Bydoun Moamen, Waisman David M
Department of Pathology, Dalhousie University, Sir Charles Tupper Medical Building, 5850 College Street, PO Box 1500, Halifax, Nova Scotia, B3H 4R2, Canada.
Future Oncol. 2014 Dec;10(15):2469-79. doi: 10.2217/fon.14.163.
Plasminogen receptors are becoming increasingly relevant in regulating many diseases such as cancer, stroke and inflammation. However, controversy has emerged concerning the putative role of some receptors, in particular annexin A2, in binding plasminogen. Several reports failed to account for the effects of annexin A2 on the stability and conformation of its binding partner S100A10. This has created an enduring ambiguity as to the actual function of annexin A2 in plasmin regulation. Supported by a long line of evidence, we conclude that S100A10, and not annexin A2, is the primary plasminogen receptor within the annexin A2-S100A10 complex and contributes to the plasmin-mediated effects that were originally ascribed to annexin A2.
纤溶酶原受体在调控许多疾病（如癌症、中风和炎症）中变得越来越重要。然而，关于某些受体，特别是膜联蛋白A2在结合纤溶酶原方面的假定作用，已经出现了争议。一些报告未能考虑膜联蛋白A2对其结合伴侣S100A10的稳定性和构象的影响。这就导致了关于膜联蛋白A2在纤溶酶调节中的实际功能一直存在模糊性。在一系列证据的支持下，我们得出结论，在膜联蛋白A2 - S100A10复合物中，S100A10而非膜联蛋白A2是主要的纤溶酶原受体，并促成了最初归因于膜联蛋白A2的纤溶酶介导的效应。
