Potential role of adenosine monophosphate-activated protein kinase in regulation of energy metabolism in dairy goat mammary epithelial cells.

ABSTRACT

The 5'-adenosine monophosphate-activated protein kinase (AMPK) is an energy sensor that regulates cellular metabolism. 5'-Adenosine monophosphate-activated protein kinase controls glucose and lipid metabolism in skeletal muscle, liver, and adipose tissues. The aim of this study was to investigate the effects of AMPK on glucose and lipid metabolism in dairy goat mammary epithelial cells. Treatment of mammary epithelial cells with an AMPK activator (5-aminoimidazole-4-carboxamide 1-ß-D-ribofuranoside) dramatically increased glucose uptake and glucose transporter-1 mRNA abundance, and decreased levels of glycogen synthase 1 mRNA. Activation of AMPK also induced an increase in carnitine palmitoyl transferase 1 mRNA and decreases in fatty acid synthase and acetyl-CoA carboxylase 1 mRNA. These results suggest that AMPK is involved in the regulation of energy metabolism in dairy goat mammary epithelial cells.