On the contribution of S100A10 and annexin A2 to plasminogen activation and oncogenesis: an enduring ambiguity

Future Oncol. 2014 Dec;10(15):2469-79. doi: 10.2217/fon.14.163.

Abstract

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.

Keywords: S100A10; ambiguity; annexin A2; cancer; fibrinolysis; heterotetramer; invasion; plasmin; plasminogen.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Annexin A2 / physiology*
  • Carcinogenesis / metabolism
  • Disease Progression
  • Enzyme Activation
  • Fibrinolysin / metabolism
  • Humans
  • Neoplasms / enzymology*
  • Plasminogen / metabolism*
  • Plasminogen Activators / physiology*
  • S100 Proteins / physiology*

Substances

  • ANXA2 protein, human
  • Annexin A2
  • S100 Proteins
  • S100 calcium binding protein A10
  • Plasminogen
  • Plasminogen Activators
  • Fibrinolysin