Boudot Cédric, Dassé Emilie, Lambert Elise, Kadri Zahra, Mayeux Patrick, Chrétien Stany, Haye Bernard, Billat Claudine, Petitfrère Emmanuelle
Laboratoire de Biochimie, CNRS FRE 2534, IFR 53 Biomolécules, UFR Sciences Exactes et Naturelles, BP 1039, Université de Reims Champagne-Ardenne, 51687 Reims Cedex 2, France.
Biochem Biophys Res Commun. 2003 Jan 10;300(2):437-42. doi: 10.1016/s0006-291x(02)02866-8.
We examined the role of the Src kinase Lyn in phospholipase C-gamma 2 (PLC-gamma 2) and phosphatidylinositol (PI) 3-kinase activation in erythropoietin (Epo)-stimulated FDC-P1 cells transfected with a wild type (WT) Epo-receptor (Epo-R). We showed that two inhibitors of Src kinases, PP1 and PP2, abolish both PLC-gamma 2 tyrosine phosphorylation and PI 3-kinase activity in WT Epo-R FDC-P1 cells. We also demonstrated that Epo-phosphorylated Lyn is associated with tyrosine phosphorylated PLC-gamma 2 and PI 3-kinase in WT Epo-R FDC-P1-stimulated cells. Moreover Epo-activated Lyn phosphorylates in vitro PLC-gamma 2 immunoprecipitated from unstimulated cells. Our results suggest that the Src kinase Lyn is involved in PLC-gamma 2 phosphorylation and PI 3-kinase activation induced by Epo.
我们研究了Src激酶Lyn在促红细胞生成素(Epo)刺激的、转染了野生型(WT)促红细胞生成素受体(Epo-R)的FDC-P1细胞中,对磷脂酶C-γ2(PLC-γ2)和磷脂酰肌醇(PI)3激酶激活的作用。我们发现,两种Src激酶抑制剂PP1和PP2,可消除WT Epo-R FDC-P1细胞中PLC-γ2的酪氨酸磷酸化和PI 3激酶活性。我们还证明,在WT Epo-R FDC-P1刺激的细胞中,Epo磷酸化的Lyn与酪氨酸磷酸化的PLC-γ2和PI 3激酶相关。此外,Epo激活的Lyn可在体外磷酸化从未刺激细胞中免疫沉淀的PLC-γ2。我们的结果表明,Src激酶Lyn参与了Epo诱导的PLC-γ2磷酸化和PI 3激酶激活。