通过C-甘露糖基化调节脂蛋白脂肪酶的分泌和酶活性。
Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.
作者信息
Okamoto Sawako, Murano Takeyoshi, Suzuki Takehiro, Uematsu Shiho, Niwa Yuki, Sasazawa Yukiko, Dohmae Naoshi, Bujo Hideaki, Simizu Siro
机构信息
Department of Applied Chemistry, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Department of Clinical-Laboratory and Experimental-Research Medicine, Toho University Sakura Medical Center, 564-1 Shimoshizu, Sakura 285-8741, Japan.
出版信息
Biochem Biophys Res Commun. 2017 Apr 29;486(2):558-563. doi: 10.1016/j.bbrc.2017.03.085. Epub 2017 Mar 19.
Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia. LPL has one predicted C-mannosylation site at Trp. In this study, we demonstrated that LPL is C-mannosylated at Trp by mass spectrometry. Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type. These data suggest the importance of C-mannosylation for LPL functions.
脂蛋白脂肪酶（LPL）是脂质代谢和转运中的一种关键酶，其酶缺乏会导致代谢紊乱，如高甘油三酯血症。LPL在色氨酸处有一个预测的C-甘露糖基化位点。在本研究中，我们通过质谱证明LPL在色氨酸处发生了C-甘露糖基化。此外，通过使用野生型和过表达LPL的C-甘露糖基化缺陷突变体细胞系，我们发现C-甘露糖基化缺陷突变体LPL的分泌效率和酶活性均低于野生型。这些数据表明C-甘露糖基化对LPL功能的重要性。
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