Matrix-driven translocation: dependence on interaction of amino-terminal domain of fibronectin with heparin-like surface components of cells or particles.

Matrix-driven translocation: dependence on interaction of amino-terminal domain of fibronectin with heparin-like surface components of cells or particles.
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基质驱动的易位:依赖于纤连蛋白氨基末端结构域与细胞或颗粒的肝素样表面成分的相互作用。

DOI:
10.1073/pnas.84.14.4791
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发表时间:
1987
影响因子:
11.1
通讯作者:
Akiyama,SK
Akiyama,SK
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Newman,SA;Frenz,DA;Hasegawa,E;Akiyama,SK

文献摘要

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在基质驱动的易位过程中,某些类型的细胞或聚苯乙烯乳胶珠在胶原基质的组成不同的区域之间转运。在适当的条件下,这种易位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位于纤连蛋白分子的氨基末端的第一个31 kDa内的位点。使用定义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,该位点被确立为促进基质驱动的易位的必要和充分条件。使用肝素、硫酸乙酰肝素和其他硫酸多糖的竞争实验表明,该纤连蛋白位点与肝素样细胞或颗粒表面组分相互作用,促进基质驱动的易位。用肝素酶处理细胞使它们对移位效应无反应。针对纤连蛋白的氨基末端结构域的抗体完全抑制基质驱动的易位而不干扰肝素结合,这表明纤连蛋白中的结合后构象变化可能是促进该效果所必需的。
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.