Phosphoglycerate dehydrogenase diverts glycolytic flux and contributes to oncogenesis

Nature Genetics - Tập 43 Số 9 - Trang 869-874 - 2011
Jason W. Locasale1, Alexandra Grassian2, Tamar Melman1, Costas A. Lyssiotis1, Katherine Mattaini3, Adam J. Bass4, Gregory J. Heffron5, Christian M. Metallo6, Taru Muranen2, Hadar Sharfi1, Atsuo T. Sasaki7, Dimitrios Anastasiou7, Edouard Mullarky7, Natalie I. Vokes3, Mika Sasaki7, Rameen Beroukhim4, Gregory Stephanopoulos6, Azra H. Ligon4, Matthew Meyerson4, Andrea L. Richardson4, Lynda Chin4, Gerhard Wagner5, John M. Asara7, Joan S. Brugge2, Lewis C. Cantley7, Matthew G. Vander Heiden4
1Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA
2Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA
3Department of Biology, Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA
4Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts, USA
5Department of Biochemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA
6Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA
7Division of Signal Transduction, Beth Israel Deaconess Medical Center, Boston, Massachusetts, USA

Tóm tắt

Từ khóa


Tài liệu tham khảo

Vander Heiden, M.G., Cantley, L.C. & Thompson, C.B. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 324, 1029–1033 (2009).

DeBerardinis, R.J., Lum, J.J., Hatzivassiliou, G. & Thompson, C.B. The biology of cancer: metabolic reprogramming fuels cell growth and proliferation. Cell Metab. 7, 11–20 (2008).

Warburg, O., Posener, K. & Negelein, E. Ueber den Stoffwechsel der Tumoren. Biochem. Z. 152, 319–344 (1924).

Bodenhausen, G. & Ruben, D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69, 185–189 (1980).

Bismut, H., Caron, M., Coudray-Lucas, C. & Capeau, J. Glucose contribution to nucleic acid base synthesis in proliferating hepatoma cells: a glycine-biosynthesis-mediated pathway. Biochem. J. 308, 761–767 (1995).

Snell, K., Natsumeda, Y. & Weber, G. The modulation of serine metabolism in hepatoma 3924A during different phases of cellular proliferation in culture. Biochem. J. 245, 609–612 (1987).

Kit, S. The biosynthesis of free glycine and serine by tumors. Cancer Res. 15, 715–718 (1955).

de Koning, T.J. et al. L-serine in disease and development. Biochem. J. 371, 653–661 (2003).

Achouri, Y., Rider, M.H., Van Schaftingen, E. & Robbi, M. Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase. Biochem. J. 323, 365–370 (1997).

Lu, W., Bennett, B.D. & Rabinowitz, J.D. Analytical strategies for LC-MS-based targeted metabolomics. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 871, 236–242 (2008).

Beroukhim, R. et al. The landscape of somatic copy-number alteration across human cancers. Nature 463, 899–905 (2010).

Greshock, J. et al. A comparison of DNA copy number profiling platforms. Cancer Res. 67, 10173–10180 (2007).

Slamon, D.J. et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235, 177–182 (1987).

Luo, J., Solimini, N.L. & Elledge, S.J. Principles of cancer therapy: oncogene and non-oncogene addiction. Cell 136, 823–837 (2009).

Pollari, S. et al. Enhanced serine production by bone metastatic breast cancer cells stimulates osteoclastogenesis. Breast Cancer Res. Treat. 125, 421–430 (2011).

Foulkes, W.D., Smith, I.E. & Reis-Filho, J. Triple-negative breast cancer. N. Engl. J. Med. 363, 1938–1948 (2010).

Debnath, J. & Brugge, J.S. Modelling glandular epithelial cancers in three-dimensional cultures. Nat. Rev. Cancer 5, 675–688 (2005).

Schafer, Z.T. et al. Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment. Nature 461, 109–113 (2009).

Tabatabaie, L. et al. Novel mutations in 3-phosphoglycerate dehydrogenase (PHGDH) are distributed throughout the protein and result in altered enzyme kinetics. Hum. Mutat. 30, 749–756 (2009).

Thompson, C.B. Metabolic enzymes as oncogenes or tumor suppressors. N. Engl. J. Med. 360, 813–815 (2009).

Teperino, R., Schoonjans, K. & Auwerx, J. Histone methyl transferases and demethylases: can they link metabolism and transcription? Cell Metab. 12, 321–327 (2010).

Nomura, D.K. et al. Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis. Cell 140, 49–61 (2010).

Hara, K. et al. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J. Biol. Chem. 273, 14484–14494 (1998).

Vander Heiden, M.G. et al. Evidence for an alternative glycolytic pathway in rapidly proliferating cells. Science 329, 1492–1499 (2010).

Locasale, J.W. & Cantley, L.C. Altered metabolism in cancer. BMC Biol. 8, 88 (2010).

Eng, C.H., Yu, K., Lucas, J., White, E. & Abraham, R.T. Ammonia derived from glutaminolysis is a diffusible regulator of autophagy. Sci. Signal. 3, ra31 (2010).

Antoniewicz, M.R., Kelleher, J.K. & Stephanopoulos, G. Accurate assessment of amino acid mass isotopomer distributions for metabolic flux analysis. Anal. Chem. 79, 7554–7559 (2007).

Fernandez, C.A., Des Rosiers, C., Previs, S.F., David, F. & Brunengraber, H. Correction of 13C mass isotopomer distributions for natural stable isotope abundance. J. Mass Spectrom. 31, 255–262 (1996).

Richardson, A.L. et al. X chromosomal abnormalities in basal-like human breast cancer. Cancer Cell 9, 121–132 (2006).

Hoek, K. et al. Expression profiling reveals novel pathways in the transformation of melanocytes to melanomas. Cancer Res. 64, 5270–5282 (2004).

Rhodes, D.R. et al. ONCOMINE: a cancer microarray database and integrated data-mining platform. Neoplasia 6, 1–6 (2004).

Thông tin
Thông tin xuất bản

Nature Genetics

Tập 43 Số 9

869-874

Thông tin tác giả