Conservation of the carboxyl terminal epitope of myelin proteolipid protein in the tetrapods and lobe-finned fish.
Immunochemical analysis of the myelin proteolipid protein (PLP) has identified the carboxyl terminal amino acid phenylalanine 276 as the only PLP epitope conserved between the PLP components of rat and lungfish, species representing the phylogenetically most widely separated groups that synthesise typical CNS myelin. Immunoblotting using a rabbit antiserum raised against the carboxyl terminal sequence of rat PLP (residues 257-276) identified this epitope on the PLP components of both tetrapod (rat, chicken, lizard, and frog) and lobe-finned fish (coelacanth and lungfish) CNS myelin, including the DM-20 isoform of PLP, which is restricted to rat, chicken, and lizard CNS myelin. The conservation of the carboxyl terminus of PLP during evolution suggests this structure may play an important role in maintaining the organisation and function of PLP in the myelin membrane.
Section of Neurology, University of Wales College of Medicine, Cardiff.
C
C
Linington
T V
TV
Waehneldt
D000818:Animals; D001059:Apoproteins / Q000276:immunology* / Q000378:metabolism; D002490:Central Nervous System / Q000378:metabolism; D002645:Chickens; D004586:Electrophoresis; D000939:Epitopes; D005399:Fishes; D006031:Glycosylation; D007106:Immune Sera / Q000276:immunology; D015151:Immunoblotting; D007120:Immunochemistry; D008116:Lizards; D009185:Myelin Proteins / Q000276:immunology* / Q000378:metabolism; D018991:Myelin Proteolipid Protein; D011817:Rabbits; D011894:Rana pipiens; D051381:Rats
D001059:Apoproteins; D000939:Epitopes; D007106:Immune Sera; D009185:Myelin Proteins; D018991:Myelin Proteolipid Protein