Laboratory of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
FEBS Lett. 2010 Aug 4;584(15):3381-5. doi: 10.1016/j.febslet.2010.06.032. Epub 2010 Jun 26.
Integrins and syndecans mediate cell adhesion to extracellular matrix and their synergistic cooperation is implicated in cell adhesion processes. We previously identified two active peptides, AG73 and EF1, from the laminin alpha1 chain LG4 module, that promote cell attachment through syndecan- and alpha2beta1 integrin-binding, respectively. Here, we examined time-dependent cell attachment on the mixed peptides AG73/EF1. The AG73/EF1 promoted stronger and more rapid cell attachment, spreading, FAK phosphorylation that reached a maximum at 20 min than that on AG73 (40 min) or EF1 (90 min) supplied singly. Thus, the syndecan- and alpha2beta1 integrin-binding peptides synergistically affect cells and accelerate cell adhesion.
整合素和 syndecans 介导细胞与细胞外基质的黏附,它们的协同合作参与了细胞黏附过程。我们之前从层粘连蛋白 α1 链 LG4 模块中鉴定出两个活性肽 AG73 和 EF1,它们分别通过与 syndecan 和 α2β1 整合素结合来促进细胞附着。在这里,我们研究了混合肽 AG73/EF1 上的时间依赖性细胞附着。与单独提供的 AG73(40 分钟)或 EF1(90 分钟)相比,AG73/EF1 促进更强和更快的细胞附着、伸展、FAK 磷酸化,在 20 分钟时达到最大值。因此,syndecan 和 α2β1 整合素结合肽协同作用于细胞并加速细胞黏附。