Activation of AMP-activated protein kinase (AMPK) inhibits fatty acid synthesis in bovine mammary epithelial cells

Joseph W McFadden, Benjamin A Corl
Biochemical and Biophysical Research Communications 2009 December 18, 390 (3): 388-93
Activation of AMP-activated protein kinase (AMPK), a heterotrimeric energy-sensing protein, decreases lipid synthesis in liver tissue of various species; however, little is known about the role of AMPK in the regulation of fatty acid synthesis in bovine mammary epithelial cells. Here we report the presence of AMPK mRNA in MAC-T bovine mammary epithelial cells and mammary gland. Treatment of MAC-T with an AMPK activator dramatically decreased de novo fatty acid synthesis by inactivating acetyl-CoA carboxylase-alpha. Activation of AMPK also modified the mRNA expression of several lipogenic genes including fatty acid synthase, glycerol-3-phosphate acyltransferase, and fatty acid binding protein-3. Additionally, decreases in energy availability or rises in intracellular Ca(2+) most likely activated AMPK in MAC-T. These data suggest the presence of LKB1 and Ca(2+)/calmodulin-dependent kinase kinase, two known AMPK kinases, in MAC-T. Identifying AMPK as a molecular target capable of modifying energy substrate utilization may result in the development of new technologies that increase milk production or modify milk composition during periods of increased energy demand.


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