Yamamoto T, Matsuda T, Junicho A, Kishi H, Yoshimura A, Muraguchi A
Department of Immunology, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Sugitani, Toyama, Japan.
FEBS Lett. 2001 Mar 2;491(3):272-8. doi: 10.1016/s0014-5793(01)02208-6.
To investigate the roles of various hematopoietic cell-specific adapter proteins in T cell receptor (TCR)-signaling leading to nuclear factor of activated T cell (NF-AT) and nuclear factor of kappaB (NF-kappaB) activation, we reconstituted TCR-signaling with CD8/zeta, various protein tyrosine kinases (PTKs), and adapter proteins in a non-lymphoid cell line, 293T. We show that SLP-76 and BLNK, but not LAT, effectively co-operated with Syk and Tec family PTKs to activate NF-AT and NF-kappaB. We also show that Tec family PTKs enhanced endogenous phospholipase C (PLC)-gamma1 phosphorylation induced by CD8/zeta and Syk in 293T cells. These results imply that PLC-gamma1 may play a critical role in a hematopoietic cell-specific adapter protein-mediated NF-AT and NF-kappaB activation in a non-lymphoid cell.
为了研究各种造血细胞特异性衔接蛋白在导致活化T细胞核因子（NF-AT）和核因子κB（NF-κB）激活的T细胞受体（TCR）信号传导中的作用，我们在非淋巴细胞系293T中用CD8/ζ、各种蛋白酪氨酸激酶（PTK）和衔接蛋白重建了TCR信号传导。我们发现，SLP-76和BLNK而非LAT能有效地与Syk和Tec家族PTK协同作用，激活NF-AT和NF-κB。我们还发现，Tec家族PTK增强了293T细胞中由CD8/ζ和Syk诱导的内源性磷脂酶C（PLC）-γ1磷酸化。这些结果表明，PLC-γ1可能在非淋巴细胞中造血细胞特异性衔接蛋白介导的NF-AT和NF-κB激活中起关键作用。
