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Gene Review

Dgat1  -  diacylglycerol O-acyltransferase 1

Mus musculus

Synonyms: ARAT, Acyl-CoA retinol O-fatty-acyltransferase, C75990, D15Ertd23e, Dgat, ...
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Disease relevance of Dgat1

  • We tested whether augmentation of triglyceride synthesis in adipose tissue by transgenic overexpression of the diacylglycerol aclytransferase-1 (Dgat1) gene causes obesity and/or alters insulin sensitivity [1].
  • These results suggest that the hyperphagia in Dgat1(-/-) mice is a secondary mechanism that compensates for the increased utilization of fuel substrates [2].
  • When fasted in a cold environment, Dgat1(-/-) mice developed hypothermia, which was associated with hypoglycemia [2].

High impact information on Dgat1

  • Obesity resistance and multiple mechanisms of triglyceride synthesis in mice lacking Dgat [3].
  • Therefore, Dgat has been considered necessary for adipose tissue formation and essential for survival [3].
  • Our findings indicate that multiple mechanisms exist for triglyceride synthesis and suggest that the selective inhibition of Dgat-mediated triglyceride synthesis may be useful for treating obesity [3].
  • Dgat deficiency also alters triglyceride metabolism in other tissues, including the mammary gland, where lactation is defective in Dgat-/- females [3].
  • Triglyceride synthesis has been assumed to occur primarily through acyl CoA:diacylglycerol transferase (Dgat), a microsomal enzyme that catalyses the final and only committed step in the glycerol phosphate pathway [3].

Biological context of Dgat1


Anatomical context of Dgat1

  • However, Dgat1(-/-) mice had reduced postabsorptive chylomicronemia (1 h after a high fat challenge) and accumulated neutral-lipid droplets in the cytoplasm of enterocytes when chronically fed a high fat diet [4].
  • Adult Dgat(-/-) mice had dry fur and hair loss, which were associated with atrophic sebaceous glands and fur lipid abnormalities [5].

Associations of Dgat1 with chemical compounds


Other interactions of Dgat1

  • Compared with control littermates, Dgat1 transgenic mice were both insulin and leptin resistant and had markedly elevated plasma free fatty acid levels [1].
  • Analysis of intestine from Dgat1(-/-) mice revealed activity for two other enzymes, DGAT2 and diacylglycerol transacylase, that catalyze triacylglycerol synthesis and apparently help to compensate for the absence of DGAT1 [4].


  1. Whole-body Insulin Resistance in the Absence of Obesity in FVB Mice With Overexpression of Dgat1 in Adipose Tissue. Chen, N., Liu, L., Zhang, Y., Ginsberg, H.N., Yu, Y.H. Diabetes (2005) [Pubmed]
  2. Analysis of energy expenditure at different ambient temperatures in mice lacking DGAT1. Chen, H.C., Ladha, Z., Smith, S.J., Farese, R.V. Am. J. Physiol. Endocrinol. Metab. (2003) [Pubmed]
  3. Obesity resistance and multiple mechanisms of triglyceride synthesis in mice lacking Dgat. Smith, S.J., Cases, S., Jensen, D.R., Chen, H.C., Sande, E., Tow, B., Sanan, D.A., Raber, J., Eckel, R.H., Farese, R.V. Nat. Genet. (2000) [Pubmed]
  4. DGAT1 is not essential for intestinal triacylglycerol absorption or chylomicron synthesis. Buhman, K.K., Smith, S.J., Stone, S.J., Repa, J.J., Wong, J.S., Knapp, F.F., Burri, B.J., Hamilton, R.L., Abumrad, N.A., Farese, R.V. J. Biol. Chem. (2002) [Pubmed]
  5. Leptin modulates the effects of acyl CoA:diacylglycerol acyltransferase deficiency on murine fur and sebaceous glands. Chen, H.C., Smith, S.J., Tow, B., Elias, P.M., Farese, R.V. J. Clin. Invest. (2002) [Pubmed]
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