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膜联蛋白II与细胞表面纤维蛋白溶解的调节

Annexin II and regulation of cell surface fibrinolysis.

作者信息

Hajjar K A, Acharya S S

机构信息

Department of Pediatrics, Weill Medical College of Cornell University, New York, New York 10021, USA.

出版信息

Ann N Y Acad Sci. 2000 May;902:265-71. doi: 10.1111/j.1749-6632.2000.tb06321.x.

Abstract

The regulated function of the fibrinolytic system is fundamental to the solubilization of fibrin-containing thrombi and to a number of other biologic processes. In recent years, several receptors, which serve to localize proteolytic activity on the cell surface, have been identified on endothelial cells, blood cells, neuronal cells, and tumor cells. One such receptor is annexin II, a calcium- and phospholipid-binding protein that serves as a profibrinolytic co-receptor for tissue plasminogen activator and plasminogen on endothelial cells. Accumulating evidence suggests that impaired cell surface fibrinolytic assembly could lead to progressive atherothrombotic disease. In addition, dysregulation of annexin II expression in acute promyelocytic leukemia is an important mechanism for the bleeding diathesis associated with this malignancy.

摘要

纤维蛋白溶解系统的调节功能对于含纤维蛋白血栓的溶解以及许多其他生物过程至关重要。近年来,已在内皮细胞、血细胞、神经元细胞和肿瘤细胞上鉴定出几种受体,这些受体可将蛋白水解活性定位在细胞表面。膜联蛋白II就是这样一种受体,它是一种钙和磷脂结合蛋白,在内皮细胞上作为组织纤溶酶原激活物和纤溶酶原的促纤溶共受体。越来越多的证据表明,细胞表面纤维蛋白溶解组装受损可能导致进行性动脉粥样硬化血栓形成疾病。此外,急性早幼粒细胞白血病中膜联蛋白II表达失调是与这种恶性肿瘤相关的出血素质的重要机制。

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