Lysine residues of annexin VI are responsible for glycosaminoglycan- and phospholipid-binding activities

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Annexin VI is known to bind to glycosaminoglycans as well as phospholipids. We investigated the effects of chemical modification of annexin VI lysine residues on glycosaminoglycan-binding by solid phase assays and on phospholipid-binding by an optical biosensor system. As the concentration of the modifying reagent, pyridoxal 5'-phosphate, was increased, the extent of modification increased and the bindings of modified annexin VI to the ligands decreased, suggesting that lysine residues are important for the interactions of annexin VI with both glycosaminoglycans and phospholipids. Quantitatively however, the chemical modification affected the binding to glycosaminoglycans more than to phospholipids.

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