INTRACELLULAR GLUTATHIONE MEDIATES THE DENITROSYLATION OF PROTEIN NITROSOTHIOLS IN THE RAT SPINAL CORD

JORGE M. ROMERO; OSCAR A. BIZZOZERO

Wiley Interscience

Lugar: New York; Año: 2009 vol. 87 p. 701 - 701

font face="Helvetica"> 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 Snitrosoglutathione (GSNO). The results show that removal of GSNO leads to a rapid disappearance of PrSNOs (t1/2 ~ 2h), 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,