Free Content Extracellular S-nitrosoglutathione, but not S-nitrosocysteine or N2O3, mediates protein S-nitrosation in rat spinal cord slices

You have access to the full text article on a website external to ingentaconnect.

Please click here to view this article on Wiley Online Library.

You may be required to register and activate access on Wiley Online Library before you can obtain the full text. If you have any queries please visit Wiley Online Library

Download Article:

Abstract:

Summary

There is evidence that protein S-nitrosothiols (PrSNOs) accumulate in inflammatory demyelinating disorders like multiple sclerosis and experimental allergic encephalomyelitis. However, very little is known regarding the mechanism by which PrSNOs are formed in target cells. The present study compares the ability of potential intercellular mediators of nitrosative damage including S-nitrosoglutathione (GSNO), S-nitrosocysteine and N2O3 to induce protein S-nitros(yl)ation in the spinal cord, a CNS region that is commonly affected in multiple sclerosis and experimental allergic encephalomyelitis. The results clearly demonstrate that while all three NO-donors cause S-nitrosation of proteins in cell-free systems, only GSNO is a viable S-nitrosating agent in rat spinal cord slices. Generation of PrSNOs with GSNO occurs by S-transnitrosation as the process was not inhibited by either the NO-scavenger rutin or the N2O3-scavenger azide. Contrary to other cell types, nerve cells incorporate intact GSNO and neither functionall-amino acid transporters nor cell-surface thiols are required. We also found that there is a restricted number of proteins available for S-nitrosation, even at high, non-physiological concentrations of GSNO. These proteins are highly concentrated in mitochondria and mitochondria-rich subcellular compartments. This study is relevant to those CNS disorders characterized by excessive nitric oxide production.

Keywords: S-nitrosoglutathione; multiple sclerosis; nitric oxide; nitrosative stress; protein nitrosothiol

Document Type: Research Article

DOI: http://dx.doi.org/10.1111/j.1471-4159.2006.04180.x

Publication date: November 1, 2006

Related content

Tools

Favourites

Share Content

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
X
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more