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

応用化学科

研究成果: Article

11 引用（Scopus）

抜粋

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.

元の言語	English
ページ（範囲）	558-563
ページ数	6
ジャーナル	Biochemical and Biophysical Research Communications
巻	486
発行部数	2
DOI	https://doi.org/10.1016/j.bbrc.2017.03.085
出版物ステータス	Published - 2017 4 29

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

文献にアクセス

10.1016/j.bbrc.2017.03.085

フィンガープリント Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

これを引用

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

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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.",

keywords = "C-mannosylation, Enzymatic activity, Glycosylation, Lipoprotein lipase, Secretion",

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

year = "2017",

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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

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