Protein phosphorylation catalysed by rat brain protein kinase C (PKC) has been studied in nuclei isolated from normal and regenerating rat liver. Histone H1 and a 40,000 molecular weight protein were hyperphosphorylated at all the explored regeneration times, ranging from 3 to 22 h after partial hepatectomy. Phosphorylation of the two substrates was totally dependent on calcium and lipids and was abolished by low concentration of staurosporine. The observed early change of phosphate content of histone H1 and of the 40,000 molecular weight protein on the time scale of liver regeneration suggests that PKC might be involved in the initial nuclear events leading to cell proliferation.

Increased phosphorylation of nuclear substrates for rat brain protein kinase C in regenerating rat liver nuclei

MAZZONI, Meri;CARINI, Cinzia;BERTAGNOLO, Valeria;PREVIATI, Maurizio;CAPITANI, Silvano
Ultimo
1992

Abstract

Protein phosphorylation catalysed by rat brain protein kinase C (PKC) has been studied in nuclei isolated from normal and regenerating rat liver. Histone H1 and a 40,000 molecular weight protein were hyperphosphorylated at all the explored regeneration times, ranging from 3 to 22 h after partial hepatectomy. Phosphorylation of the two substrates was totally dependent on calcium and lipids and was abolished by low concentration of staurosporine. The observed early change of phosphate content of histone H1 and of the 40,000 molecular weight protein on the time scale of liver regeneration suggests that PKC might be involved in the initial nuclear events leading to cell proliferation.
1992
Mazzoni, Meri; Carini, Cinzia; Matteucci, A.; Martelli, A. M.; Bertagnolo, Valeria; Previati, Maurizio; Rana, R.; Cataldi, A.; Capitani, Silvano
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11392/523467
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