Oncotarget

Research Perspectives:

Pyruvate kinase M2 regulates glucose metabolism by functioning as a coactivator for hypoxia-inducible factor 1 in cancer cells

Weibo Luo, Gregg L. Semenza _

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Oncotarget. 2011; 2:551-556. https://doi.org/10.18632/oncotarget.299

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Abstract

Weibo Luo1,2 and Gregg L. Semenza1,2,3,4,5,6,7

1 Vascular Program, Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, USA

2 McKusick-Nathans Institute of Genetic Medicine, The Johns Hopkins University School of Medicine, Baltimore, USA

3 Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, USA

4 Department of Oncology, The Johns Hopkins University School of Medicine, Baltimore, USA

5 Department of Pediatrics, The Johns Hopkins University School of Medicine, Baltimore, USA

6 Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, USA

7 Department of Radiation Oncology, The Johns Hopkins University School of Medicine, Baltimore, USA

Received: June 24, 2011; Accepted: June 24, 2011; Published: June 25, 2011;

Correspondence:

Gregg L. Semenza, email:

Abstract

Cancer cells feature altered glucose metabolism that allows their rapid growth. They consume large amounts of glucose to produce lactate, even in the presence of ample oxygen, which is known as the Warburg effect. Pyruvate kinase M2 (PKM2) contributes to the Warburg effect by previously unknown mechanisms. Hypoxia-inducible factor 1 (HIF-1) mediates PKM2 gene transcription and glucose reprogramming in cancer cells. The recent discovery of novel physical and functional interactions between PKM2 and HIF-1 in cancer cells has provided insight into molecular mechanisms underlying the Warburg effect.


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