Fibrinogen and fibrin: scaffold proteins in hemostasis
Fibrinogen and fibrin: scaffold proteins in hemostasis
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DOI：
10.1097/moh.0b013e3280dce58c
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发表时间：
2007-05-01
影响因子：
3.2
通讯作者：
Lord, Susan T.
中科院分区：
文献类型：
--
作者：
Lord, Susan T.
纤维蛋白原升高是心血管疾病的危险因素。最近的研究为这种风险提供了理论依据，因为异常的纤维蛋白凝块结构、强度和稳定性与冠状动脉疾病相关。这篇综述描述了体外实验，其目的是确定体内控制凝块结构和功能的分子机制。最近的研究发现，生化和结构数据继续定义单个单位之间的相互作用，组装成一个纤维蛋白凝块。特别是，“A: A”相互作用在纤维形成的第一步中起主导作用，而类似的“B: U”相互作用则起次要作用。研究表明，BP的n端、A α的c端和剪接变体γ′可调节纤维蛋白凝块结构。纤维蛋白原和纤维蛋白的机械性能测量表明，纤维蛋白纤维是自然界中最坚固的纤维之一。研究发现纤维蛋白原结合蛋白影响凝块结构和功能。这些发现明确了控制纤维蛋白凝块结构、强度和稳定性的机制。这些基本信息为临床研究提供了方向，以检查病理性血栓形成中的凝块特性和药物研究，以制定预防或控制心血管疾病的治疗干预措施。这些研究还建立了检测单个键、分子和纤维的新技术。
Purpose of review Elevated fibrinogen is a cardiovascular risk factor. Recent work provides a rationale for this risk, as abnormal fibrin clot structure, strength and stability correlates with coronary artery disease. This review describes in-vitro experiments whose intent is to define the molecular mechanisms that control clot architecture and function in vivo.Recent findings Biochemical and structural data continue to define the interactions between monomer units that assemble into a fibrin clot. In particular, 'A: a' interactions dominate the first step in fiber formation, while the analogous 'B: U interactions have a minor role. Studies show the N-terminus of BP, the C-terminus of A alpha, and the splice variant gamma' modulate fibrin clot structure. Measurement of the mechanical properties of fibrinogen and fibrin show fibrin fibers are among the strongest in nature. Studies have identified fibrinogen-binding proteins that influence clot structure and function.Summary These findings defined mechanisms that control fibrin clot structure, strength and stability. This basic information provides direction for clinical studies to examine clot properties in pathologic thrombosis and pharmaceutical studies to develop therapeutic interventions to prevent or control cardiovascular disease. These studies also establish novel techniques to examine individual bonds, molecules and fibers.