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Journal of Lipid Research, Vol. 48, 1305-1315, June 2007
Copyright © 2007 by American Society for Biochemistry and Molecular Biology

Quantification and regulation of the subcellular distribution of bile acid coenzyme A:amino acid N-acyltransferase activity in rat liver

Nathan A. Styles, Josie L. Falany, Stephen Barnes and Charles N. Falany¹

Department of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, AL 35294

Published, JLR Papers in Press, March 22, 2007.

¹ To whom correspondence should be addressed. e-mail: charles.falany{at}ccc.uab.edu

Bile acid coenzyme A:amino acid N-acyltransferase (BAT) is responsible for the amidation of bile acids with the amino acids glycine and taurine. To quantify total BAT activity in liver subcellular organelles, livers from young adult male and female Sprague-Dawley rats were fractionated into multiple subcellular compartments. In male and female rats, 65–75% of total liver BAT activity was found in the cytosol, 15–17% was found in the peroxisomes, and 5–10% was found in the heavy mitochondrial fraction. After clofibrate treatment, male rats displayed an increase in peroxisomal BAT specific activity and a decrease in cytosolic BAT specific activity, whereas females showed an opposite response. However, there was no overall change in BAT specific activity in whole liver homogenate. Treatment with rosiglitazone or cholestyramine had no effect on BAT activity in any subcellular compartment. These experiments indicate that the majority of BAT activity in the rat liver resides in the cytosol. Approximately 15% of BAT activity is present in the peroxisomal matrix. These data support the novel finding that clofibrate treatment does not directly regulate BAT activity but does alter the subcellular localization of BAT.

Supplementary key words peroxisomes • bile acid amidation • subcellular localization • induction • peroxisomal transport • taurine • glycine • cholyl-coenzyme A • clofibrate • bile acid ligase

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