Immunochemical detection of lipid hydroperoxide- and aldehyde-modified proteins in diseases

Abstract

Polyunsaturated fatty acid (PUFA) is easily peroxidized by free radicals and enzymes. When this occurs, it results in the compromised integrity of cellular membranes and leads to lipid hydroperoxide as a major reaction product, which is decomposed into aldehyde. Lipid hydroperoxide-modified lysine is known to be an early product of the lipid peroxidation process, suggesting that it might be a PUFAoxidative stress marker during the initial stage of oxidative stress. Lipid hydroperoxides cause or enhance ROS-mediated DNA fragmentation. The α,β-unsaturated aldehydes are end products of PUFA peroxidation. They are highly reactive and readily attack and modify the protein amino acid residues into aldehyde-modified proteins. Lipid peroxidation-derived α,β-unsaturated aldehydes are capable of inducing cellular stress-responsive processes such as cell signaling and apoptosis. The lipid hydroperoxide- and aldehyde-modified proteins have been immunohistochemically detected in diverse pathological situations such as atherosclerosis, Alzheimer’s disease, Parkinson’s disease, and chemical material-induced liver injury and renal tubular injury in humans and experimental animals. These findings suggest that the expression of the lipid hydroperoxide- and aldehyde-modified proteins is closely associated with the pathogenesis of these diseases in humans and experimental animals.