Newman S A, Frenz D A, Hasegawa E, Akiyama S K
Proc Natl Acad Sci U S A. 1987 Jul;84(14):4791-5. doi: 10.1073/pnas.84.14.4791.
During the process of matrix-driven translocation, certain types of cells or polystyrene latex beads are transported between compositionally different regions of a collagen matrix. Under appropriate conditions this translocation depends on an interaction between the cell or particle surface and fibronectin. We now show that this interaction takes place at a site located within the first 31 kDa of the amino-terminal end of the fibronectin molecule. Using defined fibronectin fragments and monoclonal antibodies directed against specific fibronectin domains, this site is established as both necessary and sufficient for the promotion of matrix-driven translocation. Competition experiments using heparin, heparan sulfate, and other sulfated polysaccharides show that this fibronectin site interacts with heparin-like cell or particle surface components in promoting matrix-driven translocation. Treatment of cells with heparinase renders them unresponsive to the translocational effect. An antibody directed against the amino-terminal domain of fibronectin completely inhibits matrix-driven translocation without interfering with heparin binding, suggesting that a post-binding conformational change in fibronectin may be required for promotion of the effect.
在基质驱动的转运过程中，某些类型的细胞或聚苯乙烯乳胶珠在胶原蛋白基质成分不同的区域之间运输。在适当条件下，这种转运取决于细胞或颗粒表面与纤连蛋白之间的相互作用。我们现在表明，这种相互作用发生在纤连蛋白分子氨基末端前31 kDa内的一个位点。使用特定的纤连蛋白片段和针对特定纤连蛋白结构域的单克隆抗体，该位点被确定为促进基质驱动转运既必要又充分的条件。使用肝素、硫酸乙酰肝素和其他硫酸化多糖的竞争实验表明，在促进基质驱动转运过程中，该纤连蛋白位点与类似肝素的细胞或颗粒表面成分相互作用。用肝素酶处理细胞会使其对转运效应无反应。一种针对纤连蛋白氨基末端结构域的抗体完全抑制基质驱动的转运，而不干扰肝素结合，这表明纤连蛋白可能需要结合后构象变化来促进该效应。
