Protein S-nitrosylation and denitrosylation in the mouse spinal cord upon injury of the sciatic nerve
Autor: | Ilka Wittig, Ulrich Brandt, Reynir Scheving, Irmgard Tegeder, Heinrich Heide, Mirco Steger, Boris Albuquerque |
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Rok vydání: | 2012 |
Předmět: |
Proteomics
Protein Disulfide-Isomerases Biophysics Biochemistry Glutathione Synthase Nitric oxide Two-Dimensional Difference Gel Electrophoresis Mice chemistry.chemical_compound medicine Animals Protein disulfide-isomerase Aconitate Hydratase S-Nitrosothiols biology Mitochondrial medicine Energy and redox metabolism [IGMD 8] S-Nitrosylation Anatomy Sciatic nerve injury Nerve injury medicine.disease Sciatic Nerve Cell biology Nitric oxide synthase Mitochondrial medicine [IGMD 8] NG-Nitroarginine Methyl Ester Spinal Cord chemistry biology.protein Synaptic signaling Sciatic nerve Nitric Oxide Synthase medicine.symptom Oxidation-Reduction Peroxiredoxin VI Signal Transduction |
Zdroj: | Journal of Proteomics, 75, 3987-4004 Journal of Proteomics, 75, 13, pp. 3987-4004 |
ISSN: | 1874-3919 |
DOI: | 10.1016/j.jprot.2012.05.006 |
Popis: | Contains fulltext : 109217.pdf (Publisher’s version ) (Closed access) Nitric oxide is a pain signaling molecule and exerts its influence through two primary pathways: by stimulation of soluble guanylylcyclase and by direct S-nitrosylation (SNO) of target proteins. We assessed in the spinal cord the SNO-proteome with two methods, two-dimensional S-nitrosothiol difference gel electrophoresis (2D SNO-DIGE) and SNO-site identification (SNOSID) at baseline and 24h after sciatic nerve injury with/without pretreatment with the nitric oxide synthase inhibitor L-NG-nitroarginine methyl ester (L-NAME). After nerve injury, SNO-DIGE revealed 30 proteins with increased and 23 proteins with decreased S-nitrosylation. SNO-sites were identified for 17 proteins. After sham surgery only 3 proteins were up-nitrosylated. L-NAME pretreatment substantially reduced both constitutive and nerve injury evoked up-S-nitrosylation. For the top candidates S-nitrosylation was confirmed with the biotin switch technique and time course analyses at 1 and 7days showed that SNO modifications of protein disulfide isomerase, glutathione synthase and peroxiredoxin-6 had returned to baseline within 7days whereas S-nitrosylation of mitochondrial aconitase 2 was further increased. The identified SNO modified proteins are involved in mitochondrial function, protein folding and transport, synaptic signaling and redox control. The data show that nitric oxide mediated S-nitrosylation contributes to the nerve injury-evoked pathology in nociceptive signaling pathways. |
Databáze: | OpenAIRE |
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