The fatty acid binding protein FABP7 is required for optimal oligodendrocyte differentiation during myelination but not during remyelination

Sarah Foerster, Alerie Guzman de la Fuente, Yoshiteru Kagawa, Theresa Bartels, Yuji Owada, Robin J.M. Franklin

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

The major constituents of the myelin sheath are lipids, which are made up of fatty acids (FAs). The hydrophilic environment inside the cells requires FAs to be bound to proteins, preventing their aggregation. Fatty acid binding proteins (FABPs) are one class of proteins known to bind FAs in a cell. Given the crucial role of FAs for myelin sheath formation we investigated the role of FABP7, the major isoform expressed in oligodendrocyte progenitor cells (OPCs), in developmental myelination and remyelination. Here, we show that the knockdown of Fabp7 resulted in a reduction of OPC differentiation in vitro. Consistent with this result, a delay in developmental myelination was observed in Fabp7 knockout animals. This delay was transient with full myelination being established before adulthood. FABP7 was dispensable for remyelination, as the knockout of Fapb7 did not alter remyelination efficiency in a focal demyelination model. In summary, while FABP7 is important in OPC differentiation in vitro, its function is not crucial for myelination and remyelination in vivo.

Original languageEnglish
Pages (from-to)1410-1420
Number of pages11
JournalGlia
Volume68
Issue number7
DOIs
Publication statusPublished - 2020 Jul 1

Keywords

  • OPC
  • fatty acid binding protein
  • myelination
  • remyelination

ASJC Scopus subject areas

  • Neurology
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'The fatty acid binding protein FABP7 is required for optimal oligodendrocyte differentiation during myelination but not during remyelination'. Together they form a unique fingerprint.

Cite this