Journal
BIOCHEMICAL PHARMACOLOGY
Volume 92, Issue 1, Pages 22-30Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bcp.2014.07.005
Keywords
Glycolysis; Cancer; Cell death; GAPDH; Hexokinase
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Funding
- Waxweiler grant for cancer prevention research from the Action Lions Vaincre le Cancer
- Recherche Cancer et Sang foundation
- Recherches Scientifiques Luxembourg association
- Een Haerz fir kriibskrank Kanner association
- Action LIONS Vaincre le Cancer association
- Televie Luxembourg
- National Research Foundation of Korea (NRF) - Korea Government, Ministry of Science, ICT & Future Planning (MSIP) [2011-0030001]
- National Research Foundation of Korea [2011-0030001] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Cancer cells depend on an altered energy metabolism characterized by increased rates of both glycolysis and glutaminolysis. Accordingly, corresponding key metabolic enzymes are overexpressed or hyperactivated. As a result, this newly acquired metabolic profile determines most other cancer hallmarks including resistance to cell death. Recent findings highlighted metabolic enzymes as direct modulators of cell death pathways. Conversely, key mediators of cell death mechanisms are emerging as new binding partners of glycolytic actors; moreover, there is evidence that metabolic regulators relocalize to specific subcellular compartments or organelles to modulate various types of cell demise. The final outcome is the resistance against cell death programs. Current findings give a new meaning to metabolic pathways and allow understanding how they affect cancer-specific pathological alterations. Furthermore, they shed light on potentially targetable functions of metabolic actors to restore susceptibility of cancer cells to death. Here, we discuss an emerging interplay between cell metabolism and cell death, focusing on interactions that may offer new options of targeted therapies in cancer treatment involving more specifically hexokinases and glyceraldehyde-3-phoiphate dehydrogenase. (C) 2014 Elsevier Inc. All rights reserved.
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