January 1, 1970 (Vol. , No. )

Kevin Ahern

That cancer cells consume glucose at a higher rate than normal cells has been known for over 75 years. The Nobel Prize winning chemist, Otto Warburg, discovered the phenomenon that bears his name and he even thought it was the cause of cancer. We know now, of course, that mutation is. Pieces of the puzzle of how cancer cells reach such a high state of glucose oxidation have been slowly revealed over the years. Many cancer cells, for example, are known to have enhanced production (compared to normal cells) of cellular receptors that import glucose. Now, it appears, another significant player in the cancer scheme has been identified and it may help tie up several loose ends. As reported by a team led by Lewis Cantley in the most recent edition of Nature, the enzyme known as pyruvate kinase catalyzes the last step in the process of glycolysis (breakdown of glucose) and it appears that cancer cells predominantly use a form, known as PKM2, that normal adult cells do not use (but fetal cells do, interestingly). Further, when cancer cells are forced by deletion of PKM2 to use the pyruvate kinase of normal cells, their growth is curbed. More importantly, when cancer cells lacking PKM2 were injected back into mice, they appeared to have a significantly reduced ability to form tumors. PKM2, thus, may be important for the high metabolic use of glucose in cancer cells. Interestingly, a compound, known as DCA, which is known to regulate the enzyme that regulates pyruvate kinase is under investigation as an anti-cancer agent and may play a role in this system.



Note – DCA is NOT approved by the FDA for any treatments of any kind and is a dangerous compound. It is illegal to sell DCA and it should never be taken outside of FDA-approved clinical trials.

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