Morgenstern E, Korell U, Richter J
Thromb Res. 1984 Mar 15;33(6):617-23. doi: 10.1016/0049-3848(84)90116-6.
The ultrastructure of platelet fibrin contacts (PFC) and the course of the strands was investigated in serial sections of retracted clots with the help of specimen tilting. We found after retraction in a test tube as well as under isometric conditions in the resonance thrombograph, after HARTERT, an uniform type of PFC. The side to side contact between platelet surface and fibrin strands displayed a 15 nm wide space which was bridged of 10 - 30 nm by filamentary structure. In each case the direction of the fibrin strands changed on contact with the platelet surface (bend). These bends recurred if the adhering strands ran over a longer distance on the platelet surface. The bends can be explained by non-directional movement of the platelets or of their pseudopodia. Microfilaments (actomyosin) which run straight in pseudopodia and often also twisted in the platelet body support this assumption. The described mechanism - contact of the thrombin activated platelets with fibrin strands and simultaneous nondirectional movement of the platelets which bind further sections of the adhering strands to their surface - would provide a more satisfactory explanation for the retraction of the clot to 1/10 of its original volume.
借助标本倾斜技术,在回缩凝块的连续切片中研究了血小板纤维蛋白接触点(PFC)的超微结构及纤维蛋白丝的走向。我们发现在试管中回缩后以及在共振血栓图仪等容条件下,按照哈特尔特的方法,会出现一种均匀类型的PFC。血小板表面与纤维蛋白丝之间的侧向接触显示出一个15纳米宽的间隙,由丝状结构以10 - 30纳米的跨度桥接。在每种情况下,纤维蛋白丝与血小板表面接触时方向都会改变(弯曲)。如果附着的纤维蛋白丝在血小板表面延伸较长距离,这些弯曲会反复出现。这些弯曲可以用血小板或其伪足的无定向运动来解释。在伪足中笔直且在血小板体内常呈扭曲状的微丝(肌动球蛋白)支持了这一假设。所描述的机制——凝血酶激活的血小板与纤维蛋白丝接触,同时血小板进行无定向运动,将附着纤维蛋白丝的更多部分结合到其表面——将为凝块回缩至其原始体积的十分之一提供更令人满意的解释。