Abstract：
: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.
journal_name
J Proteomicsjournal_title
Journal of proteomicsauthors
Scheving R,Wittig I,Heide H,Albuquerque B,Steger M,Brandt U,Tegeder Idoi
10.1016/j.jprot.2012.05.006subject
Has Abstractpub_date
2012-07-16 00:00:00pages
3987-4004issue
13eissn
1874-3919issn
1876-7737pii
S1874-3919(12)00294-1journal_volume
75pub_type
杂志文章abstract：:Dendritic cells (DCs) can shape the immune system towards an inflammatory or tolerant state depending on the bacterial antigens and the environment they encounter. In this study we provide a proteomic catalogue of differentially expressed proteins between distinct DC maturation states, brought about by bacteria that d...
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journal_title：Journal of proteomics
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journal_title：Journal of proteomics
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pub_type： 历史文章,杂志文章
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doi：10.1016/j.jprot.2012.06.016
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journal_title：Journal of proteomics
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journal_title：Journal of proteomics
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journal_title：Journal of proteomics
pub_type： 杂志文章,评审
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abstract：:One of the important challenges for MALDI imaging mass spectrometry (MALDI-IMS) is the unambiguous identification of measured analytes. One way to do this is to match tryptic peptide MALDI-IMS m/z values with LC-MS/MS identified m/z values. Matching using current MALDI-TOF/TOF MS instruments is difficult due to the va...
journal_title：Journal of proteomics
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