Protein interactions between surface annexin A2 and S100A10 mediate adhesion of breast cancer cells to microvascular endothelial cells

FEBS Lett. 2013 Oct 1;587(19):3210-5. doi: 10.1016/j.febslet.2013.08.012. Epub 2013 Aug 27.

Abstract

Annexin A2 (AnxA2) and S100A10 are known to form a molecular complex. Using fluorescence-based binding assays, we show that both proteins are localised on the cell surface, in a molecular form that allows mutual interaction. We hypothesized that binding between these proteins could facilitate cell-cell interactions. For cells that express surface S100A10 and surface annexin A2, cell-cell interactions can be blocked by competing with the interaction between these proteins. Thus an annexin A2-S100A10 molecular bridge participates in cell-cell interactions, revealing a hitherto unexplored function of this protein interaction.

Keywords: 2′,7′-bis-(2-carboxyethyl)-5,6-carboxyfluorescein acetoxymethylester; Annexin; AnxA2; BCECF-AM; Cell–cell interaction; EGM-2; HBME cells; HMEC; HUVEC; Protein interaction; S100 protein; annexin A2; endothelial growth medium-2; human bone marrow endothelial cells; human microvascular endothelial cell; human umbilical vein endothelial cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Annexin A2 / metabolism*
  • Annexin A2 / physiology
  • Breast Neoplasms / metabolism
  • Breast Neoplasms / pathology*
  • Cell Adhesion / physiology*
  • Cell Line, Tumor
  • Cells, Cultured
  • Endothelium, Vascular / cytology*
  • Female
  • Humans
  • Protein Binding
  • S100 Proteins / metabolism*
  • S100 Proteins / physiology

Substances

  • Annexin A2
  • S100 Proteins
  • S100 calcium binding protein A10