Long M M, King V J, Prasad K U, Urry D W
Laboratory of Molecular Biophysics, University of Alabama at Birmingham 35294.
Biochim Biophys Acta. 1988 Mar 11;968(3):300-11. doi: 10.1016/0167-4889(88)90021-3.
Bovine ligamentum fibroblasts, which produce elastin, migrate towards a positive chemical gradient of human platelet-derived growth factor and of the tropoelastin repeat hexapeptide Val-Gly-Val-Ala-Pro-Gly, as previously shown. They are also responsive to two permutations of a nonapeptide that repeats in tropoelastin, i.e., Ala-Gly-Val-Pro-Gly-Phe-Gly-Val-Gly and Gly-Phe-Gly-Val-Gly-Ala-Gly-Val-Pro. Concentration curves and checkerboard assays prove that the nonapeptides are chemoattractants. The component pentapeptide, Gly-Phe-Gly-Val-Gly, is chemotactic, while the component tetrapeptide Ala-Gly-Val-Pro is not. The hexapeptide competitively suppresses the nonapeptide chemotaxis suggesting the involvement of a common cell receptor. The results support the concept that elastin has multiple cell recognition sites as measured by the chemotactic response and that among the hydrophobic repeating sequences of elastin chemotacticity is selectively and multiply localized.
如前所示，产生弹性蛋白的牛韧带成纤维细胞会朝着人血小板衍生生长因子以及原弹性蛋白重复六肽Val-Gly-Val-Ala-Pro-Gly的正化学梯度迁移。它们也对原弹性蛋白中重复的九肽的两种排列有反应，即Ala-Gly-Val-Pro-Gly-Phe-Gly-Val-Gly和Gly-Phe-Gly-Val-Gly-Ala-Gly-Val-Pro。浓度曲线和棋盘分析证明这些九肽是化学引诱剂。组成成分五肽Gly-Phe-Gly-Val-Gly具有趋化性，而组成成分四肽Ala-Gly-Val-Pro则没有。该六肽竞争性地抑制九肽的趋化作用，提示存在共同的细胞受体。这些结果支持了这样的概念，即通过趋化反应测定，弹性蛋白具有多个细胞识别位点，并且在弹性蛋白的疏水重复序列中，趋化性是选择性且多重定位的。
