Megli F M, Selvaggi M, De Lisi A, Quagliariello E
Centro di Studio sui Mitocondri e Metabolismo Energetico, CNR, Università di Bari, Italy.
Biochim Biophys Acta. 1995 Jun 14;1236(2):273-8. doi: 10.1016/0005-2736(95)00057-a.
The properties of the binding of annexin V to variously composed phospholipid vesicles have been studied by applying a recently developed EPR method, using an annexin V spin label. By this approach, this protein is seen to bind to acidic phospholipid-containing vesicles, as reported, thus confirming the reliability of the method. In addition, binding of this annexin to cardiolipin-containing vesicles has been studied in more depth, and the protein has been shown to have a distinct affinity for this phospholipid. As a cardiolipin-rich natural membrane system, mitochondrial membranes and mitoplasts from rat liver were considered, and a strong binding of AV to these membranes was observed. Having compared this binding with that to phospholipid vesicles, cardiolipin-rich microdomains in the mitochondrial membranes are proposed as the putative mitochondrial binding sites for annexin V.
