title: Truncated Tau with the Fyn-binding domain and without the microtubule-binding domain hinders the myelinating capacity of an oligodendrocyte cell line.
abstract: 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.
authors.affiliation: Department of Medical Science, School of Veterinary Medicine, University of Wisconsin, Madison, Wisconsin, USA.
authors.forename: Abdelmadjid
authors.initials: A
authors.lastname: Belkadi
authors.forename: Patrizia
authors.initials: P
authors.lastname: LoPresti
mesh_terms: D020816:Amino Acid Motifs / Q000502:physiology; D000818:Animals; D002461:Cell Line, Transformed; D017690:Cell Transplantation / Q000379:methods; D003711:Demyelinating Diseases / Q000235:genetics / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism*; D009154:Mutation; D009186:Myelin Sheath / Q000378:metabolism* / Q000473:pathology / Q000648:ultrastructure; D009836:Oligodendroglia / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D051076:Proto-Oncogene Proteins c-fyn / Q000378:metabolism*; D051381:Rats; D011922:Rats, Mutant Strains; D013119:Spinal Cord Injuries / Q000601:surgery; D014162:Transfection / Q000379:methods; D016875:tau Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D016875:tau Proteins; C494957:FYN protein, human; D051076:Proto-Oncogene Proteins c-fyn