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

研究成果: Article

8 引用 (Scopus)

抄録

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
486
発行部数2
DOI
出版物ステータスPublished - 2017 4 29

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Lipoprotein Lipase
Hypertriglyceridemia
Lipid Metabolism
Mass spectrometry
Mass Spectrometry
Cells
Cell Line
Enzymes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

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.

:: Biochemical and Biophysical Research Communications, 巻 486, 番号 2, 29.04.2017, p. 558-563.

研究成果: Article

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, 巻. 486, 番号 2, pp. 558-563. https://doi.org/10.1016/j.bbrc.2017.03.085
Okamoto, Sawako ; Murano, Takeyoshi ; Suzuki, Takehiro ; Uematsu, Shiho ; Niwa, Yuki ; Sasazawa, Yukiko ; Dohmae, Naoshi ; Bujo, Hideaki ; Simizu, Siro. / Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation. :: Biochemical and Biophysical Research Communications. 2017 ; 巻 486, 番号 2. pp. 558-563.
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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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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

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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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KW - Glycosylation

KW - Lipoprotein lipase

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