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Komatsubara AT, Asano T, Tsumoto H, et al. Proteomic analysis of S-nitrosylation induced by 1-methyl-4-phenylpyridinium (MPP+). Proteome Sci. 2012;10(1):74doi: 10.1186/1477-5956-10-74.
Komatsubara, A. T., Asano, T., Tsumoto, H., Shimizu, K., Nishiuchi, T., Yoshizumi, M., & Ozawa, K. (2012). Proteomic analysis of S-nitrosylation induced by 1-methyl-4-phenylpyridinium (MPP+). Proteome science, 10(1), 74. https://doi.org/10.1186/1477-5956-10-74
Komatsubara, Akira T, et al. "Proteomic analysis of S-nitrosylation induced by 1-methyl-4-phenylpyridinium (MPP+)." Proteome science vol. 10,1 (2012): 74. doi: https://doi.org/10.1186/1477-5956-10-74
Komatsubara AT, Asano T, Tsumoto H, Shimizu K, Nishiuchi T, Yoshizumi M, Ozawa K. Proteomic analysis of S-nitrosylation induced by 1-methyl-4-phenylpyridinium (MPP+). Proteome Sci. 2012 Dec 29;10(1):74. doi: 10.1186/1477-5956-10-74. PMID: 23273257; PMCID: PMC3576269.
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Proteome Sci. 2012 Dec 29;10(1):74. doi: 10.1186/1477-5956-10-74.

Proteomic analysis of S-nitrosylation induced by 1-methyl-4-phenylpyridinium (MPP+).

Proteome science

Akira T Komatsubara, Tomoya Asano, Hiroki Tsumoto, Kazuharu Shimizu, Takumi Nishiuchi, Masanori Yoshizumi, Kentaro Ozawa

Affiliations

  1. Department of Pharmacology, Nara Medical University School of Medicine, 840 Shijo-cho, Kashihara, Nar, 634-8521, Japan.
  2. Department of Genomic Drug Discovery Science, Kyoto University Graduate School of Pharmaceutical Sciences, Sakyo-ku, Kyoto, Japan.
  3. Division of Functional Genomics, Advanced Science Research Center, Kanazawa University, Kanazawa, Japan.
  4. World-Leading Drug Discovery Research Center, Kyoto University, Sakyo-ku, Kyoto, Japan.
  5. Department of Nanobio Drug Discovery, Kyoto University Graduate School of Pharmaceutical Sciences, Sakyo-ku, Kyoto, 606-8501, Japan.

PMID: 23273257 PMCID: PMC3576269 DOI: 10.1186/1477-5956-10-74

Abstract

BACKGROUND: Nitric oxide (NO) mediates its function through the direct modification of various cellular targets. S-nitrosylation is a post-translational modification of cysteine residues by NO that regulates protein function. Recently, an imbalance of S-nitrosylation has also been linked to neurodegeneration through the impairment of pro-survival proteins by S-nitrosylation.

RESULTS: In the present study, we used two-dimensional gel electrophoresis in conjunction with the modified biotin switch assay for protein S-nitrosothiols using resin-assisted capture (SNO-RAC) to identify proteins that are S-nitrosylated more intensively in neuroblastoma cells treated with a mitochondrial complex I inhibitor, 1-methyl-4-phenylpyridinium (MPP+). We identified 14 proteins for which S-nitrosylation was upregulated and seven proteins for which it was downregulated in MPP+-treated neuroblastoma cells. Immunoblot analysis following SNO-RAC confirmed a large increase in the S-nitrosylation of esterase D (ESD), serine-threonine kinase receptor-associated protein (STRAP) and T-complex protein 1 subunit γ (TCP-1 γ) in MPP+-treated neuroblastoma cells, whereas S-nitrosylation of thioredoxin domain-containing protein 5 precursor (ERp46) was decreased.

CONCLUSIONS: These results suggest that S-nitrosylation resulting from mitochondrial dysfunction can compromise neuronal survival through altering multiple signal transduction pathways and might be a potential therapeutic target for neurodegenerative diseases.

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