INTERACTION OF HEPARIN WITH FIBRONECTIN AND ISOLATED FIBRONECTIN DOMAINS
INTERACTION OF HEPARIN WITH FIBRONECTIN AND ISOLATED FIBRONECTIN DOMAINS
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DOI：
10.1042/bj2720605
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发表时间：
1990-12-15
影响因子：
4.1
通讯作者：
ATHA, DH
中科院分区：
文献类型：
--
作者：
INGHAM, KC;BREW, SA;ATHA, DH
利用荧光极化、凝胶排斥层析和亲和层析表征了不同大小的肝素与人血浆纤维连接蛋白（Fn）及其分离结构域的相互作用。液相kDa Hep-2结构域分别位于A链和B链的c端附近。在这方面，来自重链的30 kDa Hep-2A结构域与40 kDa Hep-2B结构域难以区分；后者中额外的III型同源单位的存在对结合没有影响。有证据表明，每个Hep-2结构域有两个肝素结合位点。n端Hep-1结构域在液相中反应弱，尽管它与固定化肝素结合强烈。Fn和Hep-2片段在与不同大小的荧光胺标记的肝素反应时几乎没有区别。然而，小于十四聚糖（14-mer）结合Fn的低聚糖具有5-10倍的亲和力。这些结果表明，Fn的Hep-2结构域能够识别广泛的低聚糖，这些低聚糖可能在电荷的数量和空间分布方面变化很大。
Fluorescence polarization, gel exclusion chromatography and affinity chromatography were used to characterize the interaction of heparins of different size with human plasma fibronectin (Fn) and several of its isolated domains. The fluidphase kDa Hep-2 domains located near the C-terminal ends of the A and B chains respectively. The 30 kDa Hep-2A domain from the heavy chain was indistinguishable from the 40 kDa Hep-2B domain in this respect; the presence of an additional type III homology unit in the latter had no effect on the binding. Evidence was provided that each Hep-2 domain has two binding sites for heparin. The N-terminal Hep-1 domain reacted weakly in fluid phase even though it binds strongly to immobilized heparin. Fn and Hep-2 fragments were rather undiscriminating in their reaction with fluoresceinamine-labelled heparins of different sizes. However, oligosaccharides smaller than the tetradecasaccharide (14-mer) bound Fn with a 5-10-fold lower affinity. These results suggest that the Hep-2 domains of Fn are able to recognize a broad spectrum of oligosaccharides that presumably vary significantly with respect to the amount and spatial distribution of charge.