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Myelin Composition and Activities of CNPase and Na + , K + ‐ATPase in Hypomyelinated “pt” Mutant Rabbit
Author(s) -
DomańskaJanik K.,
Gajkowska B.,
Nkhaud B.,
Bourre J. M.
Publication year - 1988
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.1471-4159.1988.tb13238.x
Subject(s) - myelin , myelin basic protein , biology , mutant , biochemistry , microbiology and biotechnology , chemistry , central nervous system , endocrinology , gene
A disorder of CNS myelination was found in paralytic tremor (“pt”) rabbits. The condition is inherited in a sex‐linked recessive mode. Ultrastructurally, an obvious myelin deficiency with aberration of myelin sheath formation is observed. The yield of myelin isolation was reduced to 20–30% of control. Myelin isolated from 4‐week‐old “pt” rabbits contained reduced amounts of galactosphingolipids and of several myelin protein markers. Moreover, myelin basic protein, analyzed by two‐dimensional gel electrophoresis, showed a deficit in its more basic components. All these facts suggest a delay in myelin maturation. Ganglioside content was increased as well as Na + , K + ‐ATPase specific activity. 2′,3′‐Cyclic nucleotide phosphodiesterase (CNPase) specific activity was the same in “pt” as in control myelin but differed by having greater sensitivity to detergent activation.