Aniline-induced splenic iron overload may hasten iron-mediated protein oxidation/degradation. ROS attack on proteins can oxidise several amino acid residues, including lysine, histidine, methionine, tryptophan, proline, arginine, phenylalanine, and cysteine, resulting in carbonyl products that can cause protein fragmentation, aggregation, and cellular damage. Protein oxidation caused by oxidative stress also results in the loss of enzyme activities such as glutamine synthase and alcohol dehydrogenase.
Aniline has been shown to increase protein oxidation (carbonyl content) in the spleen in multiple dose and subchronic studies in rats. Initial Western blot studies revealed two oxidised proteins (114 and 69 kDa) in both postnuclear and mitochondrial fractions of aniline-treated rat spleen. Studies with the aniline metabolites PHA and NB support the role of protein oxidation in splenic toxicity. Because protein oxidation has been linked to a number of pathological conditions, including inflammation, atherosclerosis, cataractogenesis, diabetes, neurological disorders, respiratory distress syndrome, muscular dystrophy, Parkinson disease, and cystic fibrosis, aniline-induced protein oxidation in the spleen could be a critical early event, causing functional changes in the spleen.
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