Homocysteinylation and Sulfhydration in Diseases.

Si-Min Chen, Xiao-Qing Tang

Journal: Current neuropharmacology 2022;20(9):1726-1735

PMID: 34951391

Abstract

Homocysteine (Hcy) is an important intermediate in methionine metabolism and generation of one-carbon units, and its dysfunction is associated with many pathological states. Although Hcy is a non-protein amino acid, many studies have demonstrated protein-related homocysteine metabolism and possible mechanisms underlying homocysteinylation. Homocysteinylated proteins lose their original biological function and have a negative effect on the various disease phenotypes. Hydrogen sulfide (HS) has been recognized as an important gaseous signaling molecule with mounting physiological properties. HS modifies small molecules and proteins via sulfhydration, which is supposed to be essential in the regulation of biological functions and signal transduction in human health and disorders. This review briefly introduces Hcy and HS, further discusses pathophysiological consequences of homocysteine modification and sulfhydryl modification, and ultimately makes a prediction that HS might exert a protective effect on the toxicity of homocysteinylation of target protein via sulfhydration. The highlighted information here yields new insights into the role of protein modification by Hcy and HS in diseases.

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Address: Emergency Intensive Care Unit, Department of Emergency, Xiangtan Central Hospital, Xiangtan, 411100, Hunan, P. R. China.; The First Affiliated Hospital, Institute of Neurology, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, P. R. China.; Institute of Neuroscience, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, P. R. China.
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