The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters
Open accessAbstract
The final step of triacylglycerol biosynthesis is catalyzed by acyl CoA:diacylglycerol acyltransferase (DGAT) enzymes. The two known DGATs, DGAT1 and DGAT2, are encoded by unrelated genes. Although both DGAT1 and DGAT2 knockout mice have reduced tissue triacylglycerol contents, they have disparate phenotypes, prompting us to investigate whether the two enzymes have unrecognized functional differences. We now report that DGAT1 exhibits additional acyltransferase activities in vitro, including those of acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases, and acyl CoA:retinol acyltransferase (ARAT), which catalyze the synthesis of diacylglycerols, wax esters, and retinyl esters, respectively. These activities were demonstrated in in vitro assays with membranes from insect cells or homogenates from COS7 cells overexpressing DGAT1. Wax synthase and ARAT activities were also demonstrated in intact COS7 cells expressing DGAT1. Additionally, cells and tissues from DGAT1-deficient mice exhibited reduced ARAT activity, and the mice had increased levels of unesterified retinol in their livers on a high-retinol diet. Our findings indicate that DGAT1 can utilize a variety of acyl acceptors as substrates in vitro and suggest that these activities may be relevant to the in vivo functions of DGAT1.
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Cloning of DGAT2, a Second Mammalian Diacylglycerol Acyltransferase, and Related Family Members
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Self-citationDGAT2 Is a New Diacylglycerol Acyltransferase Gene Family
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Thematic review series: Glycerolipids. DGAT enzymes and triacylglycerol biosynthesis
Yen, C.-L. E., Stone, S. J., Koliwad, S., Harris, C., & Farese, R. V. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800018-jlr200 · Cited by 1,105
Self-citationTrends in insulin resistance: insights into mechanisms and therapeutic strategy
Li, M., Chi, X., Wang, Y., Setrerrahmane, S., Xie, W., & Xu, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01073-0 · Cited by 939
Vitamin A metabolism: An update
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Dissociation of Hepatic Steatosis and Insulin Resistance in Mice Overexpressing DGAT in the Liver
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Self-citationHepatic stellate cell lipid droplets: A specialized lipid droplet for retinoid storage
Blaner, W. S., O'Byrne, S. M., Wongsiriroj, N., Kluwe, J., D'Ambrosio, D. M., Jiang, H., Schwabe, R. F., Hillman, E. M. C., Piantedosi, R., & Libien, J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.11.001 · Cited by 444
Metadata
- Authors
- Yen, C.-L. E., Monetti, M., Burri, B. J., & Farese, R. V.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 46
- Issue
- 7
- Pages
- 1502-1511
- ISSN
- 0022-2275 (ISSN-L)
- OpenAlex
- W2112083470
- Cited by
- 279
- References
- 7
- FWCI
- 6.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Yen, C.-L. E., Monetti, M., Burri, B. J., & Farese, R. V. (2005). The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters. Journal of Lipid Research. https://doi.org/10.1194/jlr.m500036-jlr200
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