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Further study on S-nitrosation by nitrite
Wu-Nan Kuo1, Joseph M Kocis, Marvin J Robinson
1Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114, USA. kuow@cookman.edu
Frontiers in Bioscience : a Journal and Virtual Library
|April 18, 2003
Summary
S-nitrosoglutathione forms at neutral pH and degrades with L-cysteine or CoA-SH. Nitrite nitrosolates rat brain proteins and generates reactive species with IgG, producing gas bubbles.
Area of Science:
- Biochemistry
- Chemical Biology
- Neuroscience
Background:
- S-nitrosoglutathione (GSNO) is a key signaling molecule.
- Understanding GSNO formation and degradation is crucial for biological processes.
- Nitrite is a precursor to reactive nitrogen species.
Purpose of the Study:
- To investigate the formation and degradation of S-nitrosoglutathione.
- To explore the nitrosation of proteins by nitrite in biological systems.
- To examine the reactivity of nitrite with immune proteins.
Main Methods:
- Chemical synthesis of S-nitrosoglutathione.
- Enzymatic assays for GSNO degradation.
- Western blot analysis of nitrosated proteins.
- Incubation of nitrite with immunoglobulin G (IgG).
Main Results:
- S-nitrosoglutathione formed from reduced glutathione and sodium nitrite at neutral pH.
- L-cysteine and CoA-SH catalyzed the degradation of S-nitrosoglutathione.
- A large molecular mass protein from rat brain extract was nitrosated by nitrite and cleaved.
- Incubation of nitrite with IgG generated reactive nitrogen/oxygen species and gas bubbles.
Conclusions:
- GSNO formation and degradation pathways are influenced by biological thiols.
- Nitrite can nitrosate and modify proteins in biological extracts.
- Nitrite's interaction with IgG can lead to the generation of reactive species.