ausblenden:
Schlagwörter:
myelin protein evolution; Pelizaeus-Merzbacher disease; PLP/DM20; Gpm6a; Gpm6b; tetraspan transmembrane proteins; alternative splicing; teleostei; genome duplication; nerve regeneration; ascidian Ciona intestinalis; Drosophila melanogaster; Apis mellifera; Anopheles gambiae; Danio rerio; CNS regeneration; remyelination; neurite outgrowth; optic nerve lesion CENTRAL-NERVOUS-SYSTEM; PELIZAEUS-MERZBACHER-DISEASE; FATTY-ACID-COMPOSITION; CNS MYELIN; SPINAL-CORD; ADHESIVE PROPERTIES; PERIPHERAL MYELIN; OPTIC-NERVE; RAT-BRAIN; OLIGODENDROCYTE PROGENITORS
Zusammenfassung:
The coevolution of neurons and their supporting glia to the highly specialized axon-myelin unit included the recruitment of proteolipids as neuronal glycoproteins (DM beta, DM gamma) or myelin proteins (DM alpha/PLP/DM20). Consistent with a genome duplication at the root of teleosts, we identified three proteolipid pairs in zebrafish, termed DM alpha 1 and DM alpha 2, DM beta 1 and DM beta 2, DM gamma 1 and DM gamma 2. The paralogous amino acid sequences diverged remarkably after gene duplication, indicating functional specialization. Each proteolipid has adopted a distinct spatio-temporal expression pattern in neural progenitors, neurons, and in glia. DM alpha 2, the closest homolog to mammalian PLP/DM20, is coexpressed with P0 in oligodendrocytes and upregulated after optic nerve lesion. DM gamma 2 is expressed in multipotential stem cells, and the other four proteolipids are confined to subsets of CNS neurons. Comparing protein sequences and gene structures from birds, teleosts, one urochordate species, and four invertebrates, we have reconstructed major steps in the evolution of proteolipids. (C) 2005 Elsevier Inc. All rights reserved.