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J Biol Chem, Vol. 273, Issue 31, 19679-19684, July 31, 1998

The Annexin II-p11 Complex Is Involved in Regulated Exocytosis in Bovine Pulmonary Artery Endothelial Cells

Julia KönigDagger , Jean Prenen§, Bernd Nilius§, and Volker GerkeDagger

From the Dagger  Insitute for Medical Biochemistry, University of Münster, von-Esmarch-Str. 56, D-48149 Münster, Federal Republic of Germany and the § Laboratory of Physiology, Campus Gasthuisberg, Catholic University of Leuven, B-3000 Leuven, Belgium

Annexin II is a member of a multigene family of Ca2+-regulated, membrane-binding proteins implicated through biochemical and perforated cell experiments in Ca2+-triggered secretion. Within most cells annexin II resides in a tight heterotetrameric complex with a cellular protein ligand, p11, and complex formation is mediated via the N-terminal 14 residues of annexin II including the N-terminal acetyl group. To analyze at the single cell level whether the annexin II-p11 complex is involved in regulated secretion, we used membrane capacitance measurements to follow exocytotic fusion events in bovine aortic endothelial cells manipulated with respect to their annexin II-p11 complex formation. Upon guanosine 5'-O-(thiotriphosphate) (GTPgamma S) stimulation, the endothelial cells show a significant increase in membrane capacitance which is generally preceded by a transient rise in intracellular Ca2+ and thus indicative of the occurrence of Ca2+-regulated secretion. The GTPgamma S-induced capacitance increase is markedly reduced in cells loaded with a synthetic peptide, Ac1-14, which corresponds in sequence to the N-terminal 14 residues of annexin II in their correctly acetylated form and which is capable of disrupting preformed annexin II-p11 complexes. The effect of the peptide is highly specific as the nonacetylated variant, N1-14, which is incapable of disrupting annexin II-p11, does not interfere with the GTPgamma S-induced increase in membrane capacitance. These data show that intact annexin II-p11 complexes are indispensable for regulated exocytosis to occur in an efficient manner in endothelial cells.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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