Iron binding to microsomes and liposomes in relation to lipid peroxidation.
The effects of ADP, ATP, citrate and EDTA on iron-dependent microsomal and liposomal lipid peroxidation, and on 59FeCl3 binding to the lipid membranes were measured. The aim was to test if initiation of lipid peroxidation is a site-specific mechanism requiring bound iron. In the absence of chelator, iron was bound to both membranes. EDTA and citrate removed the iron and inhibited peroxidation. ATP and ADP stimulated peroxidation, but whereas ADP allowed only half of the iron to remain bound, all was removed by ATP. Chelators, therefore, cannot be simply influencing a site-specific mechanism. Their effects must relate to the reactivities of the different iron chelates as initiators of lipid peroxidation.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002614:Chelating Agents / Q000494:pharmacology*; D002712:Chlorides; D002951:Citrates / Q000494:pharmacology; D019343:Citric Acid; D004492:Edetic Acid / Q000494:pharmacology; D005290:Ferric Compounds / Q000378:metabolism*; D008054:Lipid Peroxides / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D002614:Chelating Agents; D002712:Chlorides; D002951:Citrates; D005290:Ferric Compounds; D008054:Lipid Peroxides; D008081:Liposomes; D019343:Citric Acid; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D004492:Edetic Acid; C024555:ferric chloride