Decorin binds fibrinogen in a Zn2+-dependent interaction
Decorin binds fibrinogen in a Zn2+-dependent interaction
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DOI：
10.1074/jbc.m300171200
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发表时间：
2003-04-18
影响因子：
4.8
通讯作者：
Höök, M
中科院分区：
文献类型：
--
作者：
Dugan, TA;Yang, VWC;Höök, M
我们先前已经表明，核心蛋白聚糖（胞外基质蛋白聚糖/糖蛋白的富含亮氨酸的小蛋白聚糖家族的成员）在生理Zn 2+浓度下是Zn 2+金属蛋白（Yang，V. W-C.，LaBrenz，S. R.，罗森伯格湖C.的方法，McQuillan，D.，Hook，M.（1999）J.Biol.Chem.274，12454 -12460）。我们现在报告，核心蛋白聚糖结合纤维蛋白原在Zn 2+的存在下。纤维蛋白原结合位点位于核心蛋白聚糖核心蛋白的N-末端结构域，代表该结构域的45个氨基酸的肽与纤维蛋白原D片段结合，表观KD为1.7 × 10 - 6 m，由荧光偏振数据确定。此外，我们表明，锌+促进核心蛋白聚糖的自缔合。核心蛋白的N-末端结构域也介导这种活性。固相结合试验和凝胶过滤色谱法的结果表明，N-末端结构域的核心蛋白聚糖，当存在于低微摩尔浓度，形成一个低聚体中的Zn 2+依赖的方式。因此，Zn 2+似乎在核心蛋白聚糖的相互作用和生物学功能中起着关键作用。
We have previously shown that decorin, a member of the small leucine-rich proteoglycan family of extracellular matrix proteoglycans/glycoproteins is a Zn2+ metalloprotein at physiological Zn2+ concentrations (Yang, V. W-C., LaBrenz, S. R., Rosenberg, L. C., McQuillan, D., and Hook, M. (1999) J. Biol. Chem. 274,12454-12460). We now report that the decorin proteoglycan binds fibrinogen in the presence of Zn2+. The fibrinogen-binding site is located in the N-terminal domain of the decorin core protein and a 45-amino acid peptide representing this domain binds to the fibrinogen D fragment with an apparent K-D of 1.7 x 10(-6) m, as determined from fluorescence polarization data. Furthermore, we show that Zn2+ promotes the self-association of decorin. The N-terminal domain of the core protein also mediates this activity. The results of solid-phase binding assays and gel filtration chromatography suggest that the N-terminal domain of decorin, when present at low micromolar concentrations, forms an oligomer in a Zn2+-dependent manner. Thus, Zn2+ appears to play a pivotal role in the interactions and biological function of decorin.