Dong Shin and Taofeek Owonikoko and Sagar Lonial and Martha Arellano and Hanna Khoury and Fadlo Khuri and Benjamin Lee and Keqiang Ye and Titus Boggon and Sumin Kang and Chuan He and Jing Chen},
  title = {Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth.},
  abstract = {<p>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.</p>
},
  year = {2012},
  journal = {Cancer Cell},
  volume = {22},
  pages = {585-600},
  month = {11/2012},
  issn = {1878-3686},
  doi = {10.1016/j.ccr.2012.09.020},
  language = {eng},
}