Journal of neural transmission. Supplementum

Deamination of methylamine and angiopathy; toxicity of formaldehyde, oxidative stress and relevance to protein glycoxidation in diabetes.

PMID 9564620


Semicarbazide-sensitive amine oxidase (SSAO) is located in the vascular smooth muscles, retina, kidney and the cartilage tissues, and it circulates in the blood. The enzyme activity has been found to be significantly increased in blood and tissues in diabetic patients and animals. Methylamine and aminoacetone are endogenous substrates for SSAO. The deaminated products are formaldehyde and methylglyoxal respectively, as well as H2O2 and ammonia, which are all potentially cytotoxic. Formaldehyde and methylglyoxal are cytotoxic towards endothelial cells. Excessive SSAO-mediated deamination may directly initiate endothelial injury and plaque formation, increase oxidative stress, which can potentiate oxidative glycation, and/or LDL oxidation and damage vascular systems. Formaldehyde is also capable of exacerbating advanced glycation, and thus increase the complexity of protein cross-linking. Uncontrolled SSAO-mediated deamination may be involved in the acceleration of the clinical complications in diabetes.