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氯喹和伯胺抑制抗凝血酶III-胰蛋白酶复合物在培养细胞中的内化。

Chloroquine and primary amines inhibit the internalization of antithrombin III.trypsin complex in cultured cells.

作者信息

Savion N, Farzame N

出版信息

Thromb Res. 1985 Sep 15;39(6):671-82. doi: 10.1016/0049-3848(85)90251-8.

Abstract

Bovine corneal endothelial (BCE) cells have been shown to specifically bind, internalize and degrade antithrombin III (AT III).protease complexes as well as thrombin. Previous studies have indicated that chloroquine has no effect on the internalization of thrombin or other cell surface-bound ligands, but it inhibits their subsequent degradation. In contrast, the present study demonstrates the unique inhibitory effect of chloroquine on the internalization of 125I-AT III.trypsin complex by BCE cultures. Similarly, the primary amines, monodansylcadaverine and methylamine, inhibit the internalization of 125I-AT III.trypsin complex, but not the internalization of 125I-thrombin. The various amines used in this study revealed: (1) differences in the process of cellular binding and internalization between AT III.protease complex and thrombin, although the degradation of both internalized ligands proceed in an analogous manner; and (2) the unique sensitivity to chloroquine of 125I-AT III.trypsin complex internalization by cultured cells. These results might indicate that AT III.protease complexes are internalized via a distinct receptor and/or a different mechanism from thrombin.

摘要

牛角膜内皮(BCE)细胞已被证明能特异性结合、内化并降解抗凝血酶III(AT III)-蛋白酶复合物以及凝血酶。先前的研究表明,氯喹对凝血酶或其他细胞表面结合配体的内化没有影响,但它会抑制它们随后的降解。相比之下,本研究证明了氯喹对BCE培养物内化125I-AT III-胰蛋白酶复合物具有独特的抑制作用。同样,伯胺单丹磺酰尸胺和甲胺会抑制125I-AT III-胰蛋白酶复合物的内化,但不会抑制125I-凝血酶的内化。本研究中使用的各种胺类表明:(1)AT III-蛋白酶复合物和凝血酶在细胞结合和内化过程中存在差异,尽管两种内化配体的降解方式类似;(2)培养细胞对125I-AT III-胰蛋白酶复合物内化对氯喹具有独特的敏感性。这些结果可能表明,AT III-蛋白酶复合物是通过与凝血酶不同的受体和/或不同的机制内化的。

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