On the contribution of S100A10 and annexin A2 to plasminogen activation and oncogenesis: an enduring ambiguity
On the contribution of S100A10 and annexin A2 to plasminogen activation and oncogenesis: an enduring ambiguity
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DOI：
10.2217/fon.14.163
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发表时间：
2014-01-01
期刊：
影响因子：
3.3
通讯作者：
Waisman, David M.
中科院分区：
文献类型：
--
作者：
Bydoun, Moamen;Waisman, David M.
纤溶酶原受体在调节许多疾病如癌症、中风和炎症中变得越来越相关。然而，关于某些受体，特别是膜联蛋白A2在结合纤溶酶原中的假定作用，出现了争议。一些报道未能解释膜联蛋白A2对其结合伴侣S100 A10的稳定性和构象的影响。这就造成了膜联蛋白A2在纤溶酶调节中的实际功能的长期模糊性。通过一系列证据的支持，我们得出结论，S100 A10，而不是膜联蛋白A2，是膜联蛋白A2-S100 A10复合物内的主要纤溶酶原受体，并有助于纤溶酶介导的作用，最初归因于膜联蛋白A2。
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.