Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation

Biochem Biophys Res Commun. 2017 Apr 29;486(2):558-563. doi: 10.1016/j.bbrc.2017.03.085. Epub 2017 Mar 19.

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.

MeSH terms

  • Amino Acid Sequence
  • Cell Line, Tumor
  • Gene Library
  • Glycosylation
  • Hep G2 Cells
  • Humans
  • Lipoprotein Lipase / genetics
  • Lipoprotein Lipase / metabolism*
  • Mannose / metabolism*
  • Mutation
  • Protein Processing, Post-Translational*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*
  • Tryptophan / metabolism*

Substances

  • Recombinant Fusion Proteins
  • Tryptophan
  • Lipoprotein Lipase
  • Mannose