Billi A M, Matteucci A, Bertagnolo V, Previati M, Manzoli F A, Capitani S
Institute of Human Anatomy, University of Bologna, Italy.
Cell Biol Int Rep. 1991 May;15(5):409-26. doi: 10.1016/0309-1651(91)90129-7.
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.
从鼠类红白血病细胞（弗瑞德细胞）中分离出的核基质，已用γ-32P-ATP和纯化的蛋白激酶C进行磷酸化处理，以便鉴定该酶的特定核底物。已采用六亚甲基双乙酰胺诱导细胞分化，并比较红系分化后磷酸化谱的变化。已发现，在从未诱导细胞中纯化出的核基质中，层粘连蛋白B被大鼠脑PK-C过度磷酸化。这种差异在六亚甲基双乙酰胺处理14至72小时的细胞中表现明显，表明层粘连蛋白B被PK-C磷酸化的能力与分化状态有关。PK-C参与层粘连蛋白的磷酸化可能代表红系分化剂靶向细胞核所利用的信号通路的早期步骤。
