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The fatty acid binding protein FABP7 is required for optimal oligodendrocyte differentiation during myelination but not during remyelination
Author(s) -
Foerster Sarah,
Guzman de la Fuente Alerie,
Kagawa Yoshiteru,
Bartels Theresa,
Owada Yuji,
Franklin Robin J. M.
Publication year - 2020
Publication title -
glia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.954
H-Index - 164
eISSN - 1098-1136
pISSN - 0894-1491
DOI - 10.1002/glia.23789
Subject(s) - remyelination , biology , myelin , galactocerebroside , gene knockdown , oligodendrocyte , myelin basic protein , microbiology and biotechnology , in vivo , knockout mouse , progenitor cell , immunology , biochemistry , stem cell , neuroscience , central nervous system , gene , genetics
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.