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S-nitrosylation of proteins increased the susceptivity of SH-SY5Y cells with high redox status to nitric oxide

Jie He;Chang ChenThe Center for Molecular Biology;the Institute of Biophysics;Chinese Academy of Sciences;P O Box 33;15 Datun Road;Chaoyang District;Beijing 100101;China

   S-nitrosylation has been brought forward to be a prototypic redox-based post-translational modification in parallel with O-phosphorylation. However, the relationship between S-nitrosylation and cell redox status and the details of the S-nitrosylation mechanism involved in the cellular processes remain to be elucidated. In the present study, we investigated the role of S-nitrosylation in the susceptibility of glutathione (GSH) -depleted SH-SY5Y to S-nitrosoglutathione (GSNO) insults. Our results showed that: (1) D,L-buthionine-[s,r]-sulfoximine (BSO) greatly increased the susceptibility of SH-SY5Y cells to GSNO s insult, and it is intriguing that the total cellular S-nitrosothiols (SNOs) increased significantly in the process. (2) The increased SNOs were primarily contributed by the S-nitrosylated proteins (PrSNO); moreover, the accumulation of PrSNO was dependent on the degree of oxidative status of the cells. (3) Reversible modification of the thiols appeared to mediate the susceptivity of the cells to GSNO s insults, and reactive oxygen species (ROS) mediated the process. These results deepened our understanding of the S-nitrosylation mechanism in the redox-related physiological and pathological processed.……