AJP - GI Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


Am J Physiol Gastrointest Liver Physiol (December 7, 2006). doi:10.1152/ajpgi.00553.2006
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
292/5/G1195    most recent
00553.2006v1
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
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gonzalez-Baró, M. R.
Right arrow Articles by Coleman, R. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gonzalez-Baró, M. R.
Right arrow Articles by Coleman, R. A.
Submitted on November 30, 2006
Accepted on December 5, 2006

Function of mitochondrial GPAT1 in the regulation of triacylglycerol biosynthesis and insulin action

Maria R. Gonzalez-Baró1, Tal M. Lewin2, and Rosalind A. Coleman3*

1 Biochemistry, Instituto de Investigaciones Bioquímicas de La Plata, La Plata, Argentina
2 Nutrition, University of North Carolina at Chapel Hill,, Chapel Hill, North Carolina, United States
3 Chapel Hill, United States; Nutrition, University of North Carolina at Chapel Hill,, Chapel Hill, North Carolina, United States

* To whom correspondence should be addressed. E-mail: rcoleman{at}unc.edu.

GPAT1, one of four known glycerol-3-phosphate acyltransferase isoforms, is located on the mitochondrial outer membrane, allowing reciprocal regulation with carnitine palmitoyltransferase-1. GPAT1 is upregulated transcriptionally by insulin and SREBP-1c and down-regulated acutely by AMP-activated protein kinase, consistent with a role in triacylglycerol synthesis. Knockout and overexpression studies suggest that GPAT1 is critical for the development of hepatic steatosis, and that steatosis initiated by overexpression of GPAT1 causes hepatic, and perhaps also peripheral, insulin resistance. Future questions include the function of GPAT1 in relation to the other GPAT isoforms and whether the lipid intermediates synthesized by GPAT and downstream enzymes in the pathway of glycerolipid biosynthesis participate in intracellular signaling pathways.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Visit Other APS Journals Online
Copyright © 1977 by the American Physiological Society.