EPR study of annexin V-cardiolipin Ca-mediated interaction in phospholipid vesicles and isolated mitochondria.
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.
Megli
F M
FM
Centro di Studio sui Mitocondri e Metabolismo Energetico, CNR, Università di Bari, Italy.
Selvaggi
M
M
De Lisi
A
A
Quagliariello
E
E
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
D017304:Annexin A5; D002308:Cardiolipins; D010743:Phospholipids; D002118:Calcium