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
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Alkaloids / pharmacology
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Animals
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Histones / metabolism*
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Liver / metabolism
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Liver Regeneration*
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Male
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Nuclear Proteins / metabolism*
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Phosphoprotein Phosphatases / metabolism
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Phosphoproteins / metabolism*
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Phosphorylation
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Protein Kinase C / antagonists & inhibitors
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Protein Kinase C / metabolism
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Protein Kinases / metabolism*
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Rats
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Rats, Inbred Strains
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Staurosporine
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Substrate Specificity
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Time Factors
Substances
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Alkaloids
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Histones
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Nuclear Proteins
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Phosphoproteins
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Adenosine Triphosphate
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Protein Kinases
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Protein Kinase C
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Phosphoprotein Phosphatases
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Staurosporine