title: EPR study of annexin V-cardiolipin Ca-mediated interaction in phospholipid vesicles and isolated mitochondria.
abstract: 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.
authors.affiliation: Centro di Studio sui Mitocondri e Metabolismo Energetico, CNR, Università di Bari, Italy.
authors.forename: F M
authors.initials: FM
authors.lastname: Megli
authors.forename: M
authors.initials: M
authors.lastname: Selvaggi
authors.forename: A
authors.initials: A
authors.lastname: De Lisi
authors.forename: E
authors.initials: E
authors.lastname: Quagliariello
mesh_terms: D000818:Animals; D017304:Annexin A5 / Q000737:chemistry*; D002118:Calcium / Q000494:pharmacology*; D002308:Cardiolipins / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D007425:Intracellular Membranes / Q000737:chemistry; D008930:Mitochondria, Liver / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D051381:Rats
chemical_list: D017304:Annexin A5; D002308:Cardiolipins; D010743:Phospholipids; D002118:Calcium