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The relationship between the binding of ATP and calcium to annexin IV. Effect of nucleotide on the calcium-dependent interaction of annexin with phosphatidylserine.

With the use of ATP analogues, we have found that porcine liver annexin (Anx) IV can be covalently labelled with 8-azido[gamma-32P]-ATP in the presence of Ca2+ (Kd 4.2 microM) and that the labelling is prevented by asolectin/cholesterol liposomes or chelation of calcium ions. On the other hand, non-covalent binding of 2'-(or 3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate (TNP-ATP) to AnxIV occurs optimally in the presence of liposomes and Ca2+ (Kd 7 microM). These observations were further confirmed by the results of intrinsic fluorescence quenching of AnxIV with various nucleotides, suggesting the existence of a relationship between Ca(2+)-, phospholipid- and ATP-binding sites within the annexin molecule. The interaction of AnxIV with nucleotides does not significantly affect its in vitro properties concerning the binding to phosphatidylserine (PS) monolayers.