血小板和内皮细胞血小板反应蛋白的细胞黏附及纤维蛋白原结合特性不受70 kDa和18 kDa抗蛋白酶结构域结构差异的影响。

Cell attachment and fibrinogen binding properties of platelet and endothelial cell thrombospondin are not affected by structural differences in the 70 and 18 kDa protease-resistant domains.

作者信息

Clezardin P, Bourdillon M C, Hunter N R, McGregor J L

机构信息

INSERM U63, Laboratoire d'Hémobiologie, Faculté de Médecine A. Carrel, Lyon, France.

出版信息

FEBS Lett. 1988 Feb 15;228(2):215-8. doi: 10.1016/0014-5793(88)80001-2.

DOI:10.1016/0014-5793(88)80001-2

PMID:3342880

Abstract

Structural differences between platelet and endothelial cell thrombospondin (TBSP) were found in two protease-resistant domains (70 and 18 kDa). The 70 kDa fragment is involved in the binding of TBSP to fibrinogen and the 18 kDa fragment in the attachment to various cultured cells. Despite these structural differences, platelet and endothelial cell TBSP bound with the same affinity to fibrinogen and mediated the attachment of smooth muscle cells but not of endothelial cells.

摘要

在血小板和内皮细胞的血小板反应蛋白（TBSP）之间发现了两个抗蛋白酶结构域（70 kDa和18 kDa）的结构差异。70 kDa片段参与TBSP与纤维蛋白原的结合，而18 kDa片段参与与各种培养细胞的附着。尽管存在这些结构差异，但血小板和内皮细胞的TBSP以相同的亲和力与纤维蛋白原结合，并介导平滑肌细胞而非内皮细胞的附着。