Protein glutathiolation by nitric oxide: An intracellular mechanism regulating redox protein modification
Abstract
This study was designed to examine whether NO regulates protein glutathiolation. Exposure to NO donors increased protein glutathiolation in COS-7 or rat aortic smooth muscle cells as detected by anti-protein glutathione (GSH) antibodies. This process was reversible and saturable. Stimulation with acetylcholine (ACh) increased protein glutathiolation in isolated rat aortic rings. This was prevented by inhibiting endothelial NO synthase (eNOS). In ACh-treated rings, proteins showing positive immunoreactivity with the anti-PSSG antibody (Ab) were identified by matrix assisted laser desorption-time-of-flight mass spectrometry to be actin, vimentin, and heat shock protein 70. Purified actin was more readily glutathiolated by S-nitrosoglutathione than by oxidized GSH as determined by electrospray-ionization mass spectrometry, and nitrosylated actin was glutathiolated by reduced GSH. Relative to wild-type (WT) mice, increased protein glutathiolation was observed in hearts of mice with cardiac-specific expression of inducible NO synthase (iNOS). Proteins immunoprecipitated from transgenic hearts revealed GSH-adducted peptides corresponding to adenine nucleotide translocator and the alpha-subunit of F1F0ATPase. These data suggest that exogenous NO or NO generated by eNOS or iNOS regulates protein adduction with GSH. This could be due to a direct reaction of proteins with S-nitrosoglutathione or denitrosylation of S-nitrosylated proteins by reduced GSH. Glutathiolation of cytoskeletal…
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S-nitrosylation is associated with activation of transcription factors, regulation of signal transduction molecules, redox protein modification, mitochondrial functions, and cell apoptosis.
“S-nitrosylation is associated with the activation of transcription factors, the regulation of a number of signal transduction molecules [10] and redox protein modification [11], mitochondrial functions [12,13], and cell apoptosis [14]”
From NO-Rich Diet for Lifestyle-Related Diseases (2015) · cites this paper as [11]
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References 72 · Cited by 116
- Authors
- West, M. B., Hill, B. G., Xuan, Y.-T., Bhatnagar, A., West, M. B., Hill, B. G., Xuan, Y.-T., & Bhatnagar, A.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2006-06-29
- Volume
- 20
- Issue
- 10
- Pages
- 1715-1717
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2120259837
- Cited by
- 116
- References
- 72
- Citations by year
- 2024: 1 · 2023: 6 · 2022: 4 · 2021: 3 · 2020: 3 · 2019: 1 · 2018: 3 · 2017: 3 · 2016: 4 · 2015: 6 · 2014: 7 · 2013: 9 · 2012: 8
- FWCI
- 5.31
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (HL-59378, ES-11860)
- American Heart Association (HL-65660)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- nitric oxide, S-nitrosoglutathione, denitrosylation, endothelial nitric oxide synthase, inducible nitric oxide synthase, actin, vimentin, HSP70, cytoskeletal proteins, mitochondrial proteins, adenine nucleotide translocase, F1F0-ATPase, acetylcholine, aortic smooth muscle cells
- MeSH terms
- Acetylcholine, Animals, Aorta, Chlorocebus aethiops, Glutathione, Myocardium, Nitric Oxide, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins, COS Cells, Nitric Oxide Donors, Myocytes, Smooth Muscle, Mice, Rats, Nitric Oxide Synthase Type II, Nitric Oxide Synthase Type III, In Vitro Techniques
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