Feagler J R, Tillack T W, Chaplin D D, Majerus P W
J Cell Biol. 1974 Mar;60(3):541-53. doi: 10.1083/jcb.60.3.541.
We have previously demonstrated that lentil phytohemagglutinin (lentil-PHA) binds to human platelet membranes without causing either aggregation or the release reaction. When platelets are treated with thrombin, there is an increase in lentil-PHA binding suggesting the appearance of new receptor sites on the cell surface. We prepared a lentil-PHA-ferritin conjugate using affinity chromatography which was used to saturate cell surface receptor sites. Studies using this conjugate suggest that thrombin causes a complex change in the platelet surface involving a decrease in the number of lentil-PHA receptor sites on the external platelet surface with a marked increase in sites within the center of the canalicular system. These increased sites may result from fusion of granule membranes with the canalicular membranes during the secretion process. There is no obvious relationship between lentil-PHA receptor sites and intramembranous particles.
我们之前已经证明,小扁豆植物血凝素(扁豆-PHA)可与人血小板膜结合,而不会引起聚集或释放反应。当用凝血酶处理血小板时,扁豆-PHA结合增加,表明细胞表面出现了新的受体位点。我们使用亲和色谱法制备了扁豆-PHA-铁蛋白缀合物,用于饱和细胞表面受体位点。使用这种缀合物的研究表明,凝血酶会导致血小板表面发生复杂变化,包括外部血小板表面上扁豆-PHA受体位点数量减少,而在管状系统中心的位点显著增加。这些增加的位点可能是由于分泌过程中颗粒膜与管状膜融合所致。扁豆-PHA受体位点与膜内颗粒之间没有明显关系。