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Review
. 2012 Feb 13;209(2):211-5.
doi: 10.1084/jem.20120162.

Targeting glucose metabolism for cancer therapy

Robert B Hamanaka  1 , Navdeep S Chandel
Affiliations
Review

Targeting glucose metabolism for cancer therapy

Robert B Hamanaka et al. J Exp Med. .

Abstract

Cellular transformation is associated with the reprogramming of cellular pathways that control proliferation, survival, and metabolism. Among the metabolic changes exhibited by tumor cells is an increase in glucose metabolism and glucose dependence. It has been hypothesized that targeting glucose metabolism may provide a selective mechanism by which to kill cancer cells. In this minireview, we discuss the benefits that high levels of glycolysis provide for tumor cells, as well as several key enzymes required by cancer cells to maintain this high level of glucose metabolism. It is anticipated that understanding which metabolic enzymes are particularly critical for tumor cell proliferation and survival will identify novel therapeutic targets.

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Figures

Figure 1.
Figure 1.
Potential targets for cancer therapy found within metabolic pathways involved in glucose metabolism. The PPP is shaded in blue, and glycolysis is shaded in yellow. Red text is used to denote potential therapeutic targets. The green arrow indicates positive regulation of PFK1.
See this image and copyright information in PMC

References

    1. Anastasiou D., Poulogiannis G., Asara J.M., Boxer M.B., Jiang J.K., Shen M., Bellinger G., Sasaki A.T., Locasale J.W., Auld D.S., et al. 2011. Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science. 334:1278–1283 10.1126/science.1211485 - DOI - PMC - PubMed
    1. Bluemlein K., Grüning N.M., Feichtinger R.G., Lehrach H., Kofler B., Ralser M. 2011. No evidence for a shift in pyruvate kinase PKM1 to PKM2 expression during tumorigenesis. Oncotarget. 2:393–400 - PMC - PubMed
    1. Chan D.A., Sutphin P.D., Nguyen P., Turcotte S., Lai E.W., Banh A., Reynolds G.E., Chi J.T., Wu J., Solow-Cordero D.E., et al. 2011. Targeting GLUT1 and the Warburg effect in renal cell carcinoma by chemical synthetic lethality. Sci. Transl. Med. 3:ra70 - PMC - PubMed
    1. Christofk H.R., Vander Heiden M.G., Harris M.H., Ramanathan A., Gerszten R.E., Wei R., Fleming M.D., Schreiber S.L., Cantley L.C. 2008a. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature. 452:230–233 10.1038/nature06734 - DOI - PubMed
    1. Christofk H.R., Vander Heiden M.G., Wu N., Asara J.M., Cantley L.C. 2008b. Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature. 452:181–186 10.1038/nature06667 - DOI - PubMed

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