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

9 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

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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

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 and Biophysical Research Communications, 486(2), 558-563. https://doi.org/10.1016/j.bbrc.2017.03.085

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

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title = "Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation",

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

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AU - Uematsu, Shiho

AU - Niwa, Yuki

AU - Sasazawa, Yukiko

AU - Dohmae, Naoshi

AU - Bujo, Hideaki

AU - Simizu, Siro

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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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10.1016/j.bbrc.2017.03.085