Nuclear protein kinases in rat liver: evidence for increased histone H1 phosphorylating activity during liver regeneration.
Comparison of protein kinase activity in normal and regenerating rat liver nuclei indicates that exogenous histone H1 is hyperphosphorylated in 22-h regenerating nuclei. The protein kinase involved is not sensitive to protein kinase A inhibitor, is inhibited by staurosporine and by an anti-PKC polyclonal antibody, utilizes only ATP, and also phosphorylates the C-terminal fragment of histone H1. These data suggest that protein kinase C is responsible for the observed effects, in agreement with the presence of this enzyme in normal and regenerating nuclei demonstrated by immunoblotting.
Martelli
A M
AM
Istituto di Anatomia Umana Normale, Università di Bologna Ferrara, Italy.
Carini
C
C
Marmiroli
S
S
Mazzoni
M
M
Barker
P J
PJ
Gilmour
R S
RS
Capitani
S
S
D000255:Adenosine Triphosphate / Q000378:metabolism; D000470:Alkaloids / Q000494:pharmacology; D000818:Animals; D006657:Histones / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D008115:Liver Regeneration; D008297:Male; D009687:Nuclear Proteins / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D019311:Staurosporine; D013379:Substrate Specificity; D013997:Time Factors
D000470:Alkaloids; D006657:Histones; D009687:Nuclear Proteins; D010750:Phosphoproteins; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D011493:Protein Kinase C; D010749:Phosphoprotein Phosphatases; D019311:Staurosporine