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MIT researchers discover an unexpected twist in cancer metabolism
Date:9/16/2010

o be a linear, nine-step process by which a cell turns one molecule of glucose into two molecules of pyruvate, an organic compound with three carbon atoms. That pyruvate is usually fed into the second phase of glucose metabolism.

"Everyone takes it for granted that this is how it works," says Vander Heiden, who did this research as a postdoctoral fellow in the lab of Harvard Medical School Professor Lewis Cantley, senior author of the paper. But the new study shows that "there is another way it can work, and this other way seems to be at play in proliferating cells." That could include rapidly dividing embryonic cells as well as cancer cells.

Scientists already knew that cancer cells replace one type of a key metabolic enzyme known as pyruvate kinase with another. Both versions of the enzyme (PKM1 and PKM2) catalyze the very last step of glycolysis, which is the transformation of a compound called PEP to the final product, pyruvate.

In the new study, the researchers found that PEP is involved in a previously unknown feedback loop that bypasses the final step of glycolysis. In cancer cells, PKM2 is not very active, causing PEP to accumulate. That excess PEP activates an enzyme called PGAM, which catalyzes an earlier step in glycolysis. When PGAM receives that extra boost, it produces even more PEP, creating a positive feedback loop in which the more PEP a cell has, the more it makes.

The most important result of this loop is that the cell generates a large pool of another chemical that is formed during an intermediate step of the reaction chain. Vander Heiden believes this compound, called 3-phosphoglycerate, is diverted into synthetic pathways such as the production of DNA, which can become part of a new cancer cell. In future studies, he plans to investigate how that diversion occurs.

This study suggests that drugs that activate PKM2 could be promising cancer treatments, says Vander Heiden. If PKM2 were highly activate
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Contact: Jennifer Hirsch
jfhirsch@mit.edu
617-253-1682
Massachusetts Institute of Technology
Source:Eurekalert

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