[Phosphorylation of HMG proteins during change in the chromatin transcription activity of neuronal and glial nuclei of the rat brain].
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.
Kulikova
O G
OG
Bogdanova
N A
NA
D000818:Animals; D001921:Brain / Q000166:cytology / Q000378:metabolism*; D047388:Casein Kinases; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism; D005786:Gene Expression Regulation; D006609:High Mobility Group Proteins / Q000378:metabolism*; D009457:Neuroglia / Q000201:enzymology / Q000378:metabolism*; D009474:Neurons / Q000201:enzymology / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D014158:Transcription, Genetic
D002843:Chromatin; D006609:High Mobility Group Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; D047388:Casein Kinases