ArticleChemico-biological interactions2009
Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation.
Article in Chemico-biological interactions, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Carboxyl Amidation of Chlorogenic Acid Improves Anti-Inflammatory Activity and Biosafety via Potent AKR1B1 Inhibition in LPS-Induced Macrophages.Molecules (Basel, Switzerland) · 2026Article
- A Potential Prognostic Biomarker for Glioma: Aldo-Keto Reductase Family 1 Member B1.Computational intelligence and neuroscience · 2022Article
- Article
- Efficacy of aldose reductase inhibitors is affected by oxidative stress induced under X-ray irradiation.Scientific reports · 2019Article
- ROLE OF THIOLS IN OXIDATIVE STRESS.Current opinion in toxicology · 2018Article
- Loss of Glyoxalase 1 Induces Compensatory Mechanism to Achieve Dicarbonyl Detoxification in Mammalian Schwann Cells.The Journal of biological chemistry · 2017Article
- Uremic Toxicity of Advanced Glycation End Products in CKD.Journal of the American Society of Nephrology : JASN · 2016Review
- S-nitrosylation: specificity, occupancy, and interaction with other post-translational modifications.Antioxidants & redox signaling · 2013Review
- S-nitrosothiols and the S-nitrosoproteome of the cardiovascular system.Antioxidants & redox signaling · 2013Review
- Protein S-glutathiolation: redox-sensitive regulation of protein function.Journal of molecular and cellular cardiology · 2012Review
- Regulation by S-nitrosylation of protein post-translational modification.The Journal of biological chemistry · 2012Review
- Osmolarity and glucose differentially regulate aldose reductase activity in cultured mouse podocytes.Experimental diabetes research · 2011Article
- Protein S-nitrosylation and cardioprotection.Circulation research · 2010Review
- Measurement and identification of S-glutathiolated proteins.Methods in enzymology · 2010Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Nitric oxide (NO) is an important regulator of the catalytic activity of aldose reductase (AR). It reacts with the active site cysteines of AR and this reaction results in the formation of several kinetically distinct forms of the protein. The catalytic activity of AR is increased in the ischemic heart and this increase in activity is associated with NO-dependent modification of AR. During reperfusion, the enzyme reverts back to its un-activated form. Although, AR activation has been linked to thiol oxidation, the mechanisms of de-activation remain unclear. Here we report that treatment of recombinant human AR (AKR1B1) by a non-thiol-based NO-donor (DEANO) results in activation and S-nitrosylation of the protein. The nitrosylated (ARSNO), but not the reduced (ARSH), protein reacted with reduced glutathione (GSH) and this reaction resulted in the formation of glutathiolated AR (ARSSG). The modification of AR by NO was site-specific at Cys-298 and was not affected by selective mutation of the neighboring residue, Cys-303 to an alanine. Incubation of the glutathiolated AR (ARSSG) with GSH resulted in the regeneration of the reduced form of the protein (ARSH). Treatment of nitrosylated AR (ARSNO) with ascorbic acid also led to the conversion of the protein to its reduced form. These observations suggest that intracellular reductants such as GSH and ascorbate could convert the nitrosylated form of AR to its basal or reduced state. In general, such reductive reactions might represent a common mechanism for denitrosylating proteins or an "off" switch in NO-mediated signaling pathways involving protein S-nitrosylation reactions.
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