Protein-tyrosine kinase, Syk, is required for CXCL12-induced polarization of B cells
Protein-tyrosine kinase, Syk, is required for CXCL12-induced polarization of B cells
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DOI：
10.1016/j.bbrc.2005.01.076
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发表时间：
2005-03-25
影响因子：
3.1
通讯作者：
Yamamura, H
中科院分区：
文献类型：
--
作者：
Matsusaka, S;Tohyama, Y;Yamamura, H
响应于CXCL 12的细胞极化和迁移对于造血是必不可少的。为了研究Syk在CXCL 12/CXCR 4诱导的信号传导中的作用，将野生型Syk或其显性阴性形式（DN-Syk）引入小鼠pro-B细胞BAF 3中。在CXCL 12刺激下，BAF 3细胞变得极化，形成前缘和收缩尾足，后端运动增加。野生型Syk的过表达引起增强的极化，而DN-Syk抑制细胞极性，由于在后端的收缩结构的损失，和改变的表型CXCL 12刺激后增强。含有DN-Syk的突变体BAF 3的运动性独立于CXCL 12刺激而增加。由于PI整合素介导的细胞粘附被抑制，粘附力下降可能会促进运动。CXCL 12刺激导致RhoA的迅速活化，但DN-Syk的表达抑制RhoA活化。这些结果表明，Syk参与CXCL I 2诱导的细胞极化，这与β 1整合素介导的细胞粘附一致。(C)2005年爱思唯尔公司All rights reserved.
Cell polarization and migration in response to CXCL12 is essential for hematopoiesis. To investigate the role of Syk in CXCL12/ CXCR4-induced signaling, wild-type Syk or its dominant-negative form (DN-Syk) was introduced in mouse pro-B cells, BAF3. With CXCL12 stimulation, BAF3 cells became polarized with the formation of a leading edge and contractile uropod at the rear end with increased motility. Overexpression of wild-type Syk caused enhanced polarization, whereas DN-Syk inhibited cell polarity due to the loss of contractile structure at the rear end, and the altered phenotype was enhanced after CXCL 12 stimulation. Motility of mutant BAF3 containing DN-Syk increased independent of CXCL12 stimulation. As PI integrin-mediated cell adhesion was inhibited, decreased adhesion might promote motility. CXCL12 stimulation led to prompt activation of RhoA, but expression of DN-Syk suppressed RhoA activation. These results demonstrate that Syk participates in CXCL I 2-induced cell polarization, which occurs in concert with cell adhesion mediated by beta1 integrin. (C) 2005 Elsevier Inc. All rights reserved.