Niewiarowski S, Regoeczi E, Stewart G J, Senyl A F, Mustard J F
J Clin Invest. 1972 Mar;51(3):685-99. doi: 10.1172/JCI106857.
Interaction of washed pig, rabbit, or human platelets with fibrinogen was studied during its transition to fibrin using photometric, isotopic, and electron microscopic techniques. Untreated fibrinogen and fully polymerized fibrin had no detectable effect on platelets. Fibrinogen, incubated with low concentrations of reptilase or thrombin, formed intermediate products which readily became associated with platelets and caused their aggregation. Neutralization of the thrombin did not prevent this interaction. In the absence of fibrinogen, reptilase did not affect platelets. The interaction of polymerizing fibrin with platelets was accompanied by small losses of platelet constituents (serotonin, adenine nucleotides, platelet factor 4, and lactic dehydrogenase). This loss did not appear to be the result of the platelet release reaction. Inhibitors of the release reaction or of adenosine diphosphate (ADP)-induced aggregation did not prevent the interaction of platelets with polymerizing fibrin. Apyrase or prostaglandin E(1) (PGE(1)) reduced the extent of platelet aggregation by polymerizing fibrin, but the amount of protein associated with platelets was slightly increased. The interaction of polymerizing fibrin with platelets was completely inhibited by ethylenediaminetetraacetate (EDTA) or ethylene glycol bis (beta-aminoethyl ether) N, N,N',N'-tetraacetic acid (EGTA).Fibers formed in solutions of polymerizing fibrin were larger in the presence than in the absence of washed platelets, suggesting that platelets affect fibrin polymerization. The adherence of platelets to polymerizing fibrin may be responsible for the establishment of links between platelets and fibrin in hemostatic plugs and thrombi.
利用光度测定法、同位素法和电子显微镜技术，研究了洗涤过的猪、兔或人血小板在纤维蛋白原向纤维蛋白转变过程中与纤维蛋白原的相互作用。未经处理的纤维蛋白原和完全聚合的纤维蛋白对血小板没有可检测到的影响。与低浓度的蛇毒凝血酶或凝血酶一起孵育的纤维蛋白原形成了中间产物，这些中间产物很容易与血小板结合并导致血小板聚集。凝血酶的中和并不能阻止这种相互作用。在没有纤维蛋白原的情况下，蛇毒凝血酶不会影响血小板。正在聚合的纤维蛋白与血小板的相互作用伴随着血小板成分（5-羟色胺、腺嘌呤核苷酸、血小板因子4和乳酸脱氢酶）的少量损失。这种损失似乎不是血小板释放反应的结果。释放反应抑制剂或二磷酸腺苷（ADP）诱导的聚集抑制剂并不能阻止血小板与正在聚合的纤维蛋白的相互作用。腺苷三磷酸双磷酸酶或前列腺素E(1)（PGE(1)）通过使纤维蛋白聚合减少了血小板聚集的程度，但与血小板结合的蛋白量略有增加。正在聚合的纤维蛋白与血小板的相互作用被乙二胺四乙酸（EDTA）或乙二醇双（β-氨基乙醚）N，N，N'，N'-四乙酸（EGTA）完全抑制。在有洗涤过的血小板存在的情况下，在正在聚合的纤维蛋白溶液中形成的纤维比没有血小板时更大，这表明血小板会影响纤维蛋白的聚合。血小板与正在聚合的纤维蛋白的黏附可能是止血栓和血栓中血小板与纤维蛋白之间建立联系的原因。
