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Dihydroartemisinin represses esophageal cancer glycolysis by down-regulating pyruvate kinase M2.

Abstract
Esophageal cancer, especially esophageal squamous cell carcinoma (ESCC) threatens so many lives in China every year. Traditional treatment of ESCC has usually been disappointing. The development of novel therapy is worth investigation. We have previously demonstrated that dihydroartemisinin (DHA) has anticancer effect on esophageal cancer. However, the mechanism has not been completely known. In this present study, we explored the effect of DHA on cancer cell glycolysis, also known as Warburg effect. Pyruvate kinase M2 (PKM2) is a key regulatory factor of glycolysis, and our results showed that it is significantly overexpressed in patients with ESCC and ESCC cell lines. In DHA treatment cells, PKM2 was down-regulated and lactate product and glucose uptake were inhibited. Overexpression of PKM2 by lentiviral transfection abrogated the inhibition effect of DHA. These results suggested that DHA might repress esophageal cancer glycolysis partly by down-regulating PKM2 expression. We believe that DHA might be a prospective agent against esophageal cancer.
AuthorsShumin Li, Peng Huang, Junqing Gan, Xiaodong Ling, Xiaoxue Du, Yuanyu Liao, Lisha Li, Yu Meng, Yanjing Li, Yuxian Bai
JournalEuropean journal of pharmacology (Eur J Pharmacol) Vol. 854 Pg. 232-239 (Jul 05 2019) ISSN: 1879-0712 [Electronic] Netherlands
PMID31004604 (Publication Type: Journal Article)
CopyrightCopyright © 2019 Elsevier B.V. All rights reserved.
Chemical References
  • Artemisinins
  • Carrier Proteins
  • Membrane Proteins
  • Thyroid Hormones
  • artenimol
  • Glucose
Topics
  • Artemisinins (metabolism, pharmacology)
  • Biological Transport (drug effects)
  • Carrier Proteins (chemistry, genetics, metabolism)
  • Cell Line, Tumor
  • Down-Regulation (drug effects)
  • Esophageal Neoplasms (pathology)
  • Glucose (metabolism)
  • Glycolysis (drug effects)
  • Humans
  • Membrane Proteins (chemistry, genetics, metabolism)
  • Models, Molecular
  • Protein Domains
  • Thyroid Hormones (chemistry, genetics, metabolism)
  • Thyroid Hormone-Binding Proteins

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