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BBA - General Subjects (v.1820, #6)
Regulation of cellular processes by S-nitrosylation
by Harvey E. Marshall; Andrew Gow (pp. 673-674).
Methodologies for the characterization, identification and quantification of S-nitrosylated proteins by Matthew W. Foster (pp. 675-683).
Protein S-nitrosylation plays a central role in signal transduction by nitric oxide (NO), and aberrant S-nitrosylation of specific proteins is increasingly implicated in disease.Here, methodologies for the characterization, identification and quantification of SNO-proteins are reviewed, focusing on techniques suitable for the structural characterization and absolute quantification of isolated SNO-proteins, the identification and relative quantification of SNO-proteins from complex mixtures as well as the mass spectrometry-based identification and relative quantification of sites of S-nitrosylation (SNO-sites) in proteins.Structural characterization of SNO-proteins by X-ray crystallography is increasingly being utilized to understand both the relationships between protein structure and Cys thiol reactivity as well as the consequences of S-nitrosylation on protein structure and function. New methods for the proteomic identification and quantification of SNO-proteins and SNO-sites have greatly impacted the ability to study protein S-nitrosylation in complex biological systems.The ability to identify and quantify SNO-proteins has long been rate-determining for scientific advances in the field of protein S-nitrosylation. Therefore, it is critical that investigators in the field have a good understand the utility and limitations of modern analytical techniques for SNO-protein analysis.This article is part of a Special Issue entitled: Regulation of cellular processes by S-nitrosylation.► Protein S-nitrosylation is critical for signal transduction by nitric oxide (NO). ► S-nitrosylated proteins (SNO-proteins) are often difficult to detect and quantify. ► Decomposition of SNO-protein to NO or nitrite is required for absolute quantification. ► Thiol-based assays can be used to identify sites of S-nitrosylation (SNO-sites).
Keywords: S-nitrosylation; S-nitrosothiol; Nitric oxide; Biotin switch
Strategies and tools to explore protein S-nitrosylation by Karthik Raju; Paschalis-Thomas Doulias; Margarita Tenopoulou; Jennifer L. Greene; Harry Ischiropoulos (pp. 684-688).
A biochemical pathway by which nitric oxide accomplishes functional diversity is the specific modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, interactions and location. However, comprehensive studies exploring protein signaling pathways or interrelated protein clusters that are regulated by S-nitrosylation have not been performed on a global scale.To provide insights to these important biological questions, sensitive, validated and quantitative proteomic approaches are required. This review summarizes current approaches for the global identification of S-nitrosylated proteins.The application of novel methods for identifying S-nitrosylated proteins, especially when combined with mass-spectrometry based proteomics to provide site-specific identification of the modified cysteine residues, promises to deliver critical clues for the regulatory role of this dynamic posttranslational modification in cellular processes.Though several studies have established S-nitrosylation as a regulator of protein function in individual proteins, the biological chemistry and the structural elements that govern the specificity of this modification in vivo are vastly unknown. Additionally, a gap in knowledge exists concerning the potential global regulatory role(s) this modification may play in cellular physiology. By further studying S-nitrosylation at a global scale, a greater appreciation of nitric oxide and protein S-nitrosylation in cellular function can be achieved. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.► S-nitrosylation of cysteine residues an important regulator of protein function ► Description of methods to identify S-nitrosylated proteins ► Mass spectrometry-based proteomics essential for further studies of S-nitrosylation biology
Keywords: S-nitrosylation; Proteomics; Mass spectrometry; Cysteine post translational modification; Nitric oxide
The role of thioredoxin in the regulation of cellular processes by S-nitrosylation by Rajib Sengupta; Arne Holmgren (pp. 689-700).
S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly associated with the S-nitrosothiols and a considerable number of S-nitrosylated proteins have been identified which can positively or negatively regulate various cellular processes including signaling and metabolic pathways.Taking account of the recent progress in the field of research, this review focuses on the regulation of cellular processes by S-nitrosylation and Trx-mediated cellular homeostasis of S-nitrosothiols.Thioredoxin (Trx) system in mammalian cells utilizes thiol and selenol groups to maintain a reducing intracellular environment to combat oxidative/nitrosative stress. Reduced glutathione (GSH) and Trx system perform the major role in denitrosylation of S-nitrosylated proteins. However, under certain conditions, oxidized form of mammalian Trx can be S-nitrosylated and then it can trans- S-nitrosylate target proteins, such as caspase 3.Investigations on the role of thioredoxin system in relation to biologically relevant RSNOs, their functions, and the mechanisms of S-denitrosylation facilitate the development of drugs and therapies. This article is part of a Special Issue entitled Regulation of Cellular Processes.► S-nitrosylation is an important feature of NO biology and pathobiology. ► Many S-nitrosylated proteins regulate various cellular processes. ► Thioredoxin system plays an important role to combat oxidative/nitrosative stress. ► GSH and Trx system perform the major role in denitrosylation of RSNOs.
Keywords: Nitric oxide; S; -nitrosylation; Thiol; Redox regulation; Thioredoxin; Thioredoxin reductase
S-nitrosylation in the regulation of gene transcription by Yonggang Sha; Harvey E. Marshall (pp. 701-711).
Post-translational modification of proteins by S-nitrosylation serves as a major mode of signaling in mammalian cells and a growing body of evidence has shown that transcription factors and their activating pathways are primary targets. S-nitrosylation directly modifies a number of transcription factors, including NF-κB, HIF-1, and AP-1. In addition, S-nitrosylation can indirectly regulate gene transcription by modulating other cell signaling pathways, in particular JNK kinase and ras.The evolution of S-nitrosylation as a signaling mechanism in the regulation of gene transcription, physiological advantages of protein S-nitrosylation in the control of gene transcription, and discussion of the many transcriptional proteins modulated by S-nitrosylation is summarized.S-nitrosylation plays a crucial role in the control of mammalian gene transcription with numerous transcription factors regulated by this modification. Many of these proteins serve as immunomodulators, and inducible nitric oxide synthase (iNOS) is regarded as a principal mediatiator of NO-dependent S-nitrosylation. However, additional targets within the nucleus (e.g. histone deacetylases) and alternative mechanisms of S-nitrosylation (e.g. GAPDH-mediated trans-nitrosylation) are thought to play a role in NOS-dependent transcriptional regulation.Derangement of SNO-regulated gene transcription is an important factor in a variety of pathological conditions including neoplasia and sepsis. A better understanding of protein S-nitrosylation as it relates to gene transcription and the physiological mechanisms behind this process is likely to lead to novel therapies for these disorders. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.► S-nitrosylation (SNO) plays a crucial role in the control of gene transcription. ► SNO-regulated gene transcription evolved in bacteria as a means to detect NO stress. ► In eukaryotes, SNO primarily regulates transcription in the context of cell signaling. ► Nitrosylating and denitrosylating enzymes precisely regulate SNO-protein formation. ► Dysregulation of SNO-protein metabolism contributes to disease pathogenesis.
Keywords: S-nitrosylation; Nitric oxide; Gene transcription; Transcription factors
Regulation of mitochondrial processes by protein S-nitrosylation by Claude A. Piantadosi (pp. 712-721).
Nitric oxide (NO) exerts powerful physiological effects through guanylate cyclase (GC), a non-mitochondrial enzyme, and through the generation of protein cysteinyl-NO (SNO) adducts—a post-translational modification relevant to mitochondrial biology. A small number of SNO proteins, generated by various mechanisms, are characteristically found in mammalian mitochondria and influence the regulation of oxidative phosphorylation and other aspects of mitochondrial function.The principles by which mitochondrial SNO proteins are formed and their actions, independently or collectively with NO binding to heme, iron–sulfur centers, or to glutathione (GSH) are reviewed on a molecular background of SNO-based signal transduction.Mitochondrial SNO-proteins have been demonstrated to inhibit Complex I of the electron transport chain, to modulate mitochondrial reactive oxygen species (ROS) production, influence calcium-dependent opening of the mitochondrial permeability transition pore (MPTP), promote selective importation of mitochondrial protein, and stimulate mitochondrial fission. The ease of reversibility and the affirmation of regulated S-nitros(yl)ating and denitros(yl)ating enzymatic reactions support hypotheses that SNO regulates the mitochondrion through redox mechanisms. SNO modification of mitochondrial proteins, whether homeostatic or adaptive (physiological), or pathogenic, is an area of active investigation.Mitochondrial SNO proteins are associated with mainly protective, bur some pathological effects; the former mainly in inflammatory and ischemia/reperfusion syndromes and the latter in neurodegenerative diseases. Experimentally, mitochondrial SNO delivery is also emerging as a potential new area of therapeutics. This article is part of a Special Issue entitled: Regulation of cellular processes by S-nitrosylation.► Mitochondria contain both S-nitrosylating and denitrosylating mechanisms. ► Reversible protein S-nitrosylation supports redox regulation in mitochondria. ► SNO inhibits Complex I and steps in intermediary and fatty acid metabolism. ► SNO activates mitochondrial protein importation and regulates mitochondrial fission. ► Mitochondrial SNO proteins are involved in both cell protection and cell damage.
Keywords: Metabolism; Mitochondria; Nitric oxide; Respiration; S-nitrosylation; S-nitrosation
S-Nitrosylation signaling regulates cellular protein interactions by Nadzeya V. Marozkina; Benjamin Gaston (pp. 722-729).
S-Nitrosothiols are made by nitric oxide synthases and other metalloproteins. Unlike nitric oxide, S-nitrosothiols are involved in localized, covalent signaling reactions in specific cellular compartments. These reactions are enzymatically regulated.S-Nitrosylation affects interactions involved in virtually every aspect of normal cell biology. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.S-Nitrosylation is a regulated signaling reaction.► Nitric oxide synthase activation forms S-nitrosothiols. ► S-nitrosylation signaling is regulated. ► Virtually every aspect of cell biology is impacted S-nitrosylation signaling.
Keywords: Cell signaling; Nitric oxide synthase; Nitrosonium; Protein–protein interaction; S-Nitrosoglutathione; S-Nitrosylation
Regulation of DNA repair by S-nitrosylation by Chi-Hui Tang; Wei Wei; Limin Liu (pp. 730-735).
Expression of the inducible nitric oxide synthase (iNOS) is commonly induced in inflammation, an important risk factor of cancer. Nitric oxide (NO) and related reactive nitrogen species can directly cause DNA damage to increase DNA mutation. They can also indirectly affect DNA mutation by modulation of DNA repair proteins, in particular through protein S-nitrosylation, a key regulatory mechanism of NO.Here we review protein targets, molecular mechanisms, and potential roles of NO in the regulation of DNA repair, with a focus on S-nitrosylation of DNA repair proteins by endogenous NO synthase activity.Recent studies have identified a number of key DNA repair proteins as targets of S-nitrosylation, including O6-alkylguanine-DNA-alkyltransferase (AGT), 8-oxoguanine glycosylase, apurinic-apyrimidinic endonuclease 1, and DNA-dependent protein kinase catalytic subunit. S-nitrosylation has been shown to modulate the activity, stability, and cellular localization of DNA repair proteins. The level of protein S-nitrosylation depends both on NO synthesis by NO synthases and on denitrosylation by a major denitrosylase, S-nitrosoglutathione reductase (GSNOR). Dysregulated S-nitrosylation of AGT due to GSNOR deficiency inactivates AGT-dependent DNA repair and appears to contribute critically to hepatocarcinogenesis.Studies on the S-nitrosylation of DNA repair proteins have started to reveal molecular mechanisms for the contribution of inflammation to mutagenesis and carcinogenesis. The modulation of protein S-nitrosylation to affect the activity of DNA repair proteins may provide a therapeutic strategy to prevent DNA damage and mutation frequently associated with chronic inflammation and to sensitize cancer cells to DNA-damaging drugs. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.►NO/RNS can directly or indirectly cause DNA mutation. ►Key DNA repair proteins AGT, Ogg1, APE1, and DNA-PKcs are targets of S-nitrosylation. ►S-nitrosylation modulates DNA repair protein activity, stability, and localization. ►S-nitrosylation levels depend on NO synthesis by NOS and denitrosylation by GSNOR. ►GSNOR deficiency leads to nitrosative inactivation of AGT and hepatocarcinogenesis.
Keywords: Abbreviations; 8-oxoG; 8-oxoguanine; AGT; O; 6; -alkylguanine-DNA-alkyltransferase; AP; apurinic-apyrimidinic; APE1; AP endonuclease 1; BER; base excision repair; DEN; diethylnitrosamine; DNA-PKcs; DNA-dependent protein kinase catalytic subunit; DSB; double-strand break; DTT; dithiothreitol; GAPDH; glyceraldehyde-3-phosphate dehydrogenase; GSNO; S-nitrosoglutathione; GSNOR; GSNO reductase; HCC; hepatocellular carcinoma; LPS; lipopolysaccharide; NER; nucleotide excision repair; NO; nitric oxide; NOS; NO synthase; Ogg1; 8-oxoG glycosylase; RNS; reactive nitrogen species; SNO; S-nitrosothiol; Zn; zincNitric oxide; S-nitrosylation; DNA repair proteins; Inflammation; Nitrosative stress; Carcinogenesis
Protein S-nitrosylation: Role for nitric oxide signaling in neuronal death by Neelam Shahani; Akira Sawa (pp. 736-742).
One of the signaling mechanisms mediated by nitric oxide (NO) is through S-nitrosylation, the reversible redox-based modification of cysteine residues, on target proteins that regulate a myriad of physiological and pathophysiological processes. In particular, an increasing number of studies have identified important roles for S-nitrosylation in regulating cell death.The present review focuses on different targets and functional consequences associated with nitric oxide and protein S-nitrosylation during neuronal cell death. S-Nitrosylation exhibits double-edged effects dependent on the levels, spatiotemporal distribution, and origins of NO in the brain: in general Snitrosylation resulting from the basal low level of NO in cells exerts anti-cell death effects, whereas S-nitrosylation elicited by induced NO upon stressed conditions is implicated in pro-cell death effects.Dysregulated protein S-nitrosylation is implicated in the pathogenesis of several diseases including degenerative diseases of the central nervous system (CNS). Elucidating specific targets of S-nitrosylation as well as their regulatory mechanisms may aid in the development of therapeutic intervention in a wide range of brain diseases.
Keywords: Nitric oxide; S; -nitrosylation; Apoptosis; Caspase; XIAP; GAPDH
S-nitrosylation-regulated GPCR signaling by Yehia Daaka (pp. 743-751).
G protein-coupled receptors (GPCRs) are the most numerous and diverse type of cell surface receptors, accounting for about 1% of the entire human genome and relaying signals from a variety of extracellular stimuli that range from lipid and peptide growth factors to ions and sensory inputs. Activated GPCRs regulate a multitude of target cell functions, including intermediary metabolism, growth and differentiation, and migration and invasion. The GPCRs contain a characteristic 7-transmembrane domain topology and their activation promotes complex formation with a variety of intracellular partner proteins, which form basis for initiation of distinct signaling networks as well as dictate fate of the receptor itself. Both termination of active GPCR signaling and removal from the plasma membrane are controlled by protein post-translational modifications of the receptor itself and its interacting partners. Phosphorylation, acylation and ubiquitination are the most studied post-translational modifications involved in GPCR signal transduction, subcellular trafficking and overall expression. Emerging evidence demonstrates that protein S-nitrosylation, the covalent attachment of a nitric oxide moiety to specified cysteine thiol groups, of GPCRs and/or their associated effectors also participates in the fine-tuning of receptor signaling and expression. This newly appreciated mode of GPCR system modification adds another set of controls to more precisely regulate the many cellular functions elicited by this large group of receptors.This article is part of a Special Issue entitled: Regulation of cellular processes by S-nitrosylation.► Regulation of GPCR signaling by GRKs and βArrestins. ► Role of GPCR phosphorylation in receptor function. ► GPCR system modification by S-nitrosylation.
Keywords: GPCR; GRK; Arrestin; Dynamin; S-nitrosylation
Regulation of cardiovascular cellular processes by S-nitrosylation by Ivonne Hernandez Schulman; Joshua M. Hare (pp. 752-762).
Nitric oxide (NO), a highly versatile signaling molecule, exerts a broad range of regulatory influences in the cardiovascular system that extends from vasodilation to myocardial contractility, angiogenesis, inflammation, and energy metabolism. Considerable attention has been paid to deciphering the mechanisms for such diversity in signaling. S-nitrosylation of cysteine thiols is a major signaling pathway through which NO exerts its actions. An emerging concept of NO pathophysiology is that the interplay between NO and reactive oxygen species (ROS), the nitroso/redox balance, is an important regulator of cardiovascular homeostasis.ROS react with NO, limit its bioavailability, and compete with NO for binding to the same thiol in effector molecules. The interplay between NO and ROS appears to be tightly regulated and spatially confined based on the co-localization of specific NO synthase (NOS) isoforms and oxidative enzymes in unique subcellular compartments. NOS isoforms are also in close contact with denitrosylases, leading to crucial regulation of S-nitrosylation.Nitroso/redox balance is an emerging regulatory pathway for multiple cells and tissues, including the cardiovascular system. Studies using relevant knockout models, isoform specific NOS inhibitors, and both in vitro and in vivo methods have provided novel insights into NO- and ROS-based signaling interactions responsible for numerous cardiovascular disorders.An integrated view of the role of nitroso/redox balance in cardiovascular pathophysiology has significant therapeutic implications. This is highlighted by human studies where pharmacologic manipulation of oxidative and nitrosative pathways exerted salutary effects in patients with advanced heart failure. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.► We review cardiovascular NO signaling through S-nitrosylation of cysteine thiols. ► Subcellular localization of NOS enzymes provides localized signal for S-nitrosylation. ► NOS isoforms are in close contact with denitrosylases, which regulate S-nitrosylation. ► The nitroso/redox balance is an important regulator of cardiovascular homeostasis.
Keywords: Abbreviations; [Ca; 2+; ]; i; Intracellular calcium concentration; cGMP; 3′,5′-cyclic guanosine monophosphate; ECM; Extracellular matrix; GRK2; G protein coupled receptor kinase; GSH; Glutathione; GSNHOH; Glutathione S-hydroxysulfenamide; GSNO; S-nitrosoglutathione; GSNOR; S-nitrosoglutathione reductase; GSSG; Oxidized glutathione; HIF; hypoxia inducible factor; K; +; potassium; LTCC; L-type Ca; 2+; channel; MKP7; mitogen activated protein kinase phosphatase 7; MVO; 2; Myocardial oxygen consumption; Na; +; sodium; NCX; Sodium–calcium exchanger; NFκB; nuclear factor κB; NO; Nitric oxide; N; 2; O; 3; dinitrogen trioxide; NOS; Nitric oxide synthases; NSF; N-ethylmaleimide sensitive factor; 5′-NU; Ecto-5′-nucleotidase; O; 2; Oxygen; PDE; Phosphodiesterase; PKG; cGMP-dependent protein kinase; PLB; Phospholamban; RNS; Reactive nitrogen species; ROS; Reactive oxygen species; RYR2; Ryanodine receptor/Ca; 2+; -release channel; SERCA; Sarcoplasmic reticulum Ca; 2+; ATPase; sGC; Soluble guanylate cyclase; SHHF; Spontaneously hypertensive-heart failure; SNO; S-nitrosothiols; SNO-Hb; S-nitrosohemoglobin; SR; Sarcoplasmic reticulum; TonEBP; Tonicity-responsive enhancer binding protein; VEGF; Vascular endothelial growth factor; XO; Xanthine oxidaseNitric oxide; Nitrosative and oxidative stress; Excitation–contraction coupling; Adrenergic contractility; Angiogenesis; Inflammation
S-nitrosylation of surfactant protein D as a modulator of pulmonary inflammation by Elena N. Atochina-Vasserman (pp. 763-769).
Surfactant protein D (SP-D) is a member of the family of proteins termed collagen-like lectins or “collectins” that play a role in non-antibody-mediated innate immune responses []. The primary function of SP-D is the modulation of host defense and inflammation .This review will discuss recent findings on the physiological importance of SP-D S-nitrosylation in biological systems and potential mechanisms that govern SP-D mediated signaling.SP-D appears to have both pro- and anti-inflammatory signaling functions.SP-D multimerization is a critical feature of its function and plays an important role in efficient innate host defense. Under baseline conditions, SP-D forms a multimer in which the N-termini are hidden in the center and the C-termini are on the surface. This multimeric form of SP-D is limited in its ability to activate inflammation. However, NO can modify key cysteine residues in the hydrophobic tail domain of SP-D resulting in a dissociation of SP-D multimers into trimers, exposing the S-nitrosylated N-termini. The exposed S-nitrosylated tail domain binds to the calreticulin/CD91 receptor complex and initiates a pro-inflammatory response through phosphorylation of p38 and NF-κB activation [3,4]. In addition, the disassembled SP-D loses its ability to block TLR4, which also results in activation of NF-κB.Recent studies have highlighted the capability of NO to modify SP-D through S-nitrosylation, causing the activation of a pro-inflammatory role for SP-D [3]. This represents a novel mechanism both for the regulation of SP-D function and NO's role in innate immunity, but also demonstrates that the S-nitrosylation can control protein function by regulating quaternary structure. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.► Multimerization of SP-D is a critical feature of its function. ► NO is capable of modifying SP-D through S-nitrosylation. ► S-nitrosylation of SP-D causes disruption of its quaternary structure into trimers. ► The formation of SNO-SP-D trimers initiates a pro-inflammatory response. ► Disruption of SP-D multimeric state causes a loss of its anti-inflammatory function.
Keywords: Abbreviations; TLR; Toll-like receptor; TIR; Toll/IL-1 receptor domain; LPS; lipopolyssacharides; LBP; LPS-binding protein; MD-2; myeloid differentiation factor 2; MyD88; myeloid differentiation protein 88; IRAK; IL-1 receptor associated kinase; TRAF6; TNF receptor associated factor; MAPK; mitogen-activated protein kinase; TAK1; transforming growth factor b-associated kinase 1; TAB1; TAK1-binding protein 1; TAB2; TAK1-binding protein 2; IKK; IκB kinase; IκB; inhibitor of NF-κB; NF-κB; nuclear factor kappa B; SIRP-1α; signal inhibitory regulatory protein-1α; SHP-1; tyrosine-protein phosphatase-1; MBL; mannose-binding lectin; ARDS; acute respiratory distress syndrome; ALI; acute lung injury; COPD; chronic obstructive pulmonary diseaseSP-D; Surfactant protein D; TLR; Toll like receptor; NO; Nitric oxide; SNO; S-; nitrosothiol; Pulmonary inflammation; Macrophages polarization
Synthesis of and signalling by small, redox active molecules in the plant immune response by Byung-Wook Yun; Steven H. Spoel; Gary J. Loake (pp. 770-776).
Reactive oxygen and nitrogen intermediates (ROIs and RNIs), respectively, are central features of the plant immune response. Rare, highly reactive protein cysteine (Cys) residues of low pKa are a major target for these intermediates. In this context, S-nitrosylation, the addition of a nitric oxide (NO) moiety to a Cys thiol to form an S-nitrosothiol (SNO), is emerging as a key, redox-based post-translational modification during plant immune function.Here, we describe some recent insights into how ROIs and RNIs are synthesized and how these small, redox active molecules help orchestrate the plant defence response.The reviewed data highlights the growing importance of ROIs and RNIs in orchestrating the development of plant immunity and provides insights into the molecular mechanisms underpinning their function.Signalling via small, redox active molecules is a key feature underpinning a diverse series of signal transduction networks in eukaryotic cells. Therefore, insights into the mechanisms that support the activity of these molecules may have potentially wide significance.This article is part of a Special Issue entitled: Regulation of cellular processes by S-nitrosylation.► We review the synthesis of reactive oxygen intermediates (ROIs) in plant immunity. ► The production of nitric oxide (NO) is also discussed. ► ROIs and NO regulate the function of key immune regulators. ► Manipulating redox status may provide novel strategies to convey disease resistance.
Keywords: Reactive oxygen intermediates; Reactive nitrogen intermediates; Nitric oxide; Plant defence; Redox signalling; S-nitrosylation
Nitroalkylation — A redox sensitive signaling pathway by Anne C. Geisler; Tanja K. Rudolph (pp. 777-784).
Redox-sensitive posttranslational modification emerged as important signaling mechanisms. Besides other posttranslational modifications nitroalkylation by nitrated fatty acids mediate favorable anti-inflammatory effects. This review gives an overview of the generation and the reactivity of nitrated fatty acids. Additionally, it provides insights into the so far described pathways regulated by nitrated fatty acids. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.► We give an overview of the generation and the reactivity of nitrated fatty acids. ► Redox-sensitive post-translational modification (nitroalkylation) of fatty acids serves as important signaling mechanism. ► Nitrated fatty acids are potent anti-inflammatory lipid signaling mediators. ► Pathways regulated by nitrated fatty acids.
Keywords: Abbreviations; AP-1; activator protein-1; AT; 1; R; angiotensin 1 receptor; HO-1; heme oxygenase-1; HSF1/2; heat shock factor 1/2; HSR; heat shock response; IκB; NF-kappa-B inhibitor; Keap1; Kelch like ECH associating protein 1; LNO; 2; linoleic acid; LPS; lipopolysaccharides; MKP-1; MAPK phosphatase 1; MMPs; matrix metalloproteinases; NFκB; nuclear factor of kappa light polypeptide gene enhancer in B-cells; NO; nitric oxide; NO; 2; nitrogen dioxide; NO; 2; −; nitrite; NO; 2; -FA; nitrated fatty acids; Nrf2; nuclear factor erythroid 2-related factor 2; O; 2; −; superoxide anion; OA-NO; 2; nitrated oleic acid; ONOO; −; peroxynitrite; PPAR-γ; peroxisome proliferator-activated receptor gamma; RNS; reactive nitrogen species; ROS; reactive oxygen species; STAT-1; signal transducer and activator of transcription-1Nitrated fatty acids; Nitroalkylation; Electrophile; Nitric oxide