In vitro phosphorylation of lamin B by protein kinase C in friend erythroleukemia. Effect of chemically induced differentiation

Anna Maria Billi, Alessandro Matteucci, Valeria Bertagnolo, Maurizio Previati, Francesco A. Manzoli, Silvano Capitani

Research output: Contribution to journalArticlepeer-review

Abstract

Nuclear matrix isolated from murine erythroleukemia cells (Friend cells) has been phosphorylated with gamma 32P-ATP and purified protein kinase C in order to identify specific nuclear substrates for the enzyme. HMBA has been employed to induce the cell to differentiate and to compare the changes of phosphorylation profile after erythroid differentiation. Lamin B has been found to be hyperphosphorylated by rat brain PK-C in nuclear matrix purified from uninduced cells. This difference characterizes the cells from 14 to 72 hrs of HMBA treatment and indicates that the ability of lamin B to be phosphorylated by PK-C is linked to the differentiated state. The involvement of PK-C in lamin phosphorylation might represent an early step of the signalling pathway utilized by erythroid differentiating agents to target the cell nucleus.

Original languageEnglish
Pages (from-to)409-426
Number of pages18
JournalCell Biology International Reports
Volume15
Issue number5
DOIs
Publication statusPublished - 1991

ASJC Scopus subject areas

  • Cell Biology

Fingerprint Dive into the research topics of 'In vitro phosphorylation of lamin B by protein kinase C in friend erythroleukemia. Effect of chemically induced differentiation'. Together they form a unique fingerprint.

Cite this