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凝血酶敏感蛋白(TSP)是血小板α-颗粒中贮存的一种糖蛋白,由3条完全相同的肽链组成,含有1152个氨基酸残基。在电镜下观察,TSP呈哑铃形。TSP分子中部有3类重复顺序,Ⅰ型重复顺序见于多种补体成分(如备解素,C7,C8及C9)及疟原虫合成的几种蛋白质;Ⅱ型重复顺序为表皮生长因子前体(EGFP)样结构;Ⅲ型重复顺序见于钙调蛋白,含能被粘连蛋白受体识别的RGD三肽顺序和凝血因子ⅩⅢa转酰胺作用的部位(IQQ),这些结构特点决定了TSP在细胞粘连、血小板聚集等过程中具有重要的生理意义。
Thrombin-sensitive protein (TSP) is a glycoprotein stored in platelet α-particles, composed of three identical peptide chains, containing 1152 amino acid residues. Observed by electron microscopy, TSP dumbbell shape. There are three kinds of repeats in the middle part of TSP, the type Ⅰ repeats are found in several kinds of complement components (such as properdin, C7, C8 and C9) and several proteins synthesized by Plasmodium. The type Ⅱ repeats are epidermal growth factor precursor EGFP). The type Ⅲ repeats were found in calmodulin, the sequence of RGD tripeptide that can be recognized by laminin receptors and the transglutaminase site (IQQ) of factor XIIIa. These structural features determine the role of TSP in cell adhesion, Platelet aggregation process has an important physiological significance.