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首页> 外文期刊>Journal of Investigative Dermatology Symposium Proceedings >The Interaction of Cellular Fibronectin with Collagen During Fibroblast-Mediated Contraction of Collagen Gels
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The Interaction of Cellular Fibronectin with Collagen During Fibroblast-Mediated Contraction of Collagen Gels

机译：成纤维细胞介导的胶原蛋白凝胶收缩过程中细胞纤连蛋白与胶原蛋白的相互作用

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In the first instance highly hydrated collagen gels contract to dense and compact gels when populated by fibroblasts. We previously reported the involvement of fibronectin (FN) in an early process of the collagen gel contraction, utilizing a specific monoclonal antibody dubbed A3A5 (MoAb-A3A5) that inhibits the gel contraction. This study was performed to further characterize the role of the epitope for MoAb-A3A5 in the interaction between fibroblasts and collagen fibrils. Although both cellular FN (cFN) and plasma FN (pFN) were reactive with MoAb-A3A5, the FN that actually participates in a process of the gel contraction was shown to be cFN. The gel contraction was significantly accelerated when fibroblasts were pretreated with excess amounts of cFN and was significantly inhibited when the collagen molecules were pretreated with excess cFN. Such effects of the pretreatments were not observed for pFN. The involvement of cFN, but not pFN, in the interaction of fibroblasts with collagen fibrils was additionally shown by the similar inhibitory action of cFN, but not pFN, on the spreading and elongation of fibroblasts on collagen fibrils. The epitope for MoAb-A3A5 was strongly suggested to be a new functional domain responsible for the interactions between fibroblasts and native collagen molecules. This was not the case for those with denatured one, because fibroblasts on collagen fibrils were not stainable with MoAb-A3A5, whereas the interactions on gelatin were stainable. The lack of the reactivity of fibroblasts on collagen fibrils toward MoAb-A3A5 was not a result of the absence of FN on the cell membrane, but seemed to be a steric hindrance to the access of the antibody.
机译：首先，当由成纤维细胞组成时，高度水合的胶原蛋白凝胶收缩成致密和致密的凝胶。我们先前报道了纤连蛋白（FN）参与胶原凝胶收缩的早期过程，它利用一种被称为A3A5（MoAb-A3A5）的特异性单克隆抗体来抑制凝胶收缩。进行该研究以进一步表征MoAb-A3A5的表位在成纤维细胞和胶原原纤维之间的相互作用中的作用。尽管细胞FN（cFN）和血浆FN（pFN）均与MoAb-A3A5发生反应，但实际参与凝胶收缩过程的FN显示为cFN。当用过量的cFN预处理成纤维细胞时，凝胶收缩明显加速，而当用过量的cFN预处理胶原蛋白分子时，凝胶收缩被明显抑制。对于pFN，未观察到预处理的这种效果。通过cFN而不是pFN对成纤维细胞在胶原纤维上的扩散和伸长的类似抑制作用，进一步显示了cFN而不是pFN参与成纤维细胞与胶原纤维的相互作用。强烈建议MoAb-A3A5的表位是负责成纤维细胞和天然胶原分子之间相互作用的新功能域。对于那些变性的人则不是这种情况，因为胶原原纤维上的成纤维细胞不可被MoAb-A3A5染色，而明胶上的相互作用可被染色。胶原纤维上的成纤维细胞缺乏针对MoAb-A3A5的反应性，并不是由于细胞膜上不存在FN的结果，而是对抗体进入的空间障碍。

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