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血小板膜拓扑结构:血小板反应蛋白和纤维蛋白原与糖蛋白IIb-IIIa复合物的共定位

Platelet membrane topography: colocalization of thrombospondin and fibrinogen with the glycoprotein IIb-IIIa complex.

作者信息

Asch A S, Leung L L, Polley M J, Nachman R L

出版信息

Blood. 1985 Oct;66(4):926-34.

PMID:2994782
Abstract

The distribution of platelet thrombospondin (TSP), fibrinogen, and glycoproteins IIb-IIIa (GPIIb-IIIa) and GPIb were studied in resting and activated human platelets using frozen thin-section immunoelectron microscopy. In resting platelets, TSP and fibrinogen were found within alpha granules and not on the platelet surface. In unstimulated platelets, GPIIb-IIIa and GPIb were distributed diffusely over the platelet membrane as well as within the body of the platelets. Upon thrombin or A23187 stimulation, TSP, fibrinogen, and GPIIb-IIIa colocalized on the platelet membrane and the canalicular system as well as on pseudopodia and between adherent platelets. GPIb distribution was unchanged by platelet activation. The findings support the hypothesis that a macromolecular complex of TSP-fibrinogen and GPIIb-IIIa forms on the activated platelet membrane.

摘要

利用冷冻超薄切片免疫电子显微镜技术,研究了静息和活化的人血小板中血小板凝血酶敏感蛋白(TSP)、纤维蛋白原、糖蛋白IIb-IIIa(GPIIb-IIIa)和糖蛋白Ib(GPIb)的分布情况。在静息血小板中,TSP和纤维蛋白原存在于α颗粒内,而不在血小板表面。在未受刺激的血小板中,GPIIb-IIIa和GPIb分散分布于血小板膜以及血小板内部。经凝血酶或A23187刺激后,TSP、纤维蛋白原和GPIIb-IIIa共定位于血小板膜、小管系统、伪足以及黏附血小板之间。血小板活化后,GPIb的分布未发生改变。这些发现支持了以下假说:在活化的血小板膜上形成了由TSP-纤维蛋白原和GPIIb-IIIa组成的大分子复合物。

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