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Increased phosphorylation of nuclear substrates for rat brain protein kinase C in regenerating rat liver nuclei.
Mazzoni, M; Carini, C; Matteucci, A; Martelli, A M; Bertagnolo, V; Previati, M; Rana, R; Cataldi, A; Capitani, S.
Afiliación
  • Mazzoni M; Istituto di Anatomia Umana Normale, Università di Ferrara, Italy.
Cell Signal ; 4(3): 313-9, 1992 May.
Article en En | MEDLINE | ID: mdl-1510879
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.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Encéfalo / Proteína Quinasa C / Núcleo Celular / Hígado / Regeneración Hepática Límite: Animals Idioma: En Revista: Cell Signal Año: 1992 Tipo del documento: Article País de afiliación: Italia
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Encéfalo / Proteína Quinasa C / Núcleo Celular / Hígado / Regeneración Hepática Límite: Animals Idioma: En Revista: Cell Signal Año: 1992 Tipo del documento: Article País de afiliación: Italia