The role of lipid hydroperoxides in the myoglobin-dependent oxidation of LDL. Arch Biochem Biophys 1994 Oct;314(1):39-44
Date
10/01/1994Pubmed ID
7944405DOI
10.1006/abbi.1994.1409Scopus ID
2-s2.0-0027943772 (requires institutional sign-in at Scopus site) 83 CitationsAbstract
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.
Author List
Hogg N, Rice-Evans C, Darley-Usmar V, Wilson MT, Paganga G, Bourne LAuthor
Neil Hogg PhD Associate Dean, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ElectrophoresisHumans
Linoleic Acids
Lipid Peroxides
Lipoproteins, LDL
Metmyoglobin
Myoglobin
Oxidation-Reduction
Pentetic Acid
