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Citation
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HERO ID
1544840
Reference Type
Journal Article
Title
Is S-nitrosocysteine a true surrogate for nitric oxide?
Author(s)
Hickok, JR; Vasudevan, D; Thatcher, GR; Thomas, DD
Year
2012
Is Peer Reviewed?
Yes
Journal
Antioxidants & Redox Signaling
ISSN:
1523-0864
EISSN:
1557-7716
Volume
17
Issue
7
Page Numbers
962-968
Language
English
PMID
22304688
DOI
10.1089/ars.2012.4543
Web of Science Id
WOS:000307231600005
Abstract
S-Nitrosothiol (RSNO) formation is one manner by which nitric oxide (•NO) exerts its biological effects. There are several proposed mechanisms of formation of RSNO in vivo: auto-oxidation of •NO, transnitrosation, oxidative nitrosylation, and from dinitrosyliron complexes (DNIC). Both free •NO, generated by •NO donors, and S-nitrosocysteine (CysNO) are widely used to study •NO biology and signaling, including protein S-nitrosation. It is assumed that the cellular effects of both compounds are analogous and indicative of in vivo •NO biology. A quantitative comparison was made of formation of DNIC and RSNO, the major •NO-derived cellular products. In RAW 264.7 cells, both •NO and CysNO were metabolized, leading to rapid intracellular RSNO and DNIC formation. DNIC were the dominant products formed from physiologic •NO concentrations, however, and RSNO were the major product from CysNO treatment. Chelatable iron was necessary for DNIC assembly from either •NO or CysNO, but not for RSNO formation. These profound differences in RSNO and DNIC formation from •NO and CysNO question the use of CysNO as a surrogate for physiologic •NO. Researchers designing experiments intended to elucidate the biological signaling mechanisms of •NO should be aware of these differences and should consider the biological relevance of the use of exogenous CysNO.
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