Seppä H E, Yamada K M, Seppä S T, Silver M H, Kleinman H K, Schiffmann E
Cell Biol Int Rep. 1981 Aug;5(8):813-9. doi: 10.1016/0309-1651(81)90253-8.
The fibroblast chemoattractant property of fibronectin is retained in the proteolytically produced 160 kilodalton peptide that contains the heparin binding and cell binding domains of the molecule, while the 40 kilodalton collagen binding peptide is inactive. Further degradation of the 160 kilodalton peptide leads to destruction of chemoattractant activity. An analysis of the migration of fibroblasts in varied gradients of the 160 K peptide shows that the effect is chemotactic, i.e. directed migration of cells towards a higher concentration of the peptide.
纤连蛋白的成纤维细胞趋化活性在经蛋白水解产生的160千道尔顿肽中得以保留，该肽包含分子的肝素结合域和细胞结合域，而40千道尔顿的胶原结合肽则无活性。160千道尔顿肽的进一步降解会导致趋化活性的破坏。对成纤维细胞在不同浓度梯度的160K肽中的迁移情况分析表明，其作用具有趋化性，即细胞朝着更高浓度的肽定向迁移。
