Premium
Oxidised low density lipoproteins induce iron release from activated myoglobin
Author(s) -
Rice-Evans Catherine,
Green Emma,
Paganga George,
Cooper Christopher,
Wrigglesworth John
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81786-y
Subject(s) - myoglobin , destabilisation , chemistry , biochemistry , low density lipoprotein , hemeprotein , oxidative phosphorylation , lipoprotein , biophysics , heme , cholesterol , enzyme , biology , medicine , nursing
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.