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Glycated protein‐iron chelate increases lipid peroxide level in cultured aortic endothelial and smooth muscle cells
Author(s) -
Nishigaki Ikuo,
Yagil Kunio,
Tanimoto Akihide,
Sasaguri Yasuyuki
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202902
Subject(s) - bovine serum albumin , chelation , chemistry , lipid peroxide , fetal bovine serum , glycation , lipid peroxidation , deferoxamine , peroxide , biochemistry , medicine , endocrinology , oxidative stress , biology , cell , inorganic chemistry , receptor , organic chemistry
Formation of an iron chelate of glycated protein was demonstrated by the appearance of an absorption peak at approximately 270 nm after mixing glycated bovine serum albumin with FeCl3. This peak disappeared and a new peak appeared at approximately 420 nm to form an isosbestic point at approximately 340 nm by the addition of deferoxamine mesylate, an ironchelating agent, to the mixture, thus confirming the formation of the iron chelate of the glycated protein in the mixture. The lipid peroxide level was increased markedly in endothelial cells and slightly in smooth muscle cells from bovine aorta incubated in the medium containing glycated fetal bovine serum‐iron chelate. Morphological observation by phase‐contrast microscopy and scanning electron microscopy revealed that the glycated fetal bovine serumiron chelate caused intense damage to the endothelial cells. These results indicate that glycated protein‐iron chelate provokes lipid peroxidation, which explains at least in part the mechanism of atherogenesis found in diabetic patients.