FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Published as doi: 10.1096/fj.06-6919com.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
fj.06-6919comv1
21/1/99    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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Reilly, S.-J.
Right arrow Articles by Hunt, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Reilly, S.-J.
Right arrow Articles by Hunt, M. C.
(The FASEB Journal. 2007;21:99-107.)
© 2007 FASEB

A peroxisomal acyltransferase in mouse identifies a novel pathway for taurine conjugation of fatty acids

Sarah-Jayne Reilly, Ethna M. O’Shea, Ulla Andersson, James O’Byrne, Stefan E. H. Alexson and Mary C. Hunt1

Karolinska Institutet, Department of Laboratory Medicine, Division of Clinical Chemistry C1–74, Karolinska University Hospital at Huddinge, Stockholm, Sweden

1Correspondence: Karolinska Institutet, Department of Laboratory Medicine, Division of Clinical Chemistry C1–74, Karolinska University Hospital at Huddinge, SE-141 86 Stockholm, Sweden. E-mail: mary.hunt{at}ki.se

A wide variety of endogenous carboxylic acids and xenobiotics are conjugated with amino acids, before excretion in urine or bile. The conjugation of carboxylic acids and bile acids with taurine and glycine has been widely characterized, and de novo synthesized bile acids are conjugated to either glycine or taurine in peroxisomes. Peroxisomes are also involved in the oxidation of several other lipid molecules, such as very long chain acyl-CoAs, branched chain acyl-CoAs, and prostaglandins. In this study, we have now identified a novel peroxisomal enzyme called acyl-coenzyme A:amino acid N-acyltransferase (ACNAT1). Recombinantly expressed ACNAT1 acts as an acyltransferase that efficiently conjugates very long-chain and long-chain fatty acids to taurine. The enzyme shows no conjugating activity with glycine, showing that it is a specific taurine conjugator. Acnat1 is mainly expressed in liver and kidney, and the gene is localized in a gene cluster, together with two further acyltransferases, one of which conjugates bile acids to glycine and taurine. In conclusion, these data describe ACNAT1 as a new acyltransferase, involved in taurine conjugation of fatty acids in peroxisomes, identifying a novel pathway for production of N-acyltaurines as signaling molecules or for excretion of fatty acids.—Sarah-Jayne Reilly, Ethna M. O’Shea, Ulla Andersson, James O’Byrne, Stefan E. H. Alexson and Mary C. Hunt. A peroxisomal acyltransferase in mouse identifies a novel pathway for taurine conjugation of fatty acids.


Key Words: acyl-coenzyme A • fatty acid amide hydrolase • N-acyltaurine




This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
S. Wiese, T. Gronemeyer, R. Ofman, M. Kunze, C. P. Grou, J. A. Almeida, M. Eisenacher, C. Stephan, H. Hayen, L. Schollenberger, et al.
Proteomics Characterization of Mouse Kidney Peroxisomes by Tandem Mass Spectrometry and Protein Correlation Profiling
Mol. Cell. Proteomics, December 1, 2007; 6(12): 2045 - 2057.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2007 by The Federation of American Societies for Experimental Biology.