ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain.
作者信息
Kristensen Kristian Kølby, Leth-Espensen Katrine Zinck, Young Stephen G, Ploug Michael
机构信息
Finsen Laboratory, Rigshospitalet, DK-2200 Copenhagen N, Denmark.
Biotech Research and Innovation Centre (BRIC), University of Copenhagen, DK-2200 Copenhagen N, Denmark.
出版信息
J Lipid Res. 2020 Sep;61(9):1253. doi: 10.1194/jlr.ILR120000780. Epub 2020 Apr 23.
Abstract
摘要
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ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain.血管生成素样蛋白4（ANGPTL4）通过催化脂蛋白脂肪酶（LPL）水解酶结构域的不可逆去折叠来使其失活。
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本文引用的文献
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GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism.GPIHBP1 和脂蛋白脂肪酶，共同参与血浆甘油三酯代谢。
Cell Metab. 2019 Jul 2;30(1):51-65. doi: 10.1016/j.cmet.2019.05.023.
2
A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase.载脂蛋白聚糖结合蛋白 1 中含硫酸酪氨酸的酸性结构域紊乱会调控脂蛋白脂肪酶。
Proc Natl Acad Sci U S A. 2018 Jun 26;115(26):E6020-E6029. doi: 10.1073/pnas.1806774115. Epub 2018 Jun 13.
3
4
The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain.内皮细胞膜蛋白GPIHBP1的酸性结构域通过防止脂蛋白脂肪酶催化结构域的去折叠来稳定其活性。
Elife. 2016 Jan 3;5:e12095. doi: 10.7554/eLife.12095.
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