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Phosphorylation of Nuclear Proteins in Myelinating Oligodendrocytes and Its Control by Cyclic AMP
Author(s) -
SatoBigbee Carmen,
Yu Robert K.
Publication year - 1991
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.1471-4159.1991.tb06364.x
Subject(s) - myelinogenesis , phosphorylation , biology , protein phosphorylation , polyacrylamide gel electrophoresis , biochemistry , molecular mass , gel electrophoresis , incubation , chromatin , intracellular , oligodendrocyte , microbiology and biotechnology , myelin , protein kinase a , endocrinology , central nervous system , enzyme , dna
: Oligodendroglial nuclei isolated from rat brains at different stages of myelinogenesis (10,18, and 30 days of age) were incubated with (γ‐ 32 P]ATP and extracted with 0.75 M perchloric acid to yield a fraction of nonacidic chromatin proteins. The protein extracts were then analyzed by poly‐acrylamide gel electrophoresis. The phosphorylation pattern of these proteins was found to be different for different age groups. In 10‐day‐old rat Oligodendrocytes the most extensive phosphorylation occurred in low molecular mass species (<30 kDa), in contrast to fractions obtained from 18‐and 30‐day‐old rat Oligodendrocytes which showed a significantly higher labeling of the proteins with molecular masses >30 kDa. The phosphorylation of the latter species was greatly stimulated by the presence of cyclic AMP in the incubation media. The results suggest that the phosphorylation of specific nuclear proteins, which may play a regulatory role at different stages of oligodendroglial maturation and myelinogenesis, may be at least partially modulated by intracellular cyclic AMP.