Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation

Sawako Okamoto; Takeyoshi Murano; Takehiro Suzuki; Shiho Uematsu; Yuki Niwa; Yukiko Sasazawa; Naoshi Dohmae; Hideaki Bujo; Siro Simizu

doi:10.1016/j.bbrc.2017.03.085

Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation

Sawako Okamoto, Takeyoshi Murano, Takehiro Suzuki, Shiho Uematsu, Yuki Niwa, Yukiko Sasazawa, Naoshi Dohmae, Hideaki Bujo, Siro Simizu

Department of Applied Chemistry

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

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	https://doi.org/10.1016/j.bbrc.2017.03.085
Publication status	Published - 2017 Apr 29

Keywords

C-mannosylation
Enzymatic activity
Glycosylation
Lipoprotein lipase
Secretion

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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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 › peer-review

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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.",

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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

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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.

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