DGAT1: Difference between revisions
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==Function== | ==Function== | ||
This gene encodes an multipass transmembrane protein that functions as a key metabolic enzyme. The encoded protein catalyzes the conversion of [[diacylglycerol]] and [[fatty acyl-CoA esters|fatty acyl CoA]] to [[triacylglycerol]]. This enzyme can also transfer acyl CoA to retinol. Activity of this protein may be associated with obesity and other metabolic diseases.<ref name="pmid18757836">{{cite journal | vauthors = Yen CL, Stone SJ, Koliwad S, Harris C, Farese RV | title = Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis | journal = Journal of Lipid Research | volume = 49 | issue = 11 | pages = 2283–301 | year = 2008 | pmid = 18757836 | pmc = 3837458 | doi = 10.1194/jlr.R800018-JLR200 }}</ref> | This gene encodes an multipass transmembrane protein that functions as a key metabolic enzyme. The encoded protein catalyzes the conversion of [[diacylglycerol]] and [[fatty acyl-CoA esters|fatty acyl CoA]] to [[triacylglycerol]]. This enzyme can also transfer acyl CoA to retinol. Activity of this protein may be associated with obesity and other metabolic diseases.<ref name="pmid18757836">{{cite journal | vauthors = Yen CL, Stone SJ, Koliwad S, Harris C, Farese RV | title = Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis | journal = Journal of Lipid Research | volume = 49 | issue = 11 | pages = 2283–301 | year = 2008 | pmid = 18757836 | pmc = 3837458 | doi = 10.1194/jlr.R800018-JLR200 }}</ref><ref name="pmid10802663">{{cite journal | vauthors = Smith SJ, Cases S, Jensen DR, Chen HC, Sande E, Tow B, Sanan DA, Raber J, Eckel RH, Farese RV | title = Obesity resistance and multiple mechanisms of triglyceride synthesis in mice lacking Dgat | journal = Nature Genetics | volume = 25 | issue = 1 | pages = 87–90 | date = May 2000 | pmid = 10802663 | doi = 10.1038/75651 }}</ref> This enzyme is essential for [[lactation]] in mice<ref name="pmid10802663" />, and mutations in this gene affect the composition and volume of milk produced by both cattle<ref name="pmid11827942">{{cite journal | vauthors = Grisart B, Coppieters W, Farnir F, Karim L, Ford C, Berzi P, Cambisano N, Mni M, Reid S, Simon P, Spelman R, Georges M, Snell R | title = Positional Candidate Cloning of a QTL in Dairy Cattle: Identification of a Missense Mutation in the Bovine ''DGAT1'' Gene with Major Effect on Milk Yield and Composition | journal = Genome Research | volume = 12 | issue = 2 | pages = 222–31 | date = February 2002 | pmid = 11827942 | doi = 10.1101/gr.224202 }}</ref> and goats<ref name="pmid28500343">{{cite journal | vauthors = Martin P, Palhière I, Maroteau C, Bardou P, Canale-Tabet K, Sarry J, Woloszyn F, Bertrand-Michel J, Racke I, Besir H, Rupp R, Tosser-Klopp G | title = A genome scan for milk production traits in dairy goats reveals two new mutations in ''Dgat1'' reducing milk fat content | journal = Scientific Reports | volume = 7 | issue = 1 | pages = 1872 | date = May 2017 | pmc = 5431851 | pmid = 28500343 | doi = 10.1038/s41598-017-02052-0 }}</ref>. | ||
== See also == | == See also == | ||
Latest revision as of 08:47, 10 January 2019
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Diacylglycerol O-acyltransferase 1 is an enzyme that in humans is encoded by the DGAT1 gene.[1]
Function
This gene encodes an multipass transmembrane protein that functions as a key metabolic enzyme. The encoded protein catalyzes the conversion of diacylglycerol and fatty acyl CoA to triacylglycerol. This enzyme can also transfer acyl CoA to retinol. Activity of this protein may be associated with obesity and other metabolic diseases.[2][3] This enzyme is essential for lactation in mice[3], and mutations in this gene affect the composition and volume of milk produced by both cattle[4] and goats[5].
See also
References
- ↑ "Entrez Gene: Diacylglycerol O-acyltransferase 1". Retrieved 2016-08-28.
- ↑ Yen CL, Stone SJ, Koliwad S, Harris C, Farese RV (2008). "Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis". Journal of Lipid Research. 49 (11): 2283–301. doi:10.1194/jlr.R800018-JLR200. PMC 3837458. PMID 18757836.
- ↑ 3.0 3.1 Smith SJ, Cases S, Jensen DR, Chen HC, Sande E, Tow B, Sanan DA, Raber J, Eckel RH, Farese RV (May 2000). "Obesity resistance and multiple mechanisms of triglyceride synthesis in mice lacking Dgat". Nature Genetics. 25 (1): 87–90. doi:10.1038/75651. PMID 10802663.
- ↑ Grisart B, Coppieters W, Farnir F, Karim L, Ford C, Berzi P, Cambisano N, Mni M, Reid S, Simon P, Spelman R, Georges M, Snell R (February 2002). "Positional Candidate Cloning of a QTL in Dairy Cattle: Identification of a Missense Mutation in the Bovine DGAT1 Gene with Major Effect on Milk Yield and Composition". Genome Research. 12 (2): 222–31. doi:10.1101/gr.224202. PMID 11827942.
- ↑ Martin P, Palhière I, Maroteau C, Bardou P, Canale-Tabet K, Sarry J, Woloszyn F, Bertrand-Michel J, Racke I, Besir H, Rupp R, Tosser-Klopp G (May 2017). "A genome scan for milk production traits in dairy goats reveals two new mutations in Dgat1 reducing milk fat content". Scientific Reports. 7 (1): 1872. doi:10.1038/s41598-017-02052-0. PMC 5431851. PMID 28500343.
Further reading
- Ludwig EH, Mahley RW, Palaoglu E, Ozbayrakçi S, Balestra ME, Borecki IB, Innerarity TL, Farese RV (July 2002). "DGAT1 promoter polymorphism associated with alterations in body mass index, high density lipoprotein levels and blood pressure in Turkish women". Clinical Genetics. 62 (1): 68–73. doi:10.1034/j.1399-0004.2002.620109.x. PMID 12123490.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.