Holahan J R, White G C
Blood. 1981 Jan;57(1):174-81.
Studies in several laboratories have suggested that platelets from patients with Glanzmann's thrombasthenia are deficient in two major membrane glycoproteins and that this membrane defect is uniform from patient to patient. We have used an improved electrophoretic technique to study further the surface composition of normal and thrombasthenic platelets. Platelets from three unrelated thrombasthenic patients were labeled by either lactoperoxidase-catalyzed iodination or the neuraminidase-galactose oxidase-[3H]NaBH4 technique and the labeled proteins were separated by two dimensional isoelectric focusing SDS polyacrylamide gel electrophoresis. With both techniques, the major radiolabeled proteins were clearly separated from each other and were present as a horizontal collection of discrete spots that suggest charge heterogeneity. Most of the labeled proteins had an acidic isoelectric point. Compared to normal platelets, platelets from patients with Glanzmann's disease contained no electrophoretically identifiable fibrinogen. In two patients with thrombasthenia, there was total absence of surface glycoproteins GPIIb and GPIII, while a third patient with thrombasthenia, who was clinically indistinguishable from the previous two patients, had decreased, but detectable, amounts of GPIIb and GPIII. These studies suggest that there are at least two phenotypic patterns of membrane abnormalities in Glanzmann's thrombasthenia involving GPIIb and GPIII and may indicate genetic heterogeneity in this disease.
多个实验室的研究表明，患有Glanzmann血小板无力症的患者的血小板缺乏两种主要的膜糖蛋白，并且这种膜缺陷在患者之间是一致的。我们使用了一种改进的电泳技术来进一步研究正常和血小板无力症血小板的表面组成。来自三名无亲缘关系的血小板无力症患者的血小板通过乳过氧化物酶催化碘化或神经氨酸酶 - 半乳糖氧化酶 - [3H]硼氢化钠技术进行标记，然后通过二维等电聚焦SDS聚丙烯酰胺凝胶电泳分离标记的蛋白质。使用这两种技术，主要的放射性标记蛋白质都能清晰地彼此分离，并呈现为离散斑点的水平集合，这表明电荷存在异质性。大多数标记的蛋白质具有酸性等电点。与正常血小板相比，患有Glanzmann病的患者的血小板中没有电泳可识别的纤维蛋白原。在两名血小板无力症患者中，表面糖蛋白GPIIb和GPIII完全缺失，而第三名血小板无力症患者在临床上与前两名患者无法区分，但其GPIIb和GPIII的含量有所减少但仍可检测到。这些研究表明，Glanzmann血小板无力症中至少存在两种涉及GPIIb和GPIII的膜异常表型模式，这可能表明该疾病存在遗传异质性。
