Cheng Dong, Iqbal Jahangir, Devenny James, Chu Ching-Hsuen, Chen Luping, Dong Jessica, Seethala Ramakrishna, Keim William J, Azzara Anthony V, Lawrence R Michael, Pelleymounter Mary Ann, Hussain M Mahmood
Department of Metabolic Diseases, Bristol-Myers Squibb Company, Princeton, New Jersey 08543-5400, USA.
J Biol Chem. 2008 Oct 31;283(44):29802-11. doi: 10.1074/jbc.M800494200. Epub 2008 Sep 3.
Acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1) is one of the four intestinal membrane bound acyltransferases implicated in dietary fat absorption. Recently, it was found that, in addition to acylating diacylglycerol (DAG), DGAT1 also possesses robust enzymatic activity for acylating monoacylglycerol (MAG) (Yen, C. L., Monetti, M., Burri, B. J., and Farese, R. V., Jr. (2005) J. Lipid Res. 46, 1502-1511). In the current paper, we have conducted a detailed characterization of this reaction in test tube, intact cell culture, and animal models. Enzymatically, we found that triacylglycerol (TAG) synthesis from MAG by DGAT1 does not behave according to classic Michaelis-Menten kinetics. At low concentrations of 2-MAG (<50 microm), the major acylation product by DGAT1 was TAG; however, increased concentrations of 2-MAG (50-200 microm) resulted in decreased TAG formation. This unique product/substrate relationship is similar to MGAT3 but distinct from DGAT2 and MGAT2. We have also found that XP620 is an inhibitor that selectively inhibits the acylation of MAG by DGAT1 (IC(50) of human DGAT1: 16.6+/-4.0 nM (MAG as substrate) and 1499+/-318 nM (DAG as substrate); IC(50) values of human DGAT2, MGAT2, and MGAT3 are >30,000 nM). Using this pharmacological tool, we have shown that approximately 76 and approximately 89% of the in vitro TAG synthesis initiated from MAG is mediated by DGAT1 in Caco-2 cell and rat intestinal mucosal membranes, respectively. When applied to intact cultured cells, XP620 substantially decreased but did not abolish apoB secretion in differentiated Caco-2 cells. It also decreased TAG and DAG syntheses in primary enterocytes. Last, when delivered orally to rats, XP620 decreased absorption of orally administered lipids by approximately 50%. Based on these data, we conclude that the acylation of acylglycerols by DGAT1 is important for dietary fat absorption in the intestine.
酰基辅酶A:二酰基甘油酰基转移酶1(DGAT1)是参与膳食脂肪吸收的四种肠膜结合酰基转移酶之一。最近发现,除了使二酰基甘油(DAG)酰化外,DGAT1对单酰基甘油(MAG)的酰化也具有很强的酶活性(Yen, C. L., Monetti, M., Burri, B. J., and Farese, R. V., Jr. (2005) J. Lipid Res. 46, 1502 - 1511)。在本文中,我们在试管、完整细胞培养和动物模型中对该反应进行了详细表征。在酶学方面,我们发现DGAT1催化MAG合成三酰基甘油(TAG)的过程不符合经典的米氏动力学。在低浓度的2 - MAG(<50微摩尔)时,DGAT1的主要酰化产物是TAG;然而,2 - MAG浓度增加(50 - 200微摩尔)会导致TAG形成减少。这种独特的产物/底物关系与MGAT3相似,但与DGAT2和MGAT2不同。我们还发现XP620是一种抑制剂,可选择性抑制DGAT1对MAG的酰化作用(人DGAT1的IC(50):以MAG为底物时为16.6±4.0纳摩尔,以DAG为底物时为1499±318纳摩尔;人DGAT2、MGAT2和MGAT3的IC(50)值均大于30,000纳摩尔)。使用这种药理学工具,我们表明在Caco - 2细胞和大鼠肠黏膜中,分别约76%和约89%由MAG起始的体外TAG合成是由DGAT1介导的。当应用于完整培养细胞时,XP620显著降低但并未消除分化的Caco - 2细胞中载脂蛋白B的分泌。它还降低了原代肠细胞中TAG和DAG的合成。最后,当口服给予大鼠时,XP620使口服脂质的吸收降低了约50%。基于这些数据,我们得出结论,DGAT1对酰基甘油的酰化作用对肠道中膳食脂肪的吸收很重要。