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Am J Physiol Endocrinol Metab 296: E812-E819, 2009. First published January 27, 2009; doi:10.1152/ajpendo.90710.2008
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Berberine improves lipid dysregulation in obesity by controlling central and peripheral AMPK activity

Woo Sik Kim,1,* Yun Sok Lee,1,* Seung Hun Cha,2,* Hyun Woo Jeong,1 Sung Sik Choe,1 Mi-Ran Lee,3 Goo Taeg Oh,3 Hye-Sun Park,4 Ki-Up Lee,4 M. Daniel Lane,2 and Jae Bum Kim1

1Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea; 2Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205; 3Division of Life and Pharmaceutical Sciences, Center for Cell Signaling Research, Ewha Womans University, Seoul 120-750; and 4Asan Institute for Life Sciences, and Department of Internal Medicine, University of Ulsan College of Medicine, Seoul, Korea 138-736

Submitted 17 November 2008 ; accepted in final form 26 January 2009

AMP-activated protein kinase (AMPK) plays an important role in regulating whole body energy homeostasis. Recently, it has been demonstrated that berberine (BBR) exerts antiobesity and antidiabetic effects in obese and diabetic rodent models through the activation of AMPK in peripheral tissues. Here we show that BBR improves lipid dysregulation and fatty liver in obese mice through central and peripheral actions. In obese db/db and ob/ob mice, BBR treatment reduced liver weight, hepatic and plasma triglyceride, and cholesterol contents. In the liver and muscle of db/db mice, BBR promoted AMPK activity and fatty acid oxidation and changed expression of genes involved in lipid metabolism. Additionally, intracerebroventricular administration of BBR decreased the level of malonyl-CoA and stimulated the expression of fatty acid oxidation genes in skeletal muscle. Together, these data suggest that BBR would improve fatty liver in obese subjects, which is probably mediated not only by peripheral AMPK activation but also by neural signaling from the central nervous system.

fatty acid oxidation; hypothalamus; malonyl-coenzyme A; AMP-activated protein kinase


Address for reprint requests and other correspondence: J. Bum Kim, Institute of Molecular Biology and Genetics, Dept. of Biological Sciences, Seoul National University, San 56-1, Sillim-Dong, Kwanak-Gu, Seoul 151-742, Korea (e-mail: jaebkim{at}snu.ac.kr)






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