期刊
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
卷 52, 期 3, 页码 340-354出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/10409238.2017.1304353
关键词
S-nitrosoglutathione; S-nitrosoglutathione reductase; alcoholdehydrogenase; nitric oxide; S-nitrosation; ADH5
资金
- Bill and Melinda Gates Foundation
- National Institute of General Medical Sciences [U54 GM104944]
- Mick Hitchcock Scholars Program
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.
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