Activation of AMP-activated protein kinase (AMPK) inhibits fatty acid synthesis in bovine mammary epithelial cells |
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Authors: | Joseph W. McFadden |
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Affiliation: | Department of Dairy Science, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA |
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Abstract: | 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-α. 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 Ca2+ most likely activated AMPK in MAC-T. These data suggest the presence of LKB1 and Ca2+/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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Keywords: | ACC AMPK Bovine mammary epithelial cell Fat synthesis |
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