Tracing the Path of Inhaled Nitric Oxide: Biological Consequences of
Protein Nitrosylation
Abstract
Nitric oxide (NO) is a comprehensive regulator of vascular and airway
tone. Endogenous NO produced by nitric oxide synthases regulates
multiple signaling cascades, including activation of soluble guanylate
cyclase to generate cGMP, relaxing smooth muscle cells. Inhaled NO is an
established therapy for pulmonary hypertension, especially in neonates,
and has been recently proposed for treatment of hypoxic respiratory
failure and acute respiratory distress syndrome due to COVID-19. In this
review, we summarize the effects of endogenous and exogenous NO on
protein S-nitrosylation, which is the selective and reversible covalent
attachment of a nitrogen monoxide group to the thiol side chain of
cysteine. This post-translational modification targets specific
cysteines based on the acid/base sequence of surrounding residues, with
significant impacts on protein interactions and function. S-nitrosothiol
(SNO) formation is tightly compartmentalized and enzymatically
controlled, but also propagated by non-enzymatic transnitrosylation of
downstream protein targets. Redox-based nitrosylation and
denitrosylation pathways dynamically regulate the equilibrium of
SNO-proteins. We review the physiological roles of SNO proteins,
including nitrosohemoglobin and autoregulation of blood flow through
hypoxic vasodilation, and pathological effects of nitrosylation
including inhibition of critical vasodilator enzymes; and discuss the
intersection of NO source and dose with redox environment, in
determining the effects of protein nitrosylation.