A glycosylated proteolipid protein is common to CNS myelin of recent lungfish (Ceratodidae, Lepidosirenidae).
1. Myelin proteins from the CNS of recent lungfish (Lepidosiren paradoxa, Protopterus dolloi, Neoceratodus forsteri) were separated and analysed by staining and immunoblotting. 2. All species showed a glycosylated component (g-PLP) that cross-reacted with antibodies against tetrapod proteolipid protein (PLP), indicating phylogenetic relationships with amphibia. 3. Actinopterygian IP or teleostean 36k components were not detectable in lungfish CNS myelin. 4. The identical size of g-PLPs from Lepidosiren and Protopterus (Mr = 29,000) underlines the close relationship of the Lepidosirenidae. The smaller size of g-PLP from the ceratodidan Neoceratodus forsteri (Mr = 27,500) pointed to an earlier diversion.
D000818:Animals; D005075:Biological Evolution; D002490:Central Nervous System / Q000032:analysis; D005399:Fishes / Q000378:metabolism*; D006031:Glycosylation; D008970:Molecular Weight; D009185:Myelin Proteins / Q000302:isolation & purification*; D018991:Myelin Proteolipid Protein
D009185:Myelin Proteins; D018991:Myelin Proteolipid Protein