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.
| Original language | English |
|---|---|
| Pages (from-to) | 558-563 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 486 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2017 Apr 29 |
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Keywords
- C-mannosylation
- Enzymatic activity
- Glycosylation
- Lipoprotein lipase
- Secretion
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation. / Okamoto, Sawako; Murano, Takeyoshi; Suzuki, Takehiro; Uematsu, Shiho; Niwa, Yuki; Sasazawa, Yukiko; Dohmae, Naoshi; Bujo, Hideaki; Simizu, Siro.
In: Biochemical and Biophysical Research Communications, Vol. 486, No. 2, 29.04.2017, p. 558-563.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation
AU - Okamoto, Sawako
AU - Murano, Takeyoshi
AU - Suzuki, Takehiro
AU - Uematsu, Shiho
AU - Niwa, Yuki
AU - Sasazawa, Yukiko
AU - Dohmae, Naoshi
AU - Bujo, Hideaki
AU - Simizu, Siro
PY - 2017/4/29
Y1 - 2017/4/29
N2 - 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.
AB - 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.
KW - C-mannosylation
KW - Enzymatic activity
KW - Glycosylation
KW - Lipoprotein lipase
KW - Secretion
UR - http://www.scopus.com/inward/record.url?scp=85015988665&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85015988665&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2017.03.085
DO - 10.1016/j.bbrc.2017.03.085
M3 - Article
C2 - 28327359
AN - SCOPUS:85015988665
VL - 486
SP - 558
EP - 563
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -