Bennett J S, Vilaire G, Burch J W
J Clin Invest. 1981 Oct;68(4):981-7. doi: 10.1172/jci110352.
Exposure of fibrinogen receptors by a variety of agonists is a prerequisite for platelet aggregation. Because the synthesis of prostaglandins and thromboxane A2 also occurs during platelet aggregation we wondered whether these agents participate in the exposure of platelet fibrinogen receptors. Therefore, we measured the binding of human 125I-fibrinogen to gel-filtered normal human platelets after prostaglandin and thromboxane synthesis had been inhibited by aspirin or indomethacin. The fibrinogen binding assay was performed at 37 degrees C but without stirring to prevent the formation of platelet aggregates. Platelet secretion, measured with [14C]serotonin, did not occur during the procedure. Aspirin or indomethacin inhibited fibrinogen binding stimulated by 10 microM epinephrine by 53%, and inhibited fibrinogen binding stimulated by 1-2 microM ADP by 37.1%. However, ADP at concentrations greater than 2 microM returned fibrinogen binding toward control values. Scatchard analysis demonstrated that aspirin decreased the number but not the affinity of the exposed fibrinogen receptors. To determine whether prostaglandins are capable of directly exposing fibrinogen receptors, prostaglandin H2 was used to stimulate platelets in the fibrinogen binding assay. Prostaglandin H2 exposed approximately 54,000 fibrinogen receptors/platelet and corrected the deficit in receptor exposure induced by aspirin. These studies demonstrate that platelet prostaglandins or thromboxane A2 can play a direct role in the exposure of platelet fibrinogen receptors. In addition, they suggest that the synthesis of prostaglandins and thromboxane A2 by stimulated platelets may be all that is required for optimal secondary platelet aggregation.
多种激动剂使纤维蛋白原受体暴露是血小板聚集的前提条件。由于血小板聚集过程中也会发生前列腺素和血栓素A2的合成,我们想知道这些物质是否参与血小板纤维蛋白原受体的暴露。因此,我们在用阿司匹林或消炎痛抑制前列腺素和血栓素合成后,测定了人125I-纤维蛋白原与凝胶过滤的正常人血小板的结合。纤维蛋白原结合试验在37℃下进行,但不搅拌以防止血小板聚集体形成。在该过程中未发生用[14C]血清素测定的血小板分泌。阿司匹林或消炎痛可抑制10μM肾上腺素刺激的纤维蛋白原结合53%,抑制1-2μM ADP刺激的纤维蛋白原结合37.1%。然而,浓度大于2μM的ADP可使纤维蛋白原结合恢复至对照值。Scatchard分析表明,阿司匹林减少了暴露的纤维蛋白原受体的数量,但不影响其亲和力。为了确定前列腺素是否能够直接使纤维蛋白原受体暴露,在纤维蛋白原结合试验中用前列腺素H2刺激血小板。前列腺素H2使每个血小板暴露约54,000个纤维蛋白原受体,并纠正了阿司匹林诱导的受体暴露缺陷。这些研究表明,血小板前列腺素或血栓素A2可在血小板纤维蛋白原受体暴露中起直接作用。此外,它们提示,受刺激的血小板合成前列腺素和血栓素A2可能是最佳二次血小板聚集所必需的全部条件。