血小板中的肌动蛋白动力学
Actin dynamics in platelets.
作者信息
Bearer E L, Prakash J M, Li Z
机构信息
Department of Pathology and Laboratory Medicine, Brown University, Providence, Rhode Island 02912, USA.
出版信息
Int Rev Cytol. 2002;217:137-82. doi: 10.1016/s0074-7696(02)17014-8.
The human blood platelet circulates in the blood as a non-adherent disk. Upon receiving signals of blood vessel damage, the platelet reorganizes its actin cytoskeleton which transforms it into a spiky dynamic adherent glue. This transformation involves a temporal sequence of four morphologically distinct steps which is reproducible in vitro. The actin dynamics underlying these shape changes depend on a large number of actin-binding proteins. Maintenance of the discoid shape requires actin-binding proteins that inhibit these reorganizations, whereas transformation involves other proteins, some to disassemble old filaments and others to polymerize new ones. F-Actin-affinity chromatography identified a large set of actin-binding proteins including VASP, Arp2 and 2E4/kaptin. Recent discoveries show that VASP inhibits filament disassembly and Arp2/3 is required to polymerize new filaments. Morphological analysis of the distribution of these actin-binding proteins in spread platelets together with biochemical measurements of their interactions with actin lead to a model of interactions with actin that mediate shape change.
人类血小板在血液中以非黏附性圆盘的形式循环。接收到血管损伤信号后，血小板会重组其肌动蛋白细胞骨架，使其转变为带刺的动态黏附性胶状物。这种转变涉及四个形态上不同的步骤的时间序列，这一序列在体外是可重现的。这些形状变化背后的肌动蛋白动力学依赖于大量肌动蛋白结合蛋白。维持盘状形状需要抑制这些重组的肌动蛋白结合蛋白，而转变则涉及其他蛋白质，一些用于拆解旧的细丝，另一些用于聚合新的细丝。F-肌动蛋白亲和层析鉴定出了一大组肌动蛋白结合蛋白，包括血管扩张刺激磷蛋白（VASP）、肌动蛋白相关蛋白2（Arp2）和2E4/卡普汀（2E4/kaptin）。最近的发现表明，血管扩张刺激磷蛋白抑制细丝拆解，而肌动蛋白相关蛋白2/3是聚合新细丝所必需的。对这些肌动蛋白结合蛋白在伸展血小板中的分布进行形态学分析，以及对它们与肌动蛋白相互作用的生化测量，得出了一个介导形状变化的与肌动蛋白相互作用的模型。
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