AMP-activated protein kinase (AMPK) is a cellular energy sensor that responds to low endogenous energy by stimulating fatty acid oxidation (through inactivation of acetyl-CoA carboxylase (ACC)) and food intake. Fasting generally stimulates phosphorylation of AMPK (pAMPK) and ACC (pACC), but it is unclear how AMPK and ACC react to a long-term fast (i.e. hibernation). We performed Western blots for total and pAMPK and pACC on tissues from a species of hibernator (Callospermophilus lateralis) after short-term summer fasting (1-5days) and long-term winter fasting (3months). Winter animals were sacrificed during hibernation at low body temperature (torpid, Tb~5°C) or at normal high Tb(euthermic, Tb~37°C). We found a general increase in pAMPK in most tissues (liver, muscle, and white adipose tissue (WAT), but not hypothalamus) and pACC in all tissues after a short-term summer fast. Response of AMPK and ACC to a long-term winter fast differed by tissue-in liver, there was no difference in total or pAMPK or pACC between groups, but in muscle, WAT and BAT, euthermic GMGS had lower relative abundance of pAMPK and pACC than torpid animals. Therefore, AMPK may be an important energy sensor at all points in hibernator's circannual cycles of food intake and Tb.
|Original language||English (US)|
|Number of pages||10|
|Journal||Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology|
|State||Published - Jul 2011|
ASJC Scopus subject areas
- Molecular Biology