Fox J E
J Clin Invest. 1985 Oct;76(4):1673-83. doi: 10.1172/JCI112153.
Experiments were performed to determine whether platelets contain a membrane skeleton. Platelets were labeled by a sodium periodate/sodium [3H]borohydride method and lysed with Triton X-100. Much of the filamentous actin could be sedimented at low g forces (15,600 g, 4 min), but some of the actin filaments required high-speed centrifugation for their sedimentation (100,000 g, 3 h). The latter filaments differed from those in the low-speed pellet in that they could not be depolymerized by Ca2+ and could not be sedimented at low g forces even from Triton X-100 lysates of platelets that had been activated with thrombin. Actin-binding protein sedimented with both types of filaments, but 3H-labeled membrane glycoproteins were recovered mainly with the high-speed filaments. The primary 3H-labeled glycoprotein recovered with this "membrane skeleton" was glycoprotein (GP) Ib. Approximately 70% of the platelet GP Ib was present in this skeleton. Several other minor glycoproteins, including greater than 50% of the GP Ia and small amounts of three unidentified glycoproteins of Mr greater than 200,000, were also recovered with the membrane skeleton. The Triton X-100 insolubility of GP Ib, GP Ia, a minor membrane glycoprotein of 250,000 Mr, and actin-binding protein resulted from their association with actin filaments as they were rendered Triton X-100-soluble when actin filaments were depolymerized with deoxyribonuclease I and co-isolated with actin filaments on sucrose gradients. When isolated platelet plasma membranes were extracted with Triton X-100, actin, actin-binding protein, and GP Ib were recovered as the Triton X-100 residue. These studies show that unstimulated platelets contain a membrane skeleton composed of actin filaments and actin-binding protein that is distinct from the rest of the cytoskeleton and is attached to GP Ib, GP Ia, and a minor glycoprotein of 250,000 Mr on the plasma membrane.
进行实验以确定血小板是否含有膜骨架。血小板用高碘酸钠/[3H]硼氢化钠法标记,并用Triton X - 100裂解。大部分丝状肌动蛋白可在低离心力(15,600 g,4分钟)下沉淀,但一些肌动蛋白丝需要高速离心(100,000 g,3小时)才能沉淀。后一种丝与低速沉淀中的丝不同,在于它们不能被Ca2+解聚,即使从经凝血酶激活的血小板的Triton X - 100裂解物中也不能在低离心力下沉淀。肌动蛋白结合蛋白与两种类型的丝一起沉淀,但3H标记的膜糖蛋白主要与高速丝一起回收。与这种“膜骨架”一起回收的主要3H标记糖蛋白是糖蛋白(GP)Ib。约70%的血小板GP Ib存在于该骨架中。其他几种次要糖蛋白,包括超过50%的GP Ia和少量三种分子量大于200,000的未鉴定糖蛋白,也与膜骨架一起回收。GP Ib、GP Ia、一种分子量为250,000的次要膜糖蛋白和肌动蛋白结合蛋白的Triton X - 100不溶性是由于它们与肌动蛋白丝的结合,因为当肌动蛋白丝用脱氧核糖核酸酶I解聚并在蔗糖梯度上与肌动蛋白丝共分离时,它们变得可溶于Triton X - 100。当用Triton X - 100提取分离的血小板质膜时,肌动蛋白、肌动蛋白结合蛋白和GP Ib作为Triton X - 100残渣被回收。这些研究表明,未受刺激的血小板含有由肌动蛋白丝和肌动蛋白结合蛋白组成的膜骨架,该骨架与细胞骨架的其余部分不同,并附着在质膜上的GP Ib、GP Ia和一种分子量为250,000的次要糖蛋白上。