| Title : Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation - Okamoto_2017_Biochem.Biophys.Res.Commun_486_558 |
| Author(s) : Okamoto S , Murano T , Suzuki T , Uematsu S , Niwa Y , Sasazawa Y , Dohmae N , Bujo H , Simizu S |
| Ref : Biochemical & Biophysical Research Communications , 486 :558 , 2017 |
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Abstract :
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 Trp417. In this study, we demonstrated that LPL is C-mannosylated at Trp417 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. |
| PubMedSearch : Okamoto_2017_Biochem.Biophys.Res.Commun_486_558 |
| PubMedID: 28327359 |
| Gene_locus related to this paper: human-LPL |
| Gene_locus | human-LPL |
Okamoto S, Murano T, Suzuki T, Uematsu S, Niwa Y, Sasazawa Y, Dohmae N, Bujo H, Simizu S (2017)
Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation
Biochemical & Biophysical Research Communications
486 :558
Okamoto S, Murano T, Suzuki T, Uematsu S, Niwa Y, Sasazawa Y, Dohmae N, Bujo H, Simizu S (2017)
Biochemical & Biophysical Research Communications
486 :558