Tsai Jones, Kam Lance
Biophys J. 2009 Mar 18;96(6):L39-41. doi: 10.1016/j.bpj.2009.01.005.
Integrin-cadherin cross talk is an important aspect of cell function. We explored this signaling using substrates micropatterned with islands of fibronectin surrounded by E-cadherin, capturing the segregation of these signals in normal tissue. While MDCK cells were able to concurrently form adhesive structures with these two proteins, engagement of fibronectin by MCF-7 cells, an adenocarcinoma cell line, inhibited response of these cells to E-cadherin. We further demonstrated that this inhibition is rigidity dependent; on soft elastomer substrates with Young's modulus in the range of tens of kiloPascals, MCF-7 cells were able to engage both integrin and cadherin ligands.
整合素-钙黏蛋白相互作用是细胞功能的一个重要方面。我们使用了由纤连蛋白岛微图案化且周围环绕着E-钙黏蛋白的底物来探究这种信号传导,以此捕捉正常组织中这些信号的分离情况。虽然MDCK细胞能够同时与这两种蛋白质形成黏附结构,但腺癌细胞系MCF-7细胞与纤连蛋白的结合抑制了这些细胞对E-钙黏蛋白的反应。我们进一步证明这种抑制作用取决于硬度;在杨氏模量处于几十千帕范围内的软弹性体底物上,MCF-7细胞能够同时结合整合素配体和钙黏蛋白配体。