Advertisement
J. Lipid Res.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on June 1, 2007

Papers In Press, published online ahead of print March 22, 2007
J. Lipid Res., doi:10.1194/jlr.M600472-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
M600472-JLR200v1
48/6/1305    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Styles, N. A.
Right arrow Articles by Falany, C. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Styles, N. A.
Right arrow Articles by Falany, C. N.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Submitted on October 25, 2006
Revised on March 12, 2007
Accepted on March 22, 2007

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

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

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

Corresponding Author: charles.falany{at}ccc.uab.edu

Bile acid CoA:amino acid N-acyltranstransferase (BAT) is responsible for the amidation of bile acids with the amino acids glycine and taurine. To quantify the 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% in the peroxisomes, and 5-10% 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. The data support the novel finding that clofibrate treatment does not directly regulate BAT activity but does alter the subcellular localization of BAT.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Lipid Res.Home page
S. Ferdinandusse, S. Denis, P. L. Faust, and R. J. A. Wanders
Bile acids: the role of peroxisomes
J. Lipid Res., November 1, 2009; 50(11): 2139 - 2147.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
E. M. Shonsey, S. M. Eliuk, M. S. Johnson, S. Barnes, C. N. Falany, V. M. Darley-Usmar, and M. B. Renfrow
Inactivation of human liver bile acid CoA:amino acid N-acyltransferase by the electrophilic lipid, 4-hydroxynonenal
J. Lipid Res., February 1, 2008; 49(2): 282 - 294.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement