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Enhanced lipid oxidation by oxidatively modified myoglobin: role of protein-bound heme.

Abstract：

:The formation of oxidized low density lipoprotein (LDL) is believed to play a significant role in the pathogenesis of atherosclerosis. Myoglobin in the presence of H(2)O(2) has been shown to catalyze LDL oxidation in vitro. It is established that an oxidatively altered form of myoglobin (Mb-H), which contains a prosthetic heme covalently crosslinked to the apoprotein, is a major product in the reaction of native myoglobin with peroxides. In the current study, we have shown for the first time that Mb-H, in the absence of exogenously added peroxides, oxidizes LDL and purified lipids, as determined by the formation of conjugated dienes, lipid peroxides, and thiobarbituric acid reactive substances. Moreover, the rate of oxidation of pure phosphatidylcholine by Mb-H was found to be at least sevenfold greater than that observed for native myoglobin. The current study strongly suggests a role for Mb-H in the lipid peroxidation observed with myoglobin.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Vuletich JL,Osawa Y,Aviram M

doi

10.1006/bbrc.2000.2349

subject

Has Abstract

pub_date

2000-03-24 00:00:00

pages

647-51

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92349-0

journal_volume

269

pub_type

杂志文章

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