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Intracellular Glutathione Mediates the Denitrosylation of Protein Nitrosothiols in the Rat Spinal Cord by Jorge M. Romero; Oscar A. Bizzozero is a Neuroscience article available to read on EtoBox.

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## Abstract Protein S‐nitrosothiols (PrSNOs) have been implicated in the pathophysiology of neuroinflammatory and neurodegenerative disorders. Although the metabolically instability of PrSNOs is well known, there is little understanding of the factors involved in the cleavage of S‐NO linkage in intact cells. To address this issue, we conducted chase experiments in spinal cord slices incubated with S‐nitrosoglutathione (GSNO). The results show that removal of GSNO leads to a rapid disappearance of PrSNOs (__t__~1⁄2~ ∼ 2 hr), which is greatly accelerated when glutathione (GSH) levels are raised with the permeable analogue GSH ethyl ester. Moreover, PrSNOs are stable in the presence of the GSH depletor diethyl maleate, indicating that GSH is critical for protein denitrosylation. Inhibition of GSH‐dependent enzymes (glutathione S‐transferase, glutathione peroxidase, and glutaredoxin) and enzymes that could mediate denitrosylation (alcohol dehydrogense‐III, thioredoxin and protein disulfide isomerase) do not alter the rate of PrSNO decomposition. These findings and the lack of protein glutathionylation during the chase indicate that most proteins are denitrosylated via rapid transnitros

Who reads Intracellular Glutathione Mediates the Denitrosylation of Protein Nitrosothiols in the Rat Spinal Cord?

Author

Jorge M. Romero; Oscar A. Bizzozero

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0360-4012)

Published

2008

Language

EN

Field

Neuroscience (Life Sciences)