Phosphorylation of focal adhesion kinase promotes extravasation of breast cancer cells
Phosphorylation of focal adhesion kinase promotes extravasation of breast cancer cells
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DOI：
10.1016/j.bbrc.2007.11.181
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发表时间：
2008-02-08
影响因子：
3.1
通讯作者：
Plopper, George E.
中科院分区：
文献类型：
--
作者：
Earley, Sarah;Plopper, George E.
抑制粘着斑激酶（FAK）可延迟乳腺癌细胞的跨内皮迁移。在这里，我们调查是否磷酸化特定的酪氨酸残基FAK（397，861，和925）已知控制细胞迁移方面的细胞外基质（ECM），也参与跨内皮迁移。表达Phe 397 FAK的Au-565和MDA-MB-231细胞显示出延迟或减少的跨内皮迁移，证明FAK自身磷酸化位点的参与。只有表达Phe 861 FAK的MDA-MB-231细胞表现出延迟的跨内皮迁移。与未处理的癌细胞相比，表达Phe 925 FAK的MDA-MB-231和Au-565细胞均未显示出跨内皮迁移的变化。这些发现表明，修饰的信号传导机制调节癌细胞通过内皮单层的迁移，而不是参与ECM上或通过ECM的细胞迁移。(c)2007年爱思唯尔公司All rights reserved.
Inhibition of focal adhesion kinase (FAK) delays transendothelial migration of breast cancer cells. Here we investigate whether phosphorylation of specific tyrosine residues of FAK (397, 861, and 925) known to control aspects of cell migration on extracellular matrix (ECM), are also involved in transendothelial migration. AU-565 and MDA-MB-231 cells expressing Phe397 FAK show delayed or decreased transendothelial migration, demonstrating the involvement of the FAK autophosphorylation site. Only MDA-MB-231 cells expressing Phe861 FAK exhibit delayed transendothelial migration. Neither MDA-MB-231 nor AU-565 cells expressing Phe925 FAK show a change in transendothelial migration compared to untreated cancer cells. These findings suggest that modified signaling mechanisms regulate cancer cell migration through an endothelial monolayer versus those involved in cell migration on or through ECM. (c) 2007 Elsevier Inc. All rights reserved.