Regulation of Glycerol Phosphate Dehydrogenase and Lactate Dehydrogenase Activity by Forskolin and Dibutyryl Cyclic AMP in the C6 Glial Cells

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Abstract
We have compared the effects of norepinephrine, forskolin, and dibutyryl cyclic AMP (Bt2cAMP) on the regulation of the cytosolic enzyme glycerol phosphate dehydrogenase (GPDH) in the C6 rat glioma cell line. Forskolin and Bt2cAMP elicit a dose‐dependent increase in the levels of the enzyme that was, however, unaffected by norepinephrine. The half‐maximal effect of forskolin was obtained at 7–8 μM. and the effect was maximal at 30 μM. Dexametha‐sone at a 50 nM concentration produced a two‐ to sixfold induction of GPDH after 48 h. The combination of dexa‐methasone with forskolin or Bt2cAMP leads to an elevation in GPDH levels that is higher than that produced by one of the compounds alone. This potentiation is found when both agents are added together with or after the glucocorticoid. The increase in uninduced and dexamethasone‐induced GPDH activity was blocked by cycloheximide and actino‐mycin D, indicating that de novo protein and RNA synthesis are required. The activity of cytosolic lactate dehydrogenase activity did not change after incubation with dexa‐methasone, but increased with forskolin or Bt2cAMP.

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