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

Research output: Contribution to journalArticle

11 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 languageEnglish
Pages (from-to)558-563
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume486
Issue number2
DOIs
Publication statusPublished - 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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