Cell recognition molecule L1 promotes embryonic stem cell differentiation through the regulation of cell surface glycosylation

Biochem Biophys Res Commun. 2013 Oct 25;440(3):405-12. doi: 10.1016/j.bbrc.2013.09.082. Epub 2013 Sep 23.

Abstract

Cell recognition molecule L1 (CD171) plays an important role in neuronal survival, migration, differentiation, neurite outgrowth, myelination, synaptic plasticity and regeneration after injury. Our previous study has demonstrated that overexpressing L1 enhances cell survival and proliferation of mouse embryonic stem cells (ESCs) through promoting the expression of FUT9 and ST3Gal4, which upregulates cell surface sialylation and fucosylation. In the present study, we examined whether sialylation and fucosylation are involved in ESC differentiation through L1 signaling. RNA interference analysis showed that L1 enhanced differentiation of ESCs into neurons through the upregulation of FUT9 and ST3Gal4. Furthermore, blocking the phospholipase Cγ (PLCγ) signaling pathway with either a specific PLCγ inhibitor or knockdown PLCγ reduced the expression levels of both FUT9 and ST3Gal4 mRNAs and inhibited L1-mediated neuronal differentiation. These results demonstrate that L1 promotes neuronal differentiation from ESCs through the L1-mediated enhancement of FUT9 and ST3Gal4 expression.

Keywords: Cell differentiation; ESC (embryonic stem cell); Glycosylation; L1; PLCγ.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane / metabolism*
  • Embryonic Stem Cells / cytology*
  • Fucosyltransferases / genetics
  • Fucosyltransferases / metabolism
  • Glycosylation
  • Humans
  • Mice
  • Neural Cell Adhesion Molecule L1 / genetics
  • Neural Cell Adhesion Molecule L1 / physiology*
  • Neurogenesis / genetics
  • Neurogenesis / physiology*
  • Phospholipase C gamma / antagonists & inhibitors
  • Phospholipase C gamma / genetics
  • Phospholipase C gamma / metabolism
  • RNA Interference
  • Sialyltransferases / genetics
  • Sialyltransferases / metabolism
  • beta-Galactoside alpha-2,3-Sialyltransferase

Substances

  • Neural Cell Adhesion Molecule L1
  • Fucosyltransferases
  • fucosyltransferase 9, mouse
  • Sialyltransferases
  • Phospholipase C gamma
  • beta-Galactoside alpha-2,3-Sialyltransferase