Disease relevance of DGAT

• Phospholipase A2, lysophosphatidylcholine acyltransferase, and diacylglycerol acyltransferase activities were not influenced by 24 or 48 h of hypoxia [1].

High impact information on DGAT

• Lysophosphatidate acyltransferase, diacylglycerol kinase, and diacylglycerol acyltransferase can be activated by the two protein kinases also in microsomes from guinea pig cerebellum [2].
• In contrast to microsomes from rat liver, about 70% of the product with the 1- and 2-monooleoylglycerol ethers was triradylglycerol, suggesting that the diacylglycerol acyltransferase from chick liver can acylate acyl, alkylglycerols [3].
• The specific activities of fatty acid CoA ligase, diacylglycerol acyltransferase, and microsomal and mitochondrial glycerol-P acyltransferases changed comparatively little during this time period [3].
• Specific activities of phosphatidic acid phosphatase, microsomal glycerophosphate acyltransferase, and diacylglycerol acyltransferase varied minimally over the time course investigated [4].
• 6. Thus an increase in intracellular Ca2+ concentration appeared to have three effects on glycerolipid metabolism: (a) slight inhibition of some metabolic step preceding phosphatidate synthesis, (b) inhibition of diacylglycerol acyltransferase and (c) activation of a triacylglycerol lipase [5].

Anatomical context of DGAT

• L-glutamine and transforming growth factor-alpha enhance recovery of monoacylglycerol acyltransferase and diacylglycerol acyltransferase activity in porcine postischemic ileum [6].

Associations of DGAT with chemical compounds

• The results provide new insight on activation of DGAT during TG accumulation as well as optimal DGAT assay conditions for solubilized fractions [7].
• The effect of phosphatidic acid was reproduced using DGAT fraction obtained by 0.5 M KCl elution on Mono S column chromatography [7].
• Diacylglycerol acyltransferase (DGAT), which catalyzes the final step in triacylglycerol (TG) biosynthesis, is crucial for lipid accumulation and formation of lipid bodies in an oleaginous fungus, Mortierella ramanniana var. angulispora [7].
• Addition of phospholipids, especially anionic phospholipids such as phosphatidic acid and phosphatidylserine, to the assay mixture greatly increased DGAT activity [7].
• Since solubilization of DGAT in the lipid body fraction from this fungus with 0.5% Triton X-100 gave very low recovery of the activity, some activation factors for solubilized DGAT activity were investigated [7].

Other interactions of DGAT

• At 72 h, MGAT and DGAT recovery in Gln plus TGF-alpha-treated loops was significantly greater than their corresponding 6-h peak damage levels (p < 0.05) [6].
• We can show now that these changes are associated with a significant increase in the activities of lysophosphatidate acyltransferase, diacylglycerol kinase, and diacylglycerol acyltransferase which reaches a maximum during the first 60 s after stimulation [2].

References