Oxidised low density lipoproteins induce iron release from activated myoglobin.
Recent reports have detected the presence of iron in human atherosclerotic lesions [Biochem. J. 286 (1992) 901-905]. This study provides evidence for a biochemical mechanism whereby iron is released from myoglobin by low density lipoprotein (LDL) which has become oxidised by the ferryl myoglobin species. The haem destabilisation and iron release are inhibited by monohydroxamate compounds and desferrioxamine through their ability to inhibit the propagation of LDL oxidation. Thus, iron may derive from the myoglobin released from ruptured cells in the oxidising environment of the atherosclerotic lesion.
Division of Biochemistry, UMDS-Guy's Hospital, London, UK.
C
C
Rice-Evans
E
E
Green
G
G
Paganga
C
C
Cooper
J
J
Wrigglesworth
D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006877:Hydroxamic Acids / Q000494:pharmacology; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D015227:Lipid Peroxidation; D008077:Lipoproteins, LDL / Q000494:pharmacology*; D008786:Metmyoglobin / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism*; D010084:Oxidation-Reduction; D013053:Spectrophotometry
D006877:Hydroxamic Acids; D008077:Lipoproteins, LDL; D009211:Myoglobin; D008786:Metmyoglobin; D006418:Heme; C082082:N-methyl hexanoylhydroxamic acid; D006861:Hydrogen Peroxide; D007501:Iron