Molecular basis of platelet granule secretion
Molecular basis of platelet granule secretion
复制标题
DOI：
10.1161/01.atv.0000075965.88456.48
复制
发表时间：
2003-07-01
影响因子：
8.7
通讯作者：
Flaumenhaft, R
中科院分区：
文献类型：
--
作者：
Flaumenhaft, R
能量依赖性释放颗粒内容物从活化血小板是一个公认的组成部分正常止血和血栓形成。膜融合在这一过程中的作用已经被推测了几十年，但直到最近才在分子水平上研究血小板膜融合的机制。这些研究表明，血小板膜融合是由膜双分子层的脂质成分、被称为SNARE蛋白的跨膜蛋白以及与SNARE蛋白相互作用的伴侣蛋白控制的。这种核心膜融合机制受细胞骨架组织、细胞内钙水平、激酶活性和细胞内蛋白酶活性的激活依赖性变化控制。通过这些机制，配体与其同源细胞表面受体的相互作用传递给膜融合机制，促进膜融合和血小板颗粒内容物的分泌。
The energy-dependent release of granule contents from activated platelets is a well-established component of normal hemostasis and thrombosis. A role for membrane fusion in this process has been presumed for decades, but only recently have the mechanisms of platelet membrane fusion been investigated at the molecular level. Such studies have demonstrated that platelet membrane fusion is controlled by lipid components of the membrane bilayer, by transmembrane proteins termed SNARE proteins, and by chaperone proteins that interact with SNARE proteins. This core membrane fusion machinery is controlled by activation-dependent changes in cytoskeletal organization, intracellular calcium levels, kinase activity, and intracellular protease activity. Through these mechanisms, interactions of ligands with their cognate cell-surface receptors are transmitted to the membrane fusion machinery to facilitate membrane fusion and secretion of granule contents from platelets.