单酰甘油脂肪酶
化学
酰基转移酶
二酰甘油激酶
生物化学
肉豆蔻酰化
药物发现
酶
药理学
生物合成
生物
内大麻素系统
膜
受体
蛋白激酶C
作者
Kim Huard,Allyn T. Londregan,Gregory J. Tesz,Kevin B. Bahnck,Thomas V. Magee,David Hepworth,Jana Polívková,Steven B. Coffey,Brandon Pabst,J Gosset,Anu Nigam,Kou Kou,Hao Sun,Kyuha Lee,Michael Herr,Markus Boehm,Philip A. Carpino,Bryan Goodwin,Christian Perreault,Qifang Li
标识
DOI:10.1021/acs.jmedchem.5b01008
摘要
Inhibition of triacylglycerol (TAG) biosynthetic enzymes has been suggested as a promising strategy to treat insulin resistance, diabetes, dyslipidemia, and hepatic steatosis. Monoacylglycerol acyltransferase 3 (MGAT3) is an integral membrane enzyme that catalyzes the acylation of both monoacylglycerol (MAG) and diacylglycerol (DAG) to generate DAG and TAG, respectively. Herein, we report the discovery and characterization of the first selective small molecule inhibitors of MGAT3. Isoindoline-5-sulfonamide (6f, PF-06471553) selectively inhibits MGAT3 with high in vitro potency and cell efficacy. Because the gene encoding MGAT3 (MOGAT3) is found only in higher mammals and humans, but not in rodents, a transgenic mouse model expressing the complete human MOGAT3 was used to characterize the effects of 6f in vivo. In the presence of a combination of diacylglycerol acyltransferases 1 and 2 (DGAT1 and DGAT2) inhibitors, an oral administration of 6f exhibited inhibition of the incorporation of deuterium-labeled glycerol into TAG in this mouse model. The availability of a potent and selective chemical tool and a humanized mouse model described in this report should facilitate further dissection of the physiological function of MGAT3 and its role in lipid homeostasis.
科研通智能强力驱动
Strongly Powered by AbleSci AI