Liang O D, Rosenblatt S, Chhatwal G S, Preissner K T
GBF-National Research Center for Biotechnology/Technical University Braunschweig, Germany.
FEBS Lett. 1997 Apr 28;407(2):169-72. doi: 10.1016/s0014-5793(97)00330-x.
Vitronectin is a multifunctional serum protein which provides a unique regulatory link between cell adhesion, humoral defense mechanism and the hemostatic system, and the heparin-binding properties of vitronectin are thought to have participated in various functional aspects. In addition to the carboxy-terminal glycosaminoglycan-binding motif, we report on two novel heparin-binding domains which were identified using phage display technique. One heparin-binding domain is located between amino acids Asp82 and Cys137 at the end of the connector region, while the other is in the second hemopexin-type repeat, between amino acids Lys175 and Asp219 of the vitronectin molecule. Our findings may shed new light to the activities of vitronectin and its binding to cells, which could not be explained solely on the basis of the known heparin-binding domain.
玻连蛋白是一种多功能血清蛋白，它在细胞黏附、体液防御机制和止血系统之间提供了独特的调节联系，并且玻连蛋白的肝素结合特性被认为参与了多个功能方面。除了羧基末端糖胺聚糖结合基序外，我们还报道了利用噬菌体展示技术鉴定出的两个新的肝素结合结构域。一个肝素结合结构域位于连接区末端的天冬氨酸82和半胱氨酸137之间的氨基酸残基处，而另一个位于玻连蛋白分子第二个血红素结合蛋白样重复序列中，在赖氨酸175和天冬氨酸219之间。我们的发现可能为玻连蛋白的活性及其与细胞的结合提供新的线索，而这仅基于已知的肝素结合结构域无法解释。
