Premium
Alcohol and lipid metabolism
Author(s) -
Crabb David W,
Liangpunsakul Suthat
Publication year - 2006
Publication title -
journal of gastroenterology and hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.214
H-Index - 130
eISSN - 1440-1746
pISSN - 0815-9319
DOI - 10.1111/j.1440-1746.2006.04582.x
Subject(s) - ampk , peroxisome , sterol regulatory element binding protein , amp activated protein kinase , peroxisome proliferator activated receptor , biochemistry , protein kinase a , peroxisome proliferator activated receptor alpha , adenosine monophosphate , lipid metabolism , acetyl coa carboxylase , biology , endocrinology , pyruvate carboxylase , adenosine , medicine , transcription factor , sterol , kinase , receptor , cholesterol , nuclear receptor , enzyme , gene
Hepatic lipid metabolism is controlled by several master transcription factors, in particular peroxisome proliferator‐activated receptor‐α (PPAR‐α) and sterol response element binding protein‐1 (SREBP‐1). Peroxisome proliferator‐activated receptor‐α is a receptor for free fatty acids (FFA), and can activate genes involved in transport, oxidation, and export of FFA. Sterol response element binding protein‐1 is a sensor for the level of cholesterol in the liver, and is able to activate genes involved in synthesis of cholesterol and FFA. Chronic ethanol treatment of cells or animals inhibited PPAR‐α function and activated SREBP. In addition, ethanol inhibited adenosine monophosphate‐dependent protein kinase (AMPK). The AMPK controls fatty acid metabolism by inhibiting acetyl‐coenzyme A carboxylase, reducing malonyl‐coenzyme A, and thereby permitting fatty acid transport into and oxidation in the mitochondrion. Adenosine monophosphate‐dependent protein kinase was inhibited in alcohol‐treated animals and cells. The mechanisms by which ethanol affects AMPK and the transcription factors are as yet incompletely understood.