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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).
The controlling role of nitric oxide within the shell of nucleus accumbens in the stress-induced metabolic disturbance
Published in Archives of Physiology and Biochemistry, 2021
Yasaman Husseini, Alireza Mohammadi, Gila Pirzad Jahromi, Gholamhossein Meftahi, Hedayat Sahraei, Boshra Hatef
Stress induces changes in gene expression of nNOS in regions related to stress responses and increases the production of NO (de Oliveira et al.2000, Krukoff and Khalili 1997). Nitric Oxide increases the production of cyclic guanosine monophosphate (cGMP) by the activation of the guanylate cyclase. This secondary messenger is also responsible for a part of the nitric oxide’s effects (Änggård 1994, Calabrese et al.2007). NO is a free radical which is able to affect a wide range of bio-molecules in the membrane, cytoplasm and intercellular space, due to its radical nature, and makes them undergo nitrosylation. It also as a neurotransmitter is a multifunctional messenger that can transfer the signal in antero- and retrograde directions (Feil and Kleppisch 2008). Moreover, nitric oxide can interact with dopaminergic and glutaminergic systems in several brain areas such as NAc and increases the release of them (Motahari et al.2016). On the other hand, the NAc is involved in the modulation of stress response (Ranjbaran et al.2017). Therefore, NO modulation in the NAc can affect the stress-related response of brain such as metabolic control shown in the current study. In the present study, although stress increased cortisol plasma concentrations, decreased the rat’s weight and changed the food and water intake, NO modulators affected these changes in different and dose-dependent manners.
Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Anna Di Fiore, Claudiu T. Supuran, Andrea Scaloni, Giuseppina De Simone
Protein S-nitrosylation, the oxidative modification of cysteine residues by nitric oxide (NO) to form S-nitrosothiols, modifies a number of proteins, also in their activity, and provides a fundamental redox-based cellular signalling mechanism76,77. Differently from other PTMs, it is generally considered to be non-enzymatic and may involve multiple chemical routes for its accomplishment. In agreement with preliminary evidences reporting S-nitrosylation of CA III in rat liver78, this isozyme is the only protein reported to be affected by this PTM (Figure 2), which occurs at C6679. This residue is not accessible on the protein surface but, probably being highly reactive, can be easily reached by small-size S-nitrosylating molecules, such as NO and SNOs. It localises close to proton shuttle residue (K64); this suggests that this modification may eventually affect the enzyme activity. Accordingly, novel studies are encouraged to investigate the role of S-nitrosylation in controlling CA III catalysis, and the participation of this isozyme in redox-based cellular signalling mechanisms, as already observed for other CAs in plants80,81.
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.