Annexin II modulates volume-activated chloride currents in vascular endothelial cells

Bernd Nilius, Volker Gerke, Jean Prenen, Geza Szücs, Stephan Heinke, Klaus Weber, Guy Droogmans

Research output: Article

65 Citations (Scopus)


The membrane-associated, microfilament-binding protein annexin II is abundantly expressed in endothelial cells from calf pulmonary artery (CPAE cells). We have analyzed its role in the regulation of volume-activated chloride currents (I(Cl, vol)) by loading the cells via the patch pipette with a peptide comprising the N-terminal 14 residues of annexin II. This sequence harbors the binding site for the intracellular annexin II ligand, p11, and the peptide interferes with the annexin II-p11 complex formation. Loading of a CPAE cell with this peptide caused a gradual decrease in the amplitude of I(Cl, vol) during repetitive stimulations with a 28% hypotonic extracellular solution. This run down of the current was virtually absent in untreated cells and in cells that were loaded with a mutated 14-amino acid peptide, which has a single amino acid replacement known to result in a more than 1000 times reduced affinity for binding to p11. We conclude that annexin II-p11 complex formation is either directly or indirectly involved in the activation of I(Cl, vol) in endothelial cells.

Original languageEnglish
Pages (from-to)30631-30636
Number of pages6
JournalJournal of Biological Chemistry
Issue number48
Publication statusPublished - dec. 14 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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