Role of heme compounds in the erythrocyte membrane damage induced by lipid hydroperoxide

• Published in: Chem. Pharm. Bull Vol. 34; no. 12; pp. 5063 - 5070
• Main Authors: 別府 正緻, 名児耶 雅子, 菊川 清見
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 01.12.1986; 公益社団法人日本薬学会; Maruzen
• Subjects: 13-linoleic acid hydroperoxide; Biological and medical sciences; Blood Proteins - metabolism; desferrioxamine; Erythrocyte Membrane - metabolism; erythrocytes; ferric ion; General and cellular metabolism. Vitamins; ghost; heme; Heme - metabolism; heme compound; hemin; hemoglobin; Humans; In Vitro Techniques; lipid oxidation; Lipid Peroxides - blood; lipids; man; Medical sciences; Pharmacology. Drug treatments; protein cross-linking; Membrane protein; Hemin; Oxyhemoglobin; Plasma membrane; Red blood cell; Hydroperoxide; Lipids; Crosslinking; Methemoglobin; Oxidation
• ISSN: 0009-2363

13-Linoleic acid hydroperoxide-induced lipid oxidation of human erythrocyte ghosts was substantially augmented by the addition of oxyhemoglobin, methernoglobin or hemin up to 100μM. The catalytic effect of the heme compounds was greater than that of ferric ion. At concentrations higher than 100μM, the effects of the heme compounds decreased, probably because the heme porphyrin scavenged the radical species generated. The heme compounds at the lower concentrations effectively stimulated the hydroperoxide-induced protein cross-linking of ghosts. Both lipid oxidation and protein cross-linking were markedly inhibited by desferrioxamine, indicating that some unidentified iron complex, not the heme compounds by themselves or the released ionic iron, acted as the catalyst of the reactions. The effective cross-linking of the ghost proteins at the lower concentrations of hemoglobin appeared to depend on the highly ordered conformation of the membrane consisting of lipid bilayer, membrane proteins and hemoglobin, since other soluble proteins were hardly cross-linked under similar conditions. At higher concentrations of hemoglobin, it may scavenge radical species and be denatured, instead of inducing lipid oxidation of ghosts.