Glucose- and insulin-independent induction of ATP citrate lyase in primary cultures of rat hepatocytes

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Abstract
ATP citrate lyase, which is involved in the translocation of the lipogenic precursor acetyl-CoA from mitochondria to cytosol, was studied in primary cultures of hepatocytes from adult rats. After an initial decrease at the first day of culture the enzyme activity was nearly constant during the following days. It could be enhanced between 24h and 48 h in culture about 1.5-fold by elevation of the insulin concentration to 10-7mol/1.22-fold by elevation of the glucose concentration from 5 to 25 mmol/l and 3.5-fold by simultaneous elevation of insulin and glucose. The increase of activity was about linear with time for 24 h and could be blocked by cycloheximide, which inhibits protein synthesis at the translational level. Both observations suggest that the enhancement of activity was due to induction rather than to activation by interconversion. The glucose-dependent induction was furthermore evidenced by immunotitration which indicated a parallel increase of activity and enzyme protein.

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