Diradylglycerols alter fatty acid inhibition of monoacylglycerol acyltransferase activity in Triton X-100 mixed micelles

Biochemistry
R A ColemanB G Bhat

Abstract

The activity of hepatic monoacylglycerol acyltransferase (MGAT) (EC 2.3.1.22), a developmentally expressed microsomal enzyme, is inhibited by long-chain fatty acids, and stimulated by its product 1, 2-diacyl-sn-glycerol. Because the quantities of fatty acids and diacylglycerols are likely to vary in membranes during different physiological conditions and could thereby alter MGAT activity, we examined their combined effects on MGAT in Triton X-100/phospholipid mixed micelles. MGAT's product, 1,2-diC18:1-sn-glycerol, which is also normally a cooperative activator of the activity, reversed the 50% inhibition caused by 10 mol % oleic acid. The presence of oleic acid also allowed low concentrations (<10 mol %) of 1, 2-diC18:1-sn-glycerol to stimulate MGAT activity without the lag that is observed in the absence of fatty acid. At 12.6 mol %, 1, 2-monoC18:1-sn-glycerol ether, which alone has no effect on MGAT activity, became an activator in the presence of 10 mol % oleic acid. Kinetic studies revealed that in the presence of 15 mol % oleic acid, 1,2-diC18:1-sn-glycerol ether increased the apparent Vmax by 3. 8-fold while minimally altering the apparent Km for palmitoyl-CoA. Other neutral lipids including tri-C18:1-glycerol, ceramide,...Continue Reading

References

Mar 1, 1995·Journal of Biochemistry·K Kasahara, U Kikkawa
Aug 11, 1995·The Journal of Biological Chemistry·G M CarmanE A Dennis

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Citations

Jul 9, 1999·Progress in Lipid Research·F M Goñi, A Alonso
Aug 15, 2000·Annual Review of Nutrition·R A ColemanD M Muoio
Jun 15, 2007·Chemistry and Physics of Lipids·Juan C Gómez-Fernández, Senena Corbalán-García

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