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

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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