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Cancer metabolism and mass spectrometry-based proteomics.

Authors
  • Zhou, Weidong1
  • Liotta, Lance A2
  • Petricoin, Emanuel F2
  • 1 Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, VA 20110, USA. Electronic address: [email protected]
  • 2 Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, VA 20110, USA.
Type
Published Article
Journal
Cancer letters
Publication Date
Jan 28, 2015
Volume
356
Issue
2 Pt A
Pages
176–183
Identifiers
DOI: 10.1016/j.canlet.2013.11.003
PMID: 24262660
Source
Medline
Keywords
License
Unknown

Abstract

Cancer metabolism has been extensively investigated by various tools, and the fact of diverse metabolic reprogramming in cancer cells has been gradually unveiled. In this review, we discuss some contributions in cancer metabolism by general proteomic analysis and post-translational modification analysis using mass spectrometry (MS) technique. Instead of following one or several metabolic enzymes/pathways, the current MS approach can quickly identify a large number of proteins and compare their expression levels in different samples, providing a potentially comprehensive picture of cancer metabolism. The MS analyses from pancreatic cancer cells support a hypothesis that hypoxia promotes cells in solid tumor to reprogram metabolic pathways in order to minimize the oxygen consumption. The oxidative stress in pancreatic cancer cells is lower than that in normal duct cells, and the cancer cells adaptively express less antioxidant proteins, contrary to claims that oxidative stress is higher in cancer cells. Separately, the MS analyses confirm that pyruvate kinase isoform 2 (PKM2) can be detected in both cancer and normal cells, disagreeing with report that tumor cells express exclusively PKM2. In addition, MS analyses from pancreatic cancer cells demonstrate that lactate dehydrogenase-B is significantly upregulated in pancreatic cancer cells, whereas previous reports show that lactate dehydrogenase-A is overexpressed and is responsible for lactate production in cancer cells. Lastly, the result from MS analysis suggests that the glutaminolysis in pancreatic cancer cells is different from that observed in glioblastoma cells.

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