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The Role of Nitric Oxide Signaling in the Pathogenesis of Necrotizing Enterocolitis
Published in David J. Hackam, Necrotizing Enterocolitis, 2021
Anatoly Grishin, Patrick T. Delaplain, Jin Wang, Michael Mallicote, Michelle Nguyen, Michael Philippe-Auguste, Christopher P. Gayer, Henri R. Ford
S-nitrosylation and nitration: NO reacts non-enzymatically with thiol groups of cysteine to form S-nitrosothiols. Peroxynitrite, a reactive intermediate of NO oxidation, converts tyrosine residues in proteins into nitrotyrosines. These modifications may alter the activity of target proteins. Relatively high concentrations of NO are required for the physiological effects of S-nitrosylation and nitration, consistent with the involvement of iNOS. Signaling mediators whose activity is regulated by S-nitrolylation and nitration can be regarded as physiologic sensors of high levels of NO (17). Elevated S-nitrosylation is associated with experimental NEC (36).
Therapeutic Gases for Neurological Disorders
Published in Sahab Uddin, Rashid Mamunur, Advances in Neuropharmacology, 2020
R. Rachana, Tanya Gupta, Saumya Yadav, Manisha Singh
S-nitrosylation is an essential posttranslational protein modification (Sun et al., 2006). It was demonstrated by experimental evidences that the process of S-nitrosylation of the proteins forms regulates the effects of NO on the functions of the cells and various S-nitrosylated proteins (SNO proteins) were identified recently and studies have shown that hypo-S-nitrosylation or hyper-S-nitrosylation of specific proteins resulting in protein function alterations are directly connected to the causes and the symptoms of a number of diseases, mainly including nervous system disorders (Foster et al., 2009). Under oxidative stress, the process of S-nitrosylation of protein thiols occurs and prevents the cells from more oxidative damage by increased level of ROS and RNS. These reactive species induce stress-signaling pathways engaged in dysfunction of mitochondria, overload of intra-cellular Ca2+, heart failure, necrosis, and apoptosis (Sun et al., 2006).
Current and future CFTR therapeutics
Published in Anthony J. Hickey, Heidi M. Mansour, Inhalation Aerosols, 2019
Marne C. Hagemeijer, Gimano D. Amatngalim, Jeffrey M. Beekman
The proteostasis network includes cellular pathways that together maintain protein homeostasis by regulating protein synthesis, folding, trafficking, and degrading, and as such it is an attractive target for the development of therapeutic approaches (125). S-nitrosation (or S-nitrosylation) is a cellular post-translational modification by which nitric oxide (NO) is transferred to a protein thiol group and thereby regulates NO-mediated signaling pathways. The S-nitrosoglutathione reductase (GSNOR) alcohol dehydrogenase (ADH) enzyme is responsible for metabolizing S-nitrosoglutathione (GSNO), which is the main source of nitric oxide in cells, and as such regulates NO levels for protein S-nitrosation (126).
S-Nitrosoglutathione formation at gastric pH is augmented by ascorbic acid and by the antioxidant vitamin complex, Resiston
Published in Pharmaceutical Biology, 2018
Vitali I. Stsiapura, Ilya Bederman, Ivan I. Stepuro, Tatiana S. Morozkina, Stephen J. Lewis, Laura Smith, Benjamin Gaston, Nadzeya Marozkina
Protein S-nitrosylation, the post-translational modification of a cysteine thiol by a nitric oxide (NO) group, is involved in a broad spectrum of cell signalling effects (Gow et al. 2002; Gaston, Singel, et al. 2006; Paige et al. 2008; Foster et al. 2009). In general, proteins and peptides that have been modified to form S-nitrosothiol bonds are involved in guanylate cyclase (GC)-independent signalling by nitrogen oxides, though S-nitrosylation also affects GC-dependent processes (Mayer et al. 1998). Disorders of S-nitrosylation are relevant to the pathophysiology of many diseases, such as cystic fibrosis, asthma, primary ciliary dyskinesia, sleep apnoea, Duchenne muscular dystrophy, etc. (Gow et al. 2002; Moya et al. 2002; Snyder et al. 2002; Gaston, Singel, et al. 2006; Colussi et al. 2008; Lim et al. 2008; Ozawa et al. 2008; Paige et al. 2008; Foster et al. 2009; Gonzalez et al. 2009; Marozkina and Gaston 2012; Marozkina et al. 2012). S-Nitrosothiols can be formed by NO synthase (NOS), by other metalloproteins, and by inorganic reactions (Mayer et al. 1998; Gow et al. 2002; Gaston, Singel, et al. 2006; Paige et al. 2008; Foster et al. 2009), but NOS knockout mice are viable (Huang 2000), suggesting that exogenous nitrogen oxides can be converted to bioavailable, physiologically sufficient nitrogen oxides. Here, we have identified a reaction in the gastric mucosa that can lead to increased formation of the endogenous, clinically beneficial S-nitrosothiol, S-nitrosoglutathione (GSNO), in vivo. Surprisingly, this reaction is augmented, not inhibited, by ascorbic acid (AA) at gastric pH.
Regulation of cytochrome P450 enzyme activity and expression by nitric oxide in the context of inflammatory disease
Published in Drug Metabolism Reviews, 2020
Edward T. Morgan, Cene Skubic, Choon-myung Lee, Kaja Blagotinšek Cokan, Damjana Rozman
Hundreds of S-nitrosated or potentially nitrosated cellular proteins have been identified via proteomic studies (Jaffrey et al. 2001; Miersch and Mutus 2005; Lee YI et al. 2014; Ibáñez-Vea et al. 2018). S-nitrosylation of proteins can regulate their functions in diverse ways; e.g. activation of thioredoxin and the Ras GTPase, inhibition of caspases and glyceraldehyde 3-phosphate dehydrogenase, inhibition of DNA-binding activity of the transcription factors NF-kB and AP-1 (Gaston et al. 2003; Miersch and Mutus 2005).