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寻找纤维蛋白原和纤维蛋白之间影响纤维蛋白溶解起始的差异。

Searching for differences between fibrinogen and fibrin that affect the initiation of fibrinolysis.

作者信息

Doolittle Russell F

机构信息

Depts. of Chemistry & Biochemistry and Molecular Biology, University of California., San Diego, La Jolla, CA 92093-0314, USA.

出版信息

Cardiovasc Hematol Agents Med Chem. 2008 Jul;6(3):181-9. doi: 10.2174/187152508784871954.

Abstract

Although in a gross sense fibrin is merely a collection of fibrinogen molecules packed together in bundles, numerous small structural differences can arise as a result of the conversion of the soluble precursor into the gelled product. Some of the consequences are obvious, others more subtle. In one way or another, all these changes are the result of a sequence of events that includes the release of the fibrinopeptides A and B, the formation of protofibrils, the cross-linking of gamma chains, the assembly into mature fibers and the cross-linking of alpha chains. Numerous immunologic differences between fibrinogen and fibrin have been cataloged, and putative sites for fibrin enhancing the activity of plasminogen activators have been identified. Although some conformational changes have been found by X-ray crystallography, the structural changes leading to the exposure of sites thought to bind t-PA and/or plasminogen remain to be demonstrated.

摘要

虽然从总体上讲,纤维蛋白仅仅是成束堆积在一起的纤维蛋白原分子的集合,但由于可溶性前体转化为凝胶状产物,会出现许多细微的结构差异。有些结果是显而易见的,有些则较为微妙。所有这些变化都以某种方式源于一系列事件,包括纤维蛋白肽A和B的释放、原纤维的形成、γ链的交联、组装成成熟纤维以及α链的交联。纤维蛋白原和纤维蛋白之间存在许多免疫学差异,并且已经确定了纤维蛋白增强纤溶酶原激活剂活性的假定位点。尽管通过X射线晶体学发现了一些构象变化,但导致被认为与组织型纤溶酶原激活剂(t-PA)和/或纤溶酶原结合的位点暴露的结构变化仍有待证实。

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