Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 109, Issue -, Pages 156-166Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2017.02.013
Keywords
S-nitrosylation; S-nitrosation; Thiol; Nitric oxide; Cysteine; Redox
Funding
- British Heart Foundation
- European Research Council (ERC)
- Medical Research Council
- Department of Health via the NIHR cBRC
- MRC [G1000458, G0600785, G0700320, MR/L009684/1, MR/K003232/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/C503646/1] Funding Source: researchfish
- British Heart Foundation [FS/11/45/28859, PG/13/13/30018, PG/15/26/31373, RG/12/12/29872, PG/10/98/28655] Funding Source: researchfish
- Medical Research Council [MR/L009684/1, MR/K003232/1, G0700320, G0600785, 998501, G1000458] Funding Source: researchfish
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Over the last 25 years protein S-nitrosylation, also known more correctly as S-nitrosation, has been progressively implicated in virtually every nitric oxide-regulated process within the cardiovascular system. The current, widely-held paradigm is that S-nitrosylation plays an equivalent role as phosphorylation, providing a stable and controllable post-translational modification that directly regulates end-effector target proteins to elicit biological responses. However, this concept largely ignores the intrinsic instability of the nitrosothiol bond, which rapidly reacts with typically abundant thiol-containing molecules to generate more stable disulfide bonds. These protein disulfides, formed via a nitrosothiol intermediate redox state, are rationally anticipated to be the predominant end-effector modification that mediates functional alterations when cells encounter nitrosative stimuli. In this review we present evidence and explain our reasoning for arriving at this conclusion that may be controversial to some researchers in the field.
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