Nuclear protein kinases in rat liver: evidence for increased histone H1 phosphorylating activity during liver regeneration

Exp Cell Res. 1991 Jul;195(1):255-62. doi: 10.1016/0014-4827(91)90525-y.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Alkaloids / pharmacology
  • Animals
  • Histones / metabolism*
  • Liver / metabolism
  • Liver Regeneration*
  • Male
  • Nuclear Proteins / metabolism*
  • Phosphoprotein Phosphatases / metabolism
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism
  • Protein Kinases / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Staurosporine
  • Substrate Specificity
  • Time Factors

Substances

  • Alkaloids
  • Histones
  • Nuclear Proteins
  • Phosphoproteins
  • Adenosine Triphosphate
  • Protein Kinases
  • Protein Kinase C
  • Phosphoprotein Phosphatases
  • Staurosporine