Development and application of site-specific proteomic approach for study protein S-nitrosylation

作者：Liu Miao; Talmadge James E; Ding Shi Jian^*

来源：Amino Acids, 2012, 42(5): 1541-1551.

DOI：10.1007/s00726-012-1279-x

• S-nitrosylation
• Proteomics
• Identification
• Quantification

Protein S-nitrosylation is the covalent redox-related modification of cysteine sulfhydryl groups with nitric oxide, creating a regulatory impact similar to phosphorylation. Recent studies have reported a growing number of proteins to be S-nitrosylated in vivo resulting in altered functions. These studies support S-nitrosylation as a critical regulatory mechanism, fine-tuning protein activities within diverse cellular processes and biochemical pathways. In addition, S-nitrosylation appears to have key roles in the etiology of a broad range of human diseases. In this review, we discuss recent advances in proteomic approaches for the enrichment, identification, and quantitation of cysteine S-nitrosylated proteins and peptides. These advances have provided analytical tools with the power to interpret the impact of S-nitrosylation at the system level, providing a new platform for drug discovery and the identification of diagnostic markers for human diseases.

• 出版日期2012-5