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Major Central Nervous System Myelin Glycoprotein of the African Lungfish ( Protopterus dolloi ) Cross‐Reacts with Myelin Proteolipid Protein Antibodies, Indicating a Close Phylogenetic Relationship with Amphibians
Author(s) -
Waehneldt T. V.,
Matthieu J.M.,
Jeserich †G.
Publication year - 1986
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.1471-4159.1986.tb01752.x
Subject(s) - proteolipid protein 1 , myelin , myelin proteolipid protein , biology , concanavalin a , biochemistry , myelin basic protein , microbiology and biotechnology , central nervous system , endocrinology , in vitro
CNS myelin was isolated from the spinal cord of the African lungfish Protopterus dolloi. Its proteins consisted of (1) two basic proteins (16,000 and 18,500 apparent M r ) that reacted with anti‐human CNS myelin basic protein antibodies and (2) a major protein (29,000 apparent M r ) that stained with concanavalin A‐horseradish peroxidase and bound to anti‐rat CNS myelin proteolipid protein (PLP) antibodies. This dominant 29,000 M r protein showed no reaction with antibodies against the major bovine PNS myelin glycoprotein P 0 . Following treatment with endoglycosidase F the 29,000 M r protein was reduced in size to a 26,000 apparent M r component that no longer bound concanavalin A but retained the anti‐PLP reactivity. These results agree with a concanavalin A‐binding oligosaccharide linked through asparagine to a protein backbone of PLP homology. The major 29,000 M r lungfish CNS myelin protein was therefore termed g‐PLP (glycosylated proteolipid protein). This is the first report demonstrating the occurrence of a PLP‐cross‐reactive protein in CNS myelin of a fish. It attests to the close phylogenetic relationship of lungfishes to amphibians. Amphibians were previously recognized as the oldest class bearing PLP in its CNS myelin.