Nair C H, Dhall D P
Vascular and Thrombosis Research Unit, Royal Canberra Hospital (South), Woden, A.C.T., Australia.
Thromb Res. 1991 Feb 1;61(3):315-25. doi: 10.1016/0049-3848(91)90109-a.
Significant differences were found between characteristics of networks developed in plasma and those developed in pure fibrinogen solution. Networks in plasma have thicker fibres, are more permeable and have lower tensile strength. In this investigation determinants of network structure under physiological conditions of clotting have been examined in an attempt to account for the differences in network structure in plasma and fibrinogen solution. Effect of antithrombin III and of physiological concentrations of fibronectin, albumin and gamma-globulin on fibrin network structure was examined using mass-length ratio (microT) from turbidity, bulk permeability of networks (tau) and kinetics of network development. At physiological concentrations effect of ATIII was too pronounced to allow this method to quantify changes in network characteristics. Whilst fibronectin and gamma-globulins increased fibrin fibre thickness and network permeability, albumin caused opposite effects. It is concluded that the final network structure is determined by kinetics of fibrin fibre growth and is highly responsive to the presence of plasma proteins.
在血浆中形成的网络结构与在纯纤维蛋白原溶液中形成的网络结构之间发现了显著差异。血浆中的网络纤维更粗,渗透性更强,拉伸强度更低。在本研究中,对凝血生理条件下网络结构的决定因素进行了研究,以解释血浆和纤维蛋白原溶液中网络结构的差异。使用来自浊度的质量-长度比(microT)、网络的总体渗透率(tau)和网络形成动力学,研究了抗凝血酶III以及生理浓度的纤连蛋白、白蛋白和γ-球蛋白对纤维蛋白网络结构的影响。在生理浓度下,抗凝血酶III的作用过于显著,以至于该方法无法量化网络特征的变化。虽然纤连蛋白和γ-球蛋白增加了纤维蛋白纤维的厚度和网络渗透性,但白蛋白则产生相反的效果。得出的结论是,最终的网络结构由纤维蛋白纤维生长动力学决定,并且对血浆蛋白的存在高度敏感。