Wu C J, Chen Z, Ullrich A, Greene M I, O'Rourke D M
Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, PA 19104, USA.
Oncogene. 2000 Aug 17;19(35):3999-4010. doi: 10.1038/sj.onc.1203748.
Several growth factors and cytokines, including EGF, are known to induce tyrosine phosphorylation of Signal Regulatory Proteins (SIRPs). Consistent with the idea that increased phosphorylation activates SIRP function, we overexpressed human SIRPalpha1 in U87MG glioblastoma cells in order to examine how SIRPalpha1 modulates EGFR signaling pathways. Endogenous EGFR proteins are overexpressed in U87MG cells and these cells exhibit survival and motility phenotypes that are influenced by EGFR kinase activity. Overexpression of the SIRPalpha1 cDNA diminished EGF-induced phosphoinositide-3-OH kinase (PI3-K) activation in U87MG cells. Reduced EGF-stimulated activation of PI3-K was mediated by interactions between carboxyl terminus of SIRPalpha1 and the Src homology-2 (SH2)-containing phosphotyrosine phosphatase, SHP2. SIRPalpha1 overexpression also reduced the EGF-induced association between SHP2 and the p85 regulatory subunit of PI3-K. Inhibition of transformation and enhanced apoptosis following gamma-irradiation were observed in SIRPalpha1-overexpressing U87MG cells, and enhanced apoptosis was associated with reduced levels of bcl-xL protein. Furthermore, SIRPalpha1-overexpressing U87MG cells displayed reduced cell migration and cell spreading that was mediated by association between SIRPalpha1 and SHP2. However, SIRPalpha1-overexpressing U87MG clonal derivatives exhibited no differences in cell growth or levels of mitogen-activated protein kinase (MAPK) activation. These data reveal a pathway that negatively regulates EGFR-induced PI3-K activation in glioblastoma cells and involves interactions between SHP2 and tyrosine phosphorylated SIRPalpha1. These results also suggest that negative regulation of PI3-K pathway activation by the SIRP family of transmembrane receptors may diminish EGFR-mediated motility and survival phenotypes that contribute to transformation of glioblastoma cells. Oncogene (2000) 19, 3999 - 4010.
包括表皮生长因子(EGF)在内的多种生长因子和细胞因子,已知可诱导信号调节蛋白(SIRP)的酪氨酸磷酸化。与磷酸化增加会激活SIRP功能这一观点相一致,我们在U87MG胶质母细胞瘤细胞中过表达人SIRPα1,以研究SIRPα1如何调节表皮生长因子受体(EGFR)信号通路。内源性EGFR蛋白在U87MG细胞中过表达,并且这些细胞表现出受EGFR激酶活性影响的存活和运动表型。SIRPα1 cDNA的过表达减少了U87MG细胞中EGF诱导的磷酸肌醇-3-羟基激酶(PI3-K)的激活。PI3-K的EGF刺激激活减少是由SIRPα1的羧基末端与含Src同源2(SH2)结构域的磷酸酪氨酸磷酸酶SHP2之间的相互作用介导的。SIRPα1的过表达还减少了EGF诱导的SHP2与PI3-K的p85调节亚基之间的结合。在过表达SIRPα1的U87MG细胞中观察到γ射线照射后转化的抑制和凋亡的增强,并且凋亡增强与bcl-xL蛋白水平降低有关。此外,过表达SIRPα1的U87MG细胞显示出细胞迁移和细胞铺展减少,这是由SIRPα1与SHP2之间的结合介导的。然而,过表达SIRPα1的U87MG克隆衍生物在细胞生长或丝裂原活化蛋白激酶(MAPK)激活水平上没有差异。这些数据揭示了一条在胶质母细胞瘤细胞中负向调节EGFR诱导的PI3-K激活的途径,并涉及SHP2与酪氨酸磷酸化的SIRPα1之间的相互作用。这些结果还表明,跨膜受体SIRP家族对PI3-K途径激活的负向调节可能会减少EGFR介导的运动和存活表型,而这些表型有助于胶质母细胞瘤细胞的转化。《癌基因》(2000年)19卷,3999 - 401页。