Extra-platelet low-molecular-mass thiols mediate the inhibitory action of S-nitrosoalbumin on human platelet aggregation via S-transnitrosylation of the platelet surface.

ABSTRACT: Nitrosylation of sulfhydryl (SH) groups of cysteine (Cys) moieties is an important post-translational modification (PTM), often on a par with phosphorylation. S-Nitrosoalbumin (ALB-Cys³⁴SNO; SNALB) in plasma and S-nitrosohemoglobin (Hb-Cys^β93SNO; HbSNO) in red blood cells are considered the most abundant high-molecular-mass pools of nitric oxide (NO) bioactivity in the human circulation. SNALB per se is not an NO donor. Yet, it acts as a vasodilator and an inhibitor of platelet aggregation. SNALB can be formed by nitrosation of the sole reduced Cys group of albumin (Cys³⁴) by nitrosating species such as nitrous acid (HONO) and nitrous anhydride (N₂O₃), two unstable intermediates of NO autoxidation. SNALB can also be formed by the trans

SUBMITTER: Tsikas D 

PROVIDER: S-EPMC8107154 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature