AI Article Synopsis
- S-Nitrosothiol formation in proteins and peptides is linked to various diseases and may regulate protein functions, as well as potentially serve as a storage form for nitric oxide (NO).
- Despite their importance, there is a lack of clarity regarding how RS-NO is formed and degraded in the body.
- The recently discovered hydropersulfides (RSSH) interact with RS-NO, leading to its degradation and the release of NO, suggesting RSSH could play a critical role in regulating RS-NO levels and its related physiological functions.
Article Abstract
S-Nitrosothiol (RS-NO) formation in proteins and peptides have been implicated as factors in the etiology of many diseases and as possible regulators of thiol protein function. They have also been proposed as possible storage forms of nitric oxide (NO). However, despite their proposed functions/roles, there appears to be little consensus regarding the physiological mechanisms of RS-NO formation and degradation. Hydropersulfides (RSSH) have recently been discovered as endogenously generated species with unique reactivity. One important reaction of RSSH is with RS-NO, which leads to the degradation of RS-NO as well as the release of NO. Thus, it can be speculated that RSSH can be a factor in the regulation of steady-state RS-NO levels, and therefore may be important in RS-NO (patho)physiology. Moreover, RSSH-mediated NO release from RS-NO may be a possible mechanism allowing RS-NO to serve as a storage form of NO.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8773330 | PMC |
| http://dx.doi.org/10.3390/antiox11010169 | DOI Listing |
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