...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The FEBS journal >Differential binding of factor XII and activated factor XII to soluble and immobilized fibronectin - localization of the Hep-1/Fib-1 binding site for activated factor XII
【24h】

Differential binding of factor XII and activated factor XII to soluble and immobilized fibronectin - localization of the Hep-1/Fib-1 binding site for activated factor XII

机译：因子XII和活化因子XII与可溶性和固定化纤连蛋白的差异结合-活化因子XII Hep-1 / Fib-1结合位点的定位

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Fibronectins (FNs) are dimeric glycoproteins that adopt a globular conformation when present in plasma and solution and an extended conformation in the extracellular matrix. Factor XII (FXII) is a zymogen of the proteolytically active FXIIa that plays a role in thrombus stabilization by enhancing clot formation and in inflammation by enhancing bradykinin formation. To investigate whether the extracellular matrix could play a role in these events, we have recently shown that FXIIa, but not FXII, binds to the extracellular matrix (ECM), and suggested that FN may be the target for the binding. Immunofluorescence microscopy has in the present investigation confirmed that FXIIa added to the ECM colocalizes with FN deposited during growth of human umbilical vein endothelial cells. The aim of the present study, therefore, was to further elucidate the interaction between FXIIa and FN by the use of a solid face binding assay. This showed, like the binding to the ECM, that FXIIa, but not FXII, binds in a Znpo-independent manner to immobilized FN. The KD for the binding was 8.5 pl 0.9 n m (n = 3). The binding was specific for the immobilized FN, as the binding could not be inhibited by soluble FN. Furthermore, soluble FN did not bind to immobilized FXIIa. However, soluble FN could bind to FXII, and this binding inhibited the surface-induced autoactivation of FXII and subsequent binding of the generated FXIIa to immobilized FN. The presence of FXII in an anti-FN immunoprecipitate of plasma indicated that some FXII in plasma circulates bound to FN. The binding of FXIIa to FN was inhibited by gelatine and fibrin but not by heparin, indicating that FXIIa binds to immobilized FN through the type I repeat modules. Accordingly, FXIIa was found to bind to immobilized fragments of FN containing the type I repeat modules in the N-terminal domain to which fibrin and gelatine bind.
机译：纤连蛋白（FNs）是二聚体糖蛋白，当存在于血浆和溶液中时呈球形构型，而在细胞外基质中呈扩展构型。因子XII（FXII）是蛋白水解活性FXIIa的酶原，通过增强血凝块形成而在血栓稳定中起作用，通过增强缓激肽形成而在炎症中起作用。为了研究细胞外基质是否可以在这些事件中发挥作用，我们最近发现FXIIa而不是FXII与细胞外基质（ECM）结合，并建议FN可能是结合的目标。免疫荧光显微镜在本研究中已证实，添加至ECM的FXIIa与人脐静脉内皮细胞生长过程中沉积的FN共定位。因此，本研究的目的是通过使用立体人脸结合测定进一步阐明FXIIa和FN之间的相互作用。这表明，与与ECM的结合一样，FXIIa（而不是FXII）以Znpo独立的方式与固定的FN结合。结合的KD为8.5 pl 0.9 n m（n = 3）。该结合对于固定的FN是特异性的，因为该结合不能被可溶性FN抑制。此外，可溶性FN不结合固定的FXIIa。但是，可溶性FN可以与FXII结合，这种结合抑制了FXII的表面诱导的自激活以及随后产生的FXIIa与固定的FN的结合。血浆抗FN免疫沉淀物中FXII的存在表明血浆中的某些FXII循环与FN结合。 FXIIa与FN的结合受到明胶和血纤蛋白的抑制，但不受肝素的抑制，表明FXIIa通过I型重复模块与固定的FN结合。因此，发现FXIIa与固定的FN片段结合，该FN片段包含在N端结构域中与纤维蛋白和明胶结合的I型重复模块。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号