Summary
The relation between the phosphorylation of deoxyglucose (2-DG) and levels of adenine nucleotides was investigated in endogenously respiring Ehrlich Lettré ascites cells pretreated with various inhibitors. Pretreatment with the respiratory inhibitor, rotenone, caused a 70% decrease in 2-deoxyglucose-6-phosphate formation. The sources of energy for 2-DG phosphorylation in the presence of rotenone were found to be endogenous reserves of adenine nucleotides, as well as a limited residual respiration. Phosphorylation of 2-DG in the presence of 10-4 m dinitrophenol was 70% of normal, and was abolished by addition of rotenone. Dinitrophenol was shown to induce a stoichiometric transamination of alanine to pyruvate, and cause a marked increase of 14CO2 and pyruvate-14C from alanine-14C or glutamic acid-14C. The evidence suggests that substrate level phosphorylation from α-oxoglutarate and subsequent formation of adenosine triphosphate by a decarboxylation reaction is at least partially responsible for the phosphorylation of 2-DG in uncoupled cells.
Footnotes
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↵1 This investigation was supported by USPHS Research Grant Number CA-22, 936-02 from the National Cancer Institute.
- Received September 2, 1966.
- Accepted June 23, 1967.
- ©1967 American Association for Cancer Research.