The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Mechanisms of copper- and iron-dependent oxidative modification of human low density lipoprotein
Open accessAbstract
Oxidative modification of low density lipoprotein (LDL) has been suggested as a causal step in atherosclerosis, and both redox-active transition metal ions and superoxide (O2.-) have been implicated in this process. In order to determine the mechanisms of metal ion-dependent oxidation of LDL in the presence of O2.-, LDL was exposed to hypoxanthine (HX) and purified xanthine oxidase (XO) without and with added CuCl2 or Fe(3+)-citrate. Production of O2.- and hydrogen peroxide (H2O2) at pH 7.4 by the HX/XO system in the absence of metal ions was not sufficient to oxidize LDL. Preincubation of LDL with Cu2+ or Fe(3+)-citrate with subsequent removal of metal ions not tightly bound to the lipoprotein did not enable the HX/XO system to oxidize LDL. However, incubation of LDL with HX/XO and Cu2+ resulted in extensive modification of LDL. Exposure of LDL to Cu2+ alone also led to extensive modification, although the LDL was initially free of detectable amounts of lipid hydroperoxides (LOOH), i.e., < 0.005 molecules of LOOH per LDL particle. Although HX/XO and Cu2+ did not produce detectable amounts of O2.- or aqueous hydroxyl radicals (HO.), oxidation of LDL under these conditions was partially inhibited by superoxide dismutase, and completely inhibited by the HO. scavenger thiourea. In contrast to Cu(2+)-mediated oxidation of LDL, oxidation mediated by Fe(3+)-citrate was strictly dependent upon O2.-, as it was abolished by omission of the HX/XO system or by addition of superoxide dismutase to this system.(ABSTRACT TRUNCATED AT 250 WORDS)
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Metadata
- Authors
- Lynch, S., & Frei, B.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 1993-10
- Volume
- 34
- Issue
- 10
- Pages
- 1745-1753
- ISSN
- 0022-2275 (ISSN-L)
- OpenAlex
- W2152344920
- Cited by
- 285
- References
- 62
- FWCI
- 7.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
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