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

Meri Mazzoni, Cinzia Carini, Alessandro Matteucci, Alberto Maria Martelli, Valeria Bertagnolo, Maurizio Previati, Rosalba Rana, Amelia Cataldi, Silvano Capitani

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)313-319
Number of pages7
JournalCellular Signalling
Volume4
Issue number3
DOIs
Publication statusPublished - 1992

Keywords

  • histone H1
  • liver regeneration
  • nucleus
  • phosphorylation
  • Protein kinase C
  • staurosporine

ASJC Scopus subject areas

  • Cell Biology

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  • Cite this

    Mazzoni, M., Carini, C., Matteucci, A., Martelli, A. M., Bertagnolo, V., Previati, M., Rana, R., Cataldi, A., & Capitani, S. (1992). Increased phosphorylation of nuclear substrates for rat brain protein kinase C in regenerating rat liver nuclei. Cellular Signalling, 4(3), 313-319. https://doi.org/10.1016/0898-6568(92)90071-F