The effect of (13 OOH) linoleic acid on human erythrocytes and on erythrocyte ghosts.
Peroxidized linoleic acid (13 OOH) induces lipid peroxidation, measured as malondialdehyde in erythrocyte ghosts and intact erythrocytes. This process can be inhibited by desferal, thiourea and butylated hydroxytoluene. During the lipid peroxidation process fluorescent chromolipids are formed. The synthesis of these chromolipids can be blocked by desferal. Peroxidized linoleic acid gives cross-linking of the proteins present in the membranes leading to the formation of higher molecular weight proteins. Also in the lower molecular weight region of SDS-electrophoresis a protein band is formed. The cross-linking process of the membrane protein is most effectively blocked by thiourea, to some extent by butylated hydroxytoluene and hardly at all by desferal. Addition of peroxidized linoleic acid to intact erythrocytes leads to a drop in the glutathione level (analogous to cumene hydroperoxide). In the presence of glucose the glutathione level can be restored.
D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D005978:Glutathione / Q000097:blood; D006801:Humans; D007700:Kinetics; D008041:Linoleic Acids / Q000494:pharmacology*; D008054:Lipid Peroxides / Q000494:pharmacology*; D008315:Malondialdehyde / Q000097:blood; D008565:Membrane Proteins / Q000097:blood / Q000302:isolation & purification; D008970:Molecular Weight
D008041:Linoleic Acids; D008054:Lipid Peroxides; D008565:Membrane Proteins; C008285:linoleic acid hydroperoxide; D008315:Malondialdehyde; D005978:Glutathione