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Identification of Functional Protein Regions Through Chimeric Protein Construction
Published on: January 8, 2019
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Protein nitrotryptophan: formation, significance and identification
Tal Nuriel1, Alex Hansler, Steven S Gross
1Department of Pharmacology, Weill Cornell Medical College, 1300 York Ave, New York, NY 10065, USA.
Journal of Proteomics
|June 18, 2011
Summary
Reactive nitrogen species can alter proteins. This review focuses on nitrotryptophan (NO(2)-Trp) formation and its role in nitrosative stress, suggesting it contributes to cell dysregulation.
Area of Science:
- Biochemistry
- Molecular Biology
- Pathophysiology
Background:
- Reactive nitrogen species (RNS) are implicated in various disease states.
- Protein modification by RNS, particularly tyrosine nitration to 3-nitrotyrosine, is well-studied.
- Emerging evidence highlights tryptophan nitration, forming nitrotryptophan (NO(2)-Trp), as a significant modification in nitrosative stress.
Purpose of the Study:
- To provide an in-depth review of nitrotryptophan (NO(2)-Trp).
- To summarize current research on NO(2)-Trp formation, prevalence, and biological significance.
- To discuss methods for identifying NO(2)-Trp-modified proteins.
Main Methods:
- Literature review of existing research on NO(2)-Trp.
- Analysis of studies detailing the formation pathways of NO(2)-Trp.
- Examination of methodologies used for detecting NO(2)-Trp in proteins.
Main Results:
- Nitrotryptophan (NO(2)-Trp) is formed through the action of reactive nitrogen species.
- NO(2)-Trp modification occurs in various disease states and potentially physiological processes.
- Specific methods exist for the identification of NO(2)-Trp-modified proteins.
Conclusions:
- Nitrotryptophan (NO(2)-Trp) is an important marker and mediator of nitrosative stress.
- NO(2)-Trp modification contributes to cellular dysregulation during disease.
- Further research is needed to fully elucidate the biological roles of NO(2)-Trp.
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