Binding of basic fibroblast growth factor to fibrinogen and fibrin
Binding of basic fibroblast growth factor to fibrinogen and fibrin
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DOI：
10.1074/jbc.273.13.7554
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发表时间：
1998-03-27
影响因子：
4.8
通讯作者：
Francis, CW
中科院分区：
文献类型：
--
作者：
Sahni, A;Odrljin, T;Francis, CW
纤维蛋白酶在组织损伤部位形成，并提供支持血管修复所需的初始内皮细胞反应所需的临时基质。碱性成纤维细胞生长因子（bFGF）也在损伤部位起作用，并刺激类似的血管细胞反应。因此，我们研究了bFGF与纤维蛋白原和纤维蛋白之间是否存在特异性相互作用，这些相互作用可能在协调这些作用中起作用。使用固定在Sepharose珠上的bFGF和可溶性I-125标记的纤维蛋白原以及使用Sepharose固定的纤维蛋白原和可溶性I-125标记的纤维蛋白原进行结合研究。125-bFGF。Scatchard分析表明，固定化bFGF的结合位点有两类，Kd值分别为1.3和260 nM;使用固定的纤维蛋白原，K-d值为0.9和70 nM。通过用凝血酶处理将琼脂糖固定的纤维蛋白原转化为纤维蛋白后，bFGF还表现出与K-d值为0.13和83 nM的两类结合位点的特异性和可饱和结合。还通过凝结bFGF和纤维蛋白原的溶液来研究纤维蛋白原结合，使用该系统证明了两类结合位点，K-d值为0.8和261 nM。bFGF与纤维蛋白原的最大摩尔结合比在2.0和4.0之间，我们得出结论，bFGF与纤维蛋白原和纤维蛋白具有高亲和力的特异性和饱和性结合，这可能对其在组织损伤部位的作用具有影响。
Fibrin is formed at sites of tissue injury and provides the temporary matrix needed to support the initial endothelial cell responses needed for vessel repair. Basic fibroblast growth factor (bFGF) also acts at sites of injury and stimulates similar vascular cell responses, We have, therefore, investigated whether there are specific interactions between bFGF and fibrinogen and fibrin that could play a role in coordinating these actions, Binding studies were performed using bFGF immobilized on Sepharose beads and soluble I-125-labeled fibrinogen and also using Sepharose-immobilized fibrinogen and soluble I-125-bFGF. Both systems demonstrated specific and saturable binding, Scatchard analysis indicated two classes of binding sites for each with K-d values of 1.3 and 260 nM using immobilized bFGF; and K-d values of 0.9 and 70 nM using immobilized fibrinogen, After conversion of Sepharose-immobilized fibrinogen to fibrin by treatment with thrombin, bFGF also demonstrated specific and saturable binding with two classes of binding sites having K-d values of 0.13 and 83 nM, Fibrin binding was also investigated by clotting a solution of bFGF and fibrinogen, and two classes of binding sites were demonstrated using this system with K-d values of 0.8 and 261 nM. The maximum molar binding ratios of bFGF to fibrinogen were between 2.0 and 4.0 with the four binding systems, We conclude that bFGF binds specifically and saturably to fibrinogen and fibrin with high affinity, and this may have implications regarding the localization of its effect at sites of tissue injury.