The role of lipid hydroperoxides in the myoglobin-dependent oxidation of LDL.
It has previously been reported that mb in both the iron-oxo ferryl and the ferric oxidation states can promote lipid peroxidation and lead to oxidative modification of low-density lipoprotein. The mechanism of these oxidation reactions is unclear and could involve either lipid hydroperoxide-dependent or independent reactions. In order to ascertain which of the afore-mentioned mechanisms predominates, the effects of exogenous lipid hydroperoxides on the ability of Mb, in its various oxidation states, to oxidize low-density lipoprotein has been investigated. The results suggest that oxidation proceeds through a one-electron redox cycle between met and ferryl myoglobin and that the reactions of both redox forms are at least partially dependent on lipid hydroperoxides within the LDL particle.
Hogg
N
N
Division of Biochemistry, UMDS-Guy's Hospital, London, UK.
Rice-Evans
C
C
Darley-Usmar
V
V
Wilson
M T
MT
Paganga
G
G
Bourne
L
L
D004586:Electrophoresis; D006801:Humans; D008041:Linoleic Acids / Q000494:pharmacology; D008054:Lipid Peroxides / Q000494:pharmacology*; D008077:Lipoproteins, LDL / Q000737:chemistry / Q000378:metabolism*; D008786:Metmyoglobin / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism*; D010084:Oxidation-Reduction; D004369:Pentetic Acid / Q000494:pharmacology
D008041:Linoleic Acids; D008054:Lipid Peroxides; D008077:Lipoproteins, LDL; D009211:Myoglobin; C028048:ferrylmyoglobin; D008786:Metmyoglobin; C038649:13-hydroperoxy-9,11-octadecadienoic acid; D004369:Pentetic Acid