S. Mukhopadhyay et Wh. Cho, INTERACTIONS OF ANNEXIN-V WITH PHOSPHOLIPID MONOLAYERS, Biochimica et biophysica acta. Biomembranes, 1279(1), 1996, pp. 58-62
To understand the mechanism of annexin V-membrane interactions, we mea
sured the interaction of human recombinant annexin V with phospholipid
monolayers with differing head group and acyl group structures. Annex
in V interacted with anionic phospholipid monolayers via non-specific
electrostatic interactions, which was highly dependent on the surface
pressure of monolayer with a sharp maximum. The unique surface pressur
e dependence of the annexin V-monolayer binding is strikingly similar
to that observed for the binding of Ca2+ to anionic phospholipid monol
ayers, which indicates that the annexin V-bound Ca2+ binds two phospho
lipids at the membrane surface and that factors governing the Ca2+-pho
spholipid complex formation regulate the overall annexin V-Ca2+-membra
ne interactions.