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-Ketoglutarate Dehydrogenase mRNA Levels in Three Human Cell Types
Manuscript received 6 August 1997. Initial reviews completed 26 September 1997. Revision accepted 11 December 1997.
Department of Molecular Biology and * Department of Psychiatry, Vanderbilt University, Nashville, TN 37235
Reductions in the levels and activities of enzymes that utilize thiamine diphosphate (ThDP) as a cofactor are thought to be responsible for the tissue damage suffered during thiamine deficiency. Although loss of cofactor can account in part for loss of enzyme activity, thiamine and its phosphorylated derivatives may also regulate the expression of the genes encoding these proteins. To examine this possibility, steady-state mRNA levels for three ThDP-dependent enzymes were measured in human fibroblasts, lymphoblasts and neuroblastoma cells cultured under conditions of thiamine sufficiency and deficiency. In all three cell types, the mRNA levels of transketolase and the E1
subunit of pyruvate dehydrogenase complex were lower in thiamine-deficient cultures. In contrast, mRNA levels for a ThDP-binding subunit of 
-ketoglutarate dehydrogenase, the E1 subunit did not differ. These results indicate that thiamine or a thiamine metabolite regulates the expression in humans of some, but not all, genes encoding ThDP-utilizing enzymes.
-ketoglutarate dehydrogenase,
pyruvate dehydrogenase complex,
gene regulation,
thiamine,
humans.
The Journal of Nutrition Vol. 128 No. 4 April 1998,
pp. 683-687
Copyright ©1998 by the American Society for Nutritional Sciences
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