Phosphorylation of HMG proteins during change in the chromatin transcription activity of neuronal and glial nuclei of the rat brain
Kulikova, O.G.; Bogdanova, N.A.
Biokhimiia 58(7): 1047-1052
1993
ISSN/ISBN: 0320-9725 PMID: 8395901 Document Number: 406916
The level of cAMP-independent phosphorylation of chromatin, the amount of weakly bound nonhistone proteins and the degree of their phosphorylation in neuronal cells are more significant than the corresponding parameters in glial cells. The mnemic stimulator ethylnorantipheine (ethymizol) increases the level of neuronal chromatin phosphorylation. In contrast, alkylnorantipheine aggravating mnemic processes decreases the phosphorylation. No effect of antipheines on phosphorylation of weakly bound proteins of glial chromatin was found. It is known that whereas ethymizol activates only neuronal, but not glial chromatin transcription, allylnorantipheine inhibits neuronal transcription. The activities of purified casein kinases N I and N II are much higher in neuronal chromatin than in glia. Antipheines have no effect on the activity of casein kinase N I but selectively modulate the phosphorylation of HMG 14 by casein kinase N II of neuronal and glial chromatin. The role of phosphorylated forms of HMG proteins and casein kinases of chromatin in regulation of the genome activity is discussed.