Protein S-nitrosylation in health and disease: a current perspective

By M. W. Foster, D. Hess, J. Stamler. Trends in Molecular Medicine, 2009

730 citations recorded by the source corpus.

Summary Protein S-nitrosylation conveys a large part of the ubiquitous influence of nitric oxide on cellular signal transduction, and accumulating evidence indicates important roles for S-nitrosylation both in normal physiology and in a broad spectrum of human diseases. Here we review recent findings that implicate S-nitrosylation in cardiovascular, pulmonary, musculoskeletal and neurological (dys)function, as well as in cancer. The emerging picture shows that, in many cases, pathophysiology correlates with hypo- or hyper-S-nitrosylation of specific protein targets, rather than a general cellular insult due to loss of or enhanced nitric oxide synthase activity. In addition, it is increasingly evident that dysregulated S-nitrosylation can result not only from alterations in the expression, compartmentalization and/or activity of nitric oxide synthases but can also reflect a contribution from denitrosylases, including prominently the S-nitrosoglutathione (GSNO)-metabolizing enzyme, GSNO reductase. Finally, because exogenous mediators of protein S-nitrosylation or denitrosylation can substantially affect the development or progression of disease, potential therapeutic agents that modulate S-nitrosylation could well have broad clinical utility.

Subfields: Cardiology and Cardiovascular Medicine, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/b0a43f1ab661ac9164db5b72064ef18be7083f43

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Citations in the corpus

• Cellular Stress Responses, The Hormesis Paradigm, and Vitagenes: Novel Targets for Therapeutic Intervention in Neurodegenerative Disorders (2010, neutral): “However, oxidative modification in protein structure and function may occur when reactive nitrogen species reach a critical threshold, and hence nitrosative stress may ensue (179).”
• Ischemia/Reperfusion (2016, neutral): “activation is triggered by release of subcellular membrane consistuents secondary to cell necrosis (127, 248, 461, 672).”
• iSNO-PseAAC: Predict Cysteine S-Nitrosylation Sites in Proteins by Incorporating Position Specific Amino Acid Propensity into Pseudo Amino Acid Composition (2013, background): “Meanwhile, increasing evidences have indicated that SNO also plays an important role in various major diseases [5], such as cancer [6], Parkinson’s [7,8], Alzheimer’s [9], and Amyotrophic Lateral Sclerosis (ALS) [10].”
• The roles of conditional disorder in redox proteins (2013, background): “These modifications provide the proteome with enormous diversity, flexibility, and the ability to rapidly adjust cellular functions to changes in environment and metabolic state [1–3].”
• Redox chemistry of biological thiols (2010, background): “Its cell regulatory role is mainly attributed to its interaction with guanylate cyclase but its reactions with protein thiols to form, among others, nitrosothiol intermediate species are increasingly recognized as major contributors to its signaling function [187].”