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


     

Originally published In Press as doi:10.1194/jlr.M600331-JLR200 on December 14, 2006

Papers In Press, published online ahead of print March 1, 2007
J. Lipid Res., doi:10.1194/jlr.M600331-JLR200
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M600331-JLR200v1
48/3/583    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
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 Cao, J.
Right arrow Articles by Shi, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cao, J.
Right arrow Articles by Shi, Y.
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?

Journal of Lipid Research, Vol. 48, 583-591, March 2007
Copyright © 2007 by American Society for Biochemistry and Molecular Biology

Catalytic properties of MGAT3, a putative triacylgycerol synthaseboxs

Jingsong Cao1,*, Long Cheng{dagger} and Yuguang Shi2,*,{dagger}

* Endocrine Research, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285
{dagger} Department of Cellular and Molecular Physiology, Pennsylvania State University School of Medicine, Hershey, PA 17033

boxs The online version of this article (available at http://www.jlr.org) contains additional two figures.

Published, JLR Papers in Press, December 14, 2006.

1 Present address of J. Cao: Cardiovascular and Metabolic Diseases, Wyeth Research, Cambridge, MA 02140.

2 To whom correspondence should be addressed. e-mail: yus11{at}psu.edu

Acyl-coenzyme A:monoacylglycerol acyltransferase 3 (MGAT3) is a member of the MGAT family of enzymes that catalyze the synthesis of diacylglycerol (DAG) from monoacylglycerol (MAG), a committed step in dietary fat absorption. Although named after the initial identification of its MGAT activity, MGAT3 shares higher sequence homology with acyl-coenzyme A:diacylglycerol acyltransferase 2 (DGAT2) than with other MGAT enzymes, suggesting that MGAT3 may also possess significant DGAT activity. This study compared the catalytic properties of MGAT3 with those of MGAT1 and MGAT2 enzymes using both MAG and DAG as substrates. Our results showed that in addition to the expected MGAT activity, the recombinant MGAT3 enzyme expressed in Sf-9 insect cells displayed a strong DGAT activity relative to that of MGAT1 and MGAT2 enzymes in the order MGAT3 > MGAT1 > MGAT2. In contrast, none of the three MGAT enzymes recognized biotinylated acyl-CoA or MAG as a substrate. Although MGAT3 possesses full DGAT activity, it differs from DGAT1 in catalytic properties and subcellular localization. The MGAT3 activity was sensitive to inhibition by the presence of 1% CHAPS, whereas DGAT1 activity was stimulated by the detergent. Consistent with high sequence homology with DGAT2, the MGAT3 enzyme demonstrated a similar subcellular distribution pattern to that of DGAT2, but not DGAT1, when expressed in COS-7 cells. Our data suggest that MGAT3 functions as a novel triacylglycerol (TAG) synthase that catalyzes efficiently the two consecutive acylation steps in TAG synthesis.

Supplementary key words acyl-coenzyme A:monoacylglycerol acyltransferase • acyltransferase • monoacylglycerol

Abbreviations: DAG, diacylglycerol; DGAT, acyl-coenzyme A:diacylglycerol acyltransferase; ER, endoplasmic reticulum; G3P, glycerol-3-phosphate; MAG, monoacylglycerol; MGAT, acyl-coenzyme A:monoacylglycerol acyltransferase; TAG, triacylglycerol


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. Biol. Chem.Home page
D. Cheng, J. Iqbal, J. Devenny, C.-H. Chu, L. Chen, J. Dong, R. Seethala, W. J. Keim, A. V. Azzara, R. M. Lawrence, et al.
Acylation of Acylglycerols by Acyl Coenzyme A:Diacylglycerol Acyltransferase 1 (DGAT1): FUNCTIONAL IMPORTANCE OF DGAT1 IN THE INTESTINAL FAT ABSORPTION
J. Biol. Chem., October 31, 2008; 283(44): 29802 - 29811.
[Abstract] [Full Text] [PDF]

Home page
 Endocr. Rev.Home page
M. Prentki and S. R. M. Madiraju
Glycerolipid Metabolism and Signaling in Health and Disease
Endocr. Rev., October 1, 2008; 29(6): 647 - 676.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Cao, D. Shan, T. Revett, D. Li, L. Wu, W. Liu, J. F. Tobin, and R. E. Gimeno
Molecular Identification of a Novel Mammalian Brain Isoform of Acyl-CoA:Lysophospholipid Acyltransferase with Prominent Ethanolamine Lysophospholipid Acylating Activity, LPEAT2
J. Biol. Chem., July 4, 2008; 283(27): 19049 - 19057.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. S. Choi, D. B. Savage, A. Kulkarni, X. X. Yu, Z.-X. Liu, K. Morino, S. Kim, A. Distefano, V. T. Samuel, S. Neschen, et al.
Suppression of Diacylglycerol Acyltransferase-2 (DGAT2), but Not DGAT1, with Antisense Oligonucleotides Reverses Diet-induced Hepatic Steatosis and Insulin Resistance
J. Biol. Chem., August 3, 2007; 282(31): 22678 - 22688.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 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