AFFINITY OF FIBRONECTIN TO COLLAGENS OF DIFFERENT GENETIC TYPES AND TO FIBRINOGEN
AFFINITY OF FIBRONECTIN TO COLLAGENS OF DIFFERENT GENETIC TYPES AND TO FIBRINOGEN
复制标题
DOI：
10.1084/jem.147.6.1584
复制
发表时间：
1978-01-01
影响因子：
15.3
通讯作者：
MILLER, EJ
中科院分区：
文献类型：
--
作者：
ENGVALL, E;RUOSLAHTI, E;MILLER, EJ
纤连蛋白是一种成纤维细胞表面蛋白，通过在与琼脂糖颗粒偶联的明胶上进行亲和层析，从人和鸡血浆以及培养鸡成纤维细胞的提取物中纯化。还从鱼雷鱼的血浆中分离出纤连蛋白样蛋白质。用几种遗传上不同的胶原蛋白研究了纤连蛋白的胶原蛋白结合特性。热变性的 I、II 和 III 型胶原蛋白的结合能力相同，并且比天然胶原蛋白或 A 链和 B 链活性更高。天然 II 型胶原蛋白比其他天然胶原蛋白更活跃。人和鸡纤连蛋白表现出大致相同的特异性模式。鸡纤连蛋白的血浆和成纤维细胞形式显示出相同的特异性。源自该链不同部分的胶原α1(II)链的两种溴化氰肽CB8和CB12在纤连蛋白结合中具有活性。三肽pro-gly-pro和聚脯氨酸的聚合物没有活性。纤连蛋白还与纤维蛋白原和纤维蛋白结合。这种结合与胶原蛋白结合的比较表明，纤维蛋白原抑制纤连蛋白与胶原蛋白的结合，但其活性低于天然胶原蛋白。另外两种纤维蛋白，原弹性蛋白和角蛋白，不结合纤连蛋白。胶原蛋白抑制纤连蛋白与纤维蛋白原的结合，明胶抑制纤连蛋白在寒冷中掺入血凝块。纤连蛋白与胶原蛋白和纤维蛋白原的结合显然取决于纤连蛋白分子中的相同结合位点。细胞表面纤连蛋白可以介导细胞与胶原细胞外基质和伤口中的临时纤维蛋白基质的附着。
Fibronectin, a fibroblast surface protein, was purified from human and chicken plasma and extracts of cultured chicken fibroblasts with affinity chromatography on gelatin coupled to Sepharose particles. A fibronectin-like protein was also isolated from the plasma of Torpedo fish. The collagen binding properties of fibronectin were studied with several genetically distinct collagens. Heat denatured types I, II and III collagens were equal in their binding capacity and more active than the native collagens or A and B chains. Native type II collagen was more active than the other native collagens. Human and chicken fibronectins showed approximately the same pattern of specificity. Identical specificities were shown by the plasma and fibroblast forms of chicken fibronectin. Two cyanogen bromide peptides of the collagen .alpha.1(II) chain, CB8 and CB12, derived from different parts of the chain, were active in fibronectin binding. A polymer of the tripeptide pro-gly-pro, and polyproline were inactive. Fibronectin also binds to fibrinogen and fibrin. Comparison of this binding to collagen binding showed that fibrinogen inhibited binding of fibronectin to collagen, but was less active than native collagen. Two other fibrous proteins, tropoelastin and keratin, did not bind fibronectin. The binding of fibronectin to fibrinogen was inhibited by collagen and incorporation of fibronectin into blood clot in the cold was inhibited by gelatin. The binding of fibronectin to collagen and fibrinogen apparently depends on the same binding site in the fibronectin molecule. Cell surface fibronectin may mediate attachment of cells to the collagenous extracellular matrix and to a temporary fibrin matrix in a wound.