Abstract
Increased activity of 6-phosphogluconate dehydrogenase was found in human colon tumors as compared to the adjacent unaffected mucosa. Glucose 1,6-diphosphate (Glc-1,6-P 2), an endogenous potent regulator of glucose metabolism, markedly inhibited the activity of 6-phosphogluconate dehydrogenase (6-PGD) in extracts of the normal and malignant human colon. Glc-1,6-P 2 also inhibited the activity of hexokinase in these extracts. The endogenous levels of Glc-1,6-P 2 in the colon and tumors were measured. Since the pentose cycle can be inhibited by Glc-1,6-P 2, means to increase endogenous levels of Glc-1,6-P 2 or to introduce it into cells, might result in antitumor effects.
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