Hydropersulfides (RSSH) and Nitric Oxide (NO) Signaling: Possible Effects on S-Nitrosothiols (RS-NO)

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/role...

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Bibliographic Details
Published in:Antioxidants 2022-01, Vol.11 (1), p.169
Main Authors: Fukuto, Jon M, Perez-Ternero, Cristina, Zarenkiewicz, Jessica, Lin, Joseph, Hobbs, Adrian J, Toscano, John P
Format: Article
Language:English
Subjects:
Etiology
hydropersulfide
Kinases
Nitric oxide
nitroxyl
perthiyl radical
Phosphatase
Phosphorylation
Physiology
Proteins
Review
S-nitrosothiol
Smooth muscle
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Summary: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.
ISSN:2076-3921
2076-3921
DOI:10.3390/antiox11010169