Identification of major S-nitrosylated proteins in murine experimental autoimmune encephalomyelitis.
Identification of major S-nitrosylated proteins in murine experimental autoimmune encephalomyelitis.
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DOI：
10.1002/jnr.22113
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发表时间：
2009-10
影响因子：
4.2
通讯作者：
Zheng, Jianzheng
中科院分区：
文献类型：
--
作者：
Bizzozero, Oscar A.;Zheng, Jianzheng
Nitrosative stress has been implicated in the pathophysiology of several CNS disorders including multiple sclerosis (MS) and its animal model experimental autoimmune encephalomyelitis (EAE). We have recently shown that protein nitrosothiols (PrSNOs) accumulate in the brain of MS patients and there is indirect evidence that PrSNO levels are also increased in EAE. In this study we sought to identify the major PrSNOs in the spinal cord of EAE animals prepared by active immunization of C57/BL6 mice with MOG35-55 peptide. For this purpose, PrSNOs from control and EAE mice at various disease stages were derivatized with HPDP-biotin, and the biotinylated proteins were isolated with streptavidin-agarose. Proteins from total and streptavidin-bound fractions were then analyzed by western blotting using antibodies against the major S-nitrosylated substrates of CNS tissue. Using this approach we found that the proportion of S-nitrosylated neurofilament proteins, NMDA receptors, α/β-tubulin, β-actin and GAPDH is increased in EAE. Other potential substrates were either not S-nitrosylated in vivo (HCN3, HSP-72, CRMP-2, γ-actin, calbindin) or their S-nitrosylation levels were unaltered in EAE (Na/K ATPase, hexokinase, glycogen phosphorylase). We also discovered that neuronal specific enolase is the major S-nitrosylated protein in acute EAE. Given that S-nitrosylation affects protein function it is likely that the observed changes are significant to the pathophysiology of inflammatory demyelination.
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