Hepatic pyruvate dehydrogenase kinase activities during the starved-to-fed transition

Biochim Biophys Acta. 1992 Mar 16;1134(2):164-8. doi: 10.1016/0167-4889(92)90040-i.


Starvation for 48 h elicited a 74% increase in hepatic pyruvate dehydrogenase (PDH) kinase activity, measured directly by 32Pi-incorporation from [gamma-32P]ATP into a synthetic peptide corresponding to the major phosphorylation site on E1. The administration of chow ad libitum to previously-starved rats suppressed hepatic PDH kinase activity by only approx. 20% within 2 h of re-feeding, and the relatively high activity of PDH kinase was associated with continued suppression of PDC complex re-activation. Whereas there was no further decline in PDH kinase activity over the next 2 h, PDC re-activation to the fed value was observed during this time interval. PDH kinase activity decreased to fed values only after 8 h.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Fatty Acids, Nonesterified / blood
  • Female
  • Insulin / blood
  • Pyruvate Dehydrogenase Complex / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Starvation / enzymology*


  • Fatty Acids, Nonesterified
  • Insulin
  • Pyruvate Dehydrogenase Complex
  • Adenosine Triphosphate