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Truncated Tau with the Fyn‐binding domain and without the microtubule‐binding domain hinders the myelinating capacity of an oligodendrocyte cell line
Author(s) -
Belkadi Abdelmadjid,
LoPresti Patrizia
Publication year - 2008
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2008.05600.x
Subject(s) - fyn , myelin , oligodendrocyte , microtubule , microbiology and biotechnology , transfection , neuroscience , spinal cord , biology , cell culture , chemistry , central nervous system , proto oncogene tyrosine protein kinase src , signal transduction , genetics
The mechanisms underlying developmental myelination have therapeutic potential following CNS injury and degeneration. We report that transplanted central glial (CG)‐4 cells had a diminished myelinating capacity in myelin‐deficient ( md ) rats when cells express a mutated form of Tau (Tau [688]), which binds Fyn but not the microtubules. In the brain of the md rats, Tau [688]‐transfected CG‐4 cells displayed a decrease in cellular process outgrowth and myelination; in the spinal cord the extent of myelination rostral and caudal to the injection site was decreased. In contrast, control Tau [605]‐transfected CG‐4 cells formed long cellular processes and substantial areas of myelin both in the brain and spinal cord. In culture, Tau [688]‐transfected CG‐4 cells displayed a decrease in cellular process outgrowth, and Fyn localized largely in the cell body, not the processes. Thus, Tau in oligodendrocytes plays a key role in myelination, and a functional Tau‐Fyn interaction might have therapeutic potential during demyelination and myelin repair following CNS injury and degeneration.