Monitoring the switch: The warburg effect and targeted proteomic analysis of cancer metabolism

  1. Get@NRC: Monitoring the switch: The warburg effect and targeted proteomic analysis of cancer metabolism (Opens in a new window)
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Journal titleCurrent Proteomics
Pages2639; # of pages: 14
Subjectglucose; glucose 6 phosphate dehydrogenase; hexokinase; hexokinase 2; hypoxia inducible factor 1; immunoglobulin enhancer binding protein; mammalian target of rapamycin; Myc protein; phosphatidylinositol 3 kinase; phosphatidylinositol 3,4,5 trisphosphate 3 phosphatase; protein kinase B; protein p53; pyruvate kinase; pyruvate kinase M2; reduced nicotinamide adenine dinucleotide phosphate; unclassified drug; alternative RNA splicing; apoptosis; article; cancer metabolism; cancer prognosis; cell metabolism; cell proliferation; computer model; computer prediction; fatty acid synthesis; functional proteomics; gene expression regulation; gene overexpression; gene targeting; glucose transport; glycolysis; human; liquid chromatography; liquid chromatography multiple reaction monitoring; malignant neoplastic disease; metabolic rate; metabolism; monitoring; nonhuman; nucleic acid synthesis; priority journal; protein protein interaction; tumor microenvironment; Warburg effect
AbstractCancer cells dramatically alter their metabolism in order to increase the production rate of intermediates required for nucleic and fatty acid biosynthesis in rapidly proliferating cells. While not well understood, dysregulation of oncogenes and tumour suppressors appears to result in the altered expression of specific isoforms of glycolysis proteins. A full understanding of glycolytic alterations in cancer through a systems biology approach requires tools to observe changes in the set of proteins that make up the glycolytic proteome. We propose that a targeted proteomics approach employing multiple reaction monitoring (MRM) is an excellent strategy to quantitatively monitor sets of proteins, such as those making up the glycolytic proteome. MRM is particularly well suited to proteins of glycolysis as they are of moderate to high abundance. Such systems-based efforts provide a means to understand the mechanisms for an altered glycolytic proteome in cancer, perhaps leading to novel drug targets and metabolic signatures for use in cancer prognosis. ©2012 Bentham Science Publishers.
Publication date
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Marine Biosciences (IMB-IBM)
Peer reviewedYes
NPARC number21269462
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Record identifier79abda0d-af9d-4dd8-a3e4-6e9d0802908f
Record created2013-12-12
Record modified2016-05-09
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