The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy
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Authors
Barnett, Scott D.
Buxton, Iain L. O.
Issue Date
2017
Type
Article
Language
Keywords
S-nitrosoglutathione , S-nitrosoglutathione reductase , alcohol dehydrogenase , nitric oxide , S-nitrosation , ADH5
Alternative Title
Abstract
S-nitrosoglutathione reductase (GSNOR), or ADH5, is an enzyme in the alcohol dehydrogenase (ADH) family. It is unique when compared to other ADH enzymes in that primary short-chain alcohols are not its principle substrate. GSNOR metabolizes S-nitrosoglutathione (GSNO), S-hydroxymethylglutathione (the spontaneous adduct of formaldehyde and glutathione), and some alcohols. GSNOR modulates reactive nitric oxide (center dot NO) availability in the cell by catalyzing the breakdown of GSNO, and indirectly regulates S-nitrosothiols (RSNOs) through GSNO-mediated protein S-nitrosation. The dysregulation of GSNOR can significantly alter cellular homeostasis, leading to disease. GSNOR plays an important regulatory role in smooth muscle relaxation, immune function, inflammation, neuronal development and cancer progression, among many other processes. In recent years, the therapeutic inhibition of GSNOR has been investigated to treat asthma, cystic fibrosis and interstitial lung disease (ILD). The direct action of center dot NO on cellular pathways, as well as the important regulatory role of protein S-nitrosation, is closely tied to GSNOR regulation and defines this enzyme as an important therapeutic target.
Description
Citation
Barnett, S. D., & Buxton, I. L. O. (2017). The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy. Critical Reviews in Biochemistry and Molecular Biology, 52(3), 340�"354. doi:10.1080/10409238.2017.1304353
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License
Creative Commons Attribution 4.0 International
Journal
Volume
Issue
PubMed ID
ISSN
1040-9238