磷脂酶C-γ1与T细胞中CD3结构的关联
Phospholipase C-gamma 1 association with CD3 structure in T cells.
作者信息
Dasgupta J D, Granja C, Druker B, Lin L L, Yunis E J, Relias V
机构信息
Division of Immunogenetics, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.
出版信息
J Exp Med. 1992 Jan 1;175(1):285-8. doi: 10.1084/jem.175.1.285.
Abstract
Recently, we and others have reported tyrosine phosphorylation of phospholipase C-gamma 1 (PLC gamma 1) enzyme after CD3 activation of T cells, and have proposed that PLC gamma 1 mediates signal transduction through the T cell receptor (TCR/CD3). Here, using immunoblotting and immune complex PLC assays, we show that CD3 stimulation of Jurkat cells induces the association of PLC gamma 1 enzyme with CD3 complex. PLC activity is also found to co-precipitate with the CD3 zeta chain from activated cells. In addition, in vitro PLC assays show that CD3 activation leads to about 10-fold stimulation of PLC gamma 1 activity. These results, along with the observation that Jurkat cells preferentially express PLC gamma 1, indicate that PLC gamma 1 participates in CD3 signaling.
摘要
最近，我们和其他研究人员报道了T细胞经CD3激活后磷脂酶C-γ1（PLCγ1）酶发生酪氨酸磷酸化，并提出PLCγ1通过T细胞受体（TCR/CD3）介导信号转导。在此，我们运用免疫印迹和免疫复合物PLC检测法，发现对Jurkat细胞进行CD3刺激可诱导PLCγ1酶与CD3复合物结合。还发现PLC活性可与活化细胞中的CD3ζ链共沉淀。此外，体外PLC检测表明，CD3激活可使PLCγ1活性增强约10倍。这些结果，连同Jurkat细胞优先表达PLCγ1这一观察结果，表明PLCγ1参与CD3信号传导。
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