The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Breast cancer stem cells rely on fermentative glycolysis and are sensitive to 2-deoxyglucose treatment
Open accessAbstract
A number of studies suggest that cancer stem cells are essential for tumour growth, and failure to target these cells can result in tumour relapse. As this population of cells has been shown to be resistant to radiation and chemotherapy, it is essential to understand their biology and identify new therapeutic approaches. Targeting cancer metabolism is a potential alternative strategy to counteract tumour growth and recurrence. Here we applied a proteomic and targeted metabolomic analysis in order to point out the main metabolic differences between breast cancer cells grown as spheres and thus enriched in cancer stem cells were compared with the same cells grown in adherent differentiating conditions. This integrated approach allowed us to identify a metabolic phenotype associated with the stem-like condition and shows that breast cancer stem cells (BCSCs) shift from mitochondrial oxidative phosphorylation towards fermentative glycolysis. Functional validation of proteomic and metabolic data provide evidences for increased activities of key enzymes of anaerobic glucose fate such as pyruvate kinase M2 isoform, lactate dehydrogenase and glucose 6-phopshate dehydrogenase in cancer stem cells as well as different redox status. Moreover, we show that treatment with 2-deoxyglucose, a well known inhibitor of glycolysis, inhibits BCSC proliferation when used alone and shows a synergic effect when used in combination with doxorubicin. In conclusion, we suggest that inhibition of glycolysis may be a potentially effective strategy to target BCSCs.
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Cites
Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
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Hypoxia — a key regulatory factor in tumour growth
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The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
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Keith, B., & Simon, M. C. (2007) · Cell · doi:10.1016/j.cell.2007.04.019 · Cited by 1,179
Serine is a natural ligand and allosteric activator of pyruvate kinase M2
Chaneton, B., Hillmann, P., Zheng, L., Martin, A. C. L., Maddocks, O. D. K., Chokkathukalam, A., Coyle, J. E., Jankevics, A., Holding, F. P., Vousden, K. H., et al. (2012) · Nature · doi:10.1038/nature11540 · Cited by 661
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“Indeed, Figure 1 Data quality evaluation, Venn analysis, and expression ratios for significantly regulated proteins in BCSCs compared with SDACs.”
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Cited by
Peiris-Pagès, M., Martinez-Outschoorn, U. E., Pestell, R. G., Sotgia, F., & Lisanti, M. P. (2016) · Breast Cancer Research · doi:10.1186/s13058-016-0712-6 · Cited by 465
Ganapathy-Kanniappan, S. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1556578 · Cited by 216
O’Neill, S., Porter, R. K., McNamee, N., Martinez, V. G., & O’Driscoll, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-39789-9 · Cited by 93
Metadata
- Authors
- Ciavardelli, D., Rossi, C., Barcaroli, D., Volpe, S., Consalvo, A., Zucchelli, M., De Cola, A., Scavo, E., Carollo, R., D'Agostino, D., Forlì, F., D'Aguanno, S., Todaro, M., Stassi, G., Di Ilio, C., De Laurenzi, V, & Urbani, A.
- Venue
- Cell Death & Disease
- Published
- 2014-07-17
- Volume
- 5
- Issue
- 7
- Pages
- e1336-e1336
- ISSN
- 2041-4889 (ISSN-L)
- OpenAlex
- W2028303721
- Cited by
- 269
- References
- 6
- FWCI
- 7.00
- Type
- journal article
- Language
- en
- Open access
- gold
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