Gillery P, Maquart F X, Borel J P
Exp Cell Res. 1986 Nov;167(1):29-37. doi: 10.1016/0014-4827(86)90201-6.
The role of fibronectin in the contraction of collagen lattices by human skin fibroblasts has been investigated. Incubation of lattice cultures in Dulbecco's modified Eagle's medium supplemented with increasing concentrations of non-dialysed or dialysed fetal calf serum demonstrated that the rate of contraction was dependent on non-dialysable serum components. The suppression of contraction observed when fibronectin was eliminated from serum, either by affinity chromatography on gelatin-agarose columns or by precipitation with anti-fibronectin antibodies, showed that fibronectin is critical for the contraction. When collagen lattices were incubated in a serum-free culture medium totally devoid of fibronectin, no contraction occurred. When fibronectin was added to this medium, their contraction was correlated with the concentration of fibronectin added. The contraction was inhibited by cycloheximide, tunicamycin, and monensin. These results demonstrate that the contraction of collagen lattices by human skin fibroblasts is dependent on fibronectin, and that other protein factors synthesized by the cells or contained in serum are also necessary.
已对纤连蛋白在人皮肤成纤维细胞收缩胶原晶格中的作用进行了研究。在补充了浓度不断增加的未透析或透析胎牛血清的杜尔贝科改良伊格尔培养基中培养晶格培养物,结果表明收缩速率取决于不可透析的血清成分。通过在明胶 - 琼脂糖柱上进行亲和层析或用抗纤连蛋白抗体沉淀从血清中去除纤连蛋白时观察到的收缩抑制,表明纤连蛋白对收缩至关重要。当胶原晶格在完全不含纤连蛋白的无血清培养基中培养时,未发生收缩。当向该培养基中添加纤连蛋白时,它们的收缩与添加的纤连蛋白浓度相关。收缩受到环己酰亚胺、衣霉素和莫能菌素的抑制。这些结果表明,人皮肤成纤维细胞收缩胶原晶格依赖于纤连蛋白,并且细胞合成或血清中所含的其他蛋白质因子也是必需的。