| Literature DB >> 1706487 |
T Yoshimura1, T Kobayashi, N Shinnoh, I Goto.
Abstract
In attempts to elucidate mechanisms of demyelination in the twitcher mouse (Twi), phosphorylation and methylation of myelin basic protein (MBP) were examined in the brainstem and spinal cord of this species. Phosphorylation of MBP in isolated myelin by an endogenous kinase and an exogenous [32P]ATP was not impaired and protein kinase C activity in the brain cytosol was not reduced. When the methylation of an arginine residue of MBP was examined in slices of the brainstem and spinal cord, using [3H]methionine as a donor of the methyl groups, no difference was found between Twi and the controls. Radioactivity of the [3H] methionine residue of MBP of Twi was also similar to that of the controls. Thus, accumulation of psychosine in Twi does not interfere with the activity of endogenous kinase, methylation of MBP, and the synthesis and transport of MBP into myelin membrane.Entities:
Mesh:
Substances:
Year: 1990 PMID: 1706487 DOI: 10.1007/bf00965740
Source DB: PubMed Journal: Neurochem Res ISSN: 0364-3190 Impact factor: 3.996