Hitomi T, Yanagi S, Inatome R, Yamamura H
Department of Biochemistry, Kobe University School of Medicine, Japan.
FEBS Lett. 1999 Feb 26;445(2-3):371-4. doi: 10.1016/s0014-5793(99)00153-2.
Phospholipase D (PLD) has been proposed to play a key role in the signal transduction of cellular responses to various extracellular signals. Herein we provide biochemical and genetic evidence that cross-linking of the B cell receptor (BCR) induces rapid activation of PLD through a Syk-, Btk- and phospholipase C (PLC)-gamma2-dependent pathway in DT40 cells. Activation of PLD upon BCR engagement is completely blocked in Syk- or Btk-deficient cells, but unaffected in Lyn-deficient cells. Furthermore, in PLC-gamma2-deficient cells, BCR engagement failed to activate PLD. These results demonstrate that Syk, Btk and PLC-gamma2 are essential for BCR-induced PLD activation.
磷脂酶D（PLD）被认为在细胞对各种细胞外信号的反应的信号转导中起关键作用。在此，我们提供生物化学和遗传学证据，证明B细胞受体（BCR）的交联通过Syk、Btk和磷脂酶C（PLC）-γ2依赖性途径在DT40细胞中诱导PLD的快速激活。在缺乏Syk或Btk的细胞中，BCR结合后PLD的激活被完全阻断，但在缺乏Lyn的细胞中不受影响。此外，在缺乏PLC-γ2的细胞中，BCR结合未能激活PLD。这些结果表明，Syk、Btk和PLC-γ2对于BCR诱导的PLD激活至关重要。
