scholarly journals Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 435
Author(s):  
Elena Kalinina ◽  
Maria Novichkova
Keyword(s):  
Redox State ◽  
Nitrosative Stress ◽  
Redox Status ◽  
Thiol Groups ◽  
Redox Modulation ◽  
Post Translational Modifications ◽  
Cellular Redox ◽  
Physiological Conditions ◽  
Analyze Data

S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically. They are important for the regulation of the functional activity of proteins and intracellular processes. Connecting link and “switch” functions between S-glutathionylation and S-nitrosylation may be performed by GSNO, the generation of which depends on the GSH content, the GSH/GSSG ratio, and the cellular redox state. An important role in the regulation of these processes is played by Trx family enzymes (Trx, Grx, PDI), the activity of which is determined by the cellular redox status and depends on the GSH/GSSG ratio. In this review, we analyze data concerning the role of GSH/GSSG in the modulation of S-glutathionylation and S-nitrosylation and their relationship for the maintenance of cell viability.

scholarly journals Post-Translational S-Nitrosylation of Proteins in Regulating Cardiac Oxidative Stress

Antioxidants ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1051 ◽  
Author(s):  
Xiaomeng Shi ◽  
Hongyu Qiu
Keyword(s):  
Therapeutic Potential ◽  
Heart Diseases ◽  
Redox Homeostasis ◽  
Redox Status ◽  
Cardiac Protection ◽  
Cellular Functions ◽  
Post Translational Modifications ◽  
Cellular Redox ◽  
Novel Therapeutic Strategies

Like other post-translational modifications (PTMs) of proteins, S-nitrosylation has been considered a key regulatory mechanism of multiple cellular functions in many physiological and disease conditions. Emerging evidence has demonstrated that S-nitrosylation plays a crucial role in regulating redox homeostasis in the stressed heart, leading to discoveries in the mechanisms underlying the pathogenesis of heart diseases and cardiac protection. In this review, we summarize recent studies in understanding the molecular and biological basis of S-nitrosylation, including the formation, spatiotemporal specificity, homeostatic regulation, and association with cellular redox status. We also outline the currently available methods that have been applied to detect S-nitrosylation. Additionally, we synopsize the up-to-date studies of S-nitrosylation in various cardiac diseases in humans and animal models, and we discuss its therapeutic potential in cardiac protection. These pieces of information would bring new insights into understanding the role of S-nitrosylation in cardiac pathogenesis and provide novel avenues for developing novel therapeutic strategies for heart diseases.

scholarly journals The Effectiveness of Glutathione Redox Status as a Possible Tumor Marker in Colorectal Cancer

2021 ◽  
Vol 22 (12) ◽  
pp. 6183
Author(s):  
Delia Acevedo-León ◽  
Lidia Monzó-Beltrán ◽  
Segundo Ángel Gómez-Abril ◽  
Nuria Estañ-Capell ◽  
Natalia Camarasa-Lillo ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Redox State ◽  
Reduced Glutathione ◽  
Redox Status ◽  
Oxidation Products ◽  
Interventional Study ◽  
Thiol Redox State ◽  
Thiol Redox ◽  
Glutathione Redox

The role of oxidative stress (OS) in cancer is a matter of great interest due to the implication of reactive oxygen species (ROS) and their oxidation products in the initiation of tumorigenesis, its progression, and metastatic dissemination. Great efforts have been made to identify the mechanisms of ROS-induced carcinogenesis; however, the validation of OS byproducts as potential tumor markers (TMs) remains to be established. This interventional study included a total of 80 colorectal cancer (CRC) patients and 60 controls. By measuring reduced glutathione (GSH), its oxidized form (GSSG), and the glutathione redox state in terms of the GSSG/GSH ratio in the serum of CRC patients, we identified significant changes as compared to healthy subjects. These findings are compatible with the effectiveness of glutathione as a TM. The thiol redox state showed a significant increase towards oxidation in the CRC group and correlated significantly with both the tumor state and the clinical evolution. The sensitivity and specificity of serum glutathione levels are far above those of the classical TMs CEA and CA19.9. We conclude that the GSSG/GSH ratio is a simple assay which could be validated as a novel clinical TM for the diagnosis and monitoring of CRC.

scholarly journals Regulatory redox state in tree seeds

2017 ◽  
Vol 86 (4) ◽  
Author(s):  
Ewelina Ratajczak ◽  
Karl Josef Dietz
Keyword(s):  
Redox State ◽  
Redox Status ◽  
Long Term Storage ◽  
Tree Seeds ◽  
Term Storage ◽  
Intermediate Seeds

Peroxiredoxins (Prx) are important regulators of the redox status of tree seeds during maturation and long-term storage. Thioredoxins (Trx) are redox transmitters and thereby regulate Prx activity. Current research is focused on the association of Trx with Prx in tree seeds differing in the tolerance to desiccation. The results will allow for better understanding the regulation of the redox status in orthodox, recalcitrant, and intermediate seeds. The findings will also elucidate the role of the redox status during the loss of viability of sensitive seeds during drying and long-term storage.

scholarly journals A Regulatory Role of NAD Redox Status on Flavin Cofactor Homeostasis inS. cerevisiaeMitochondria

2013 ◽  
Vol 2013 ◽  
pp. 1-16 ◽  
Author(s):  
Teresa Anna Giancaspero ◽  
Vittoria Locato ◽  
Maria Barile
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nicotinamide Adenine Dinucleotide ◽  
Flavin Adenine Dinucleotide ◽  
Redox Balance ◽  
Redox Status ◽  
Cellular Redox ◽  
Isolated Mitochondria ◽  
Nudix Hydrolases ◽  
Order Of Magnitude

Flavin adenine dinucleotide (FAD) and nicotinamide adenine dinucleotide (NAD) are two redox cofactors of pivotal importance for mitochondrial functionality and cellular redox balance. Despite their relevance, the mechanism by which intramitochondrial NAD(H) and FAD levels are maintained remains quite unclear inSaccharomyces cerevisiae. We investigated here the ability of isolated mitochondria to degrade externally added FAD and NAD (in both its reduced and oxidized forms). A set of kinetic experiments demonstrated that mitochondrial FAD and NAD(H) destroying enzymes are different from each other and from the already characterized NUDIX hydrolases. We studied here, in some detail, FAD pyrophosphatase (EC 3.6.1.18), which is inhibited by NAD+and NADH according to a noncompetitive inhibition, withKivalues that differ from each other by an order of magnitude. These findings, together with the ability of mitochondrial FAD pyrophosphatase to metabolize endogenous FAD, presumably deriving from mitochondrial holoflavoproteins destined to degradation, allow for proposing a novel possible role of mitochondrial NAD redox status in regulating FAD homeostasis and/or flavoprotein degradation inS. cerevisiae.

scholarly journals Role of hydrogen peroxide and the redox state of ascorbate in the induction of antioxidant enzymes in pea leaves under excess light stress

2004 ◽  
Vol 31 (4) ◽  
pp. 359 ◽  
Author(s):  
Jose A. Hernández ◽  
Carolina Escobar ◽  
Gary Creissen ◽  
Phil M. Mullineaux
Keyword(s):  
Antioxidant Enzymes ◽  
Redox State ◽  
Light Stress ◽  
Redox Status ◽  
Protein Accumulation ◽  
Photoinhibition Of Photosynthesis ◽  
Transcript Accumulation ◽  
Land Race ◽  
Excess Light

In this work we used two different pea cultivars, JI281 is a semidomesticated land race of pea from Ethiopia whereas JI399 is a typical domesticated pea variety. Exposure of pea leaves to excess light (EL) for 1 h caused a reversible photoinhibition of photosynthesis as showed by changes in Fv / Fm. Although little difference existed between the two pea genotypes with respect to photoinhibition, after 60 min of EL the decline in Fv / Fm was higher in JI281 than in JI399 leaves. As a consequence of EL, H2O2 increased in both pea cultivars, whereas lipid peroxidation and protein oxidation slightly increased, although differences between cultivars were minimal. The redox state of ascorbate shifted towards its oxidized form under EL stress in both cultivars. Transcript levels of genes coding antioxidant enzymes varied with EL in both cultivars, but the response was more pronounced in JI399. The induction observed during EL was maintained or increased after the stress period, as occurred for cytGR and chlMDHAR. GR protein accumulation and activity correlated with the transcript accumulation in JI399, but not in JI288. In this work, a possible role for H2O2 and redox status of ascorbate in the photoxidative stress signalling is discussed.

Nitric oxide and hydrogen sulfide modulate the NADPH-generating enzymatic system in higher plants

2020 ◽  
Author(s):  
Francisco J Corpas ◽  
Salvador González-Gordo ◽  
José M Palma
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Sulfide ◽  
Plant Cells ◽  
Redox Status ◽  
Signal Molecules ◽  
Tyrosine Nitration ◽  
Enzymatic System ◽  
Post Translational Modifications ◽  
Cellular Redox ◽  
Wide Range

Abstract Nitric oxide (NO) and hydrogen sulfide (H2S) are two key molecules in plant cells that participate, directly or indirectly, as regulators of protein functions through derived post-translational modifications, mainly tyrosine nitration, S-nitrosation, and persulfidation. These post-translational modifications allow the participation of both NO and H2S signal molecules in a wide range of cellular processes either physiological or under stressful circumstances. NADPH participates in cellular redox status and it is a key cofactor necessary for cell growth and development. It is involved in significant biochemical routes such as fatty acid, carotenoid and proline biosynthesis, and the shikimate pathway, as well as in cellular detoxification processes including the ascorbate–glutathione cycle, the NADPH-dependent thioredoxin reductase (NTR), or the superoxide-generating NADPH oxidase. Plant cells have diverse mechanisms to generate NADPH by a group of NADP-dependent oxidoreductases including ferredoxin-NADP reductase (FNR), NADP-glyceraldehyde-3-phosphate dehydrogenase (NADP-GAPDH), NADP-dependent malic enzyme (NADP-ME), NADP-dependent isocitrate dehydrogenase (NADP-ICDH), and both enzymes of the oxidative pentose phosphate pathway, designated as glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH). These enzymes consist of different isozymes located in diverse subcellular compartments (chloroplasts, cytosol, mitochondria, and peroxisomes) which contribute to the NAPDH cellular pool. We provide a comprehensive overview of how post-translational modifications promoted by NO (tyrosine nitration and S-nitrosation), H2S (persulfidation), and glutathione (glutathionylation), affect the cellular redox status through regulation of the NADP-dependent dehydrogenases.

scholarly journals Oxidative Stress-Mediated Skeletal Muscle Degeneration: Molecules, Mechanisms, and Therapies

2016 ◽  
Vol 2016 ◽  
pp. 1-13 ◽  
Author(s):  
Min Hee Choi ◽  
Jin Rong Ow ◽  
Nai-Di Yang ◽  
Reshma Taneja
Keyword(s):  
Oxidative Stress ◽  
Molecular Level ◽  
Redox Homeostasis ◽  
Redox Status ◽  
Muscle Degeneration ◽  
Dystrophic Muscle ◽  
Telomere Shortening ◽  
Cellular Redox ◽  
Pathological Conditions

Oxidative stress is a loss of balance between the production of reactive oxygen species during cellular metabolism and the mechanisms that clear these species to maintain cellular redox homeostasis. Increased oxidative stress has been associated with muscular dystrophy, and many studies have proposed mechanisms that bridge these two pathological conditions at the molecular level. In this review, the evidence indicating a causal role of oxidative stress in the pathogenesis of various muscular dystrophies is revisited. In particular, the mediation of cellular redox status in dystrophic muscle by NF-κB pathway, autophagy, telomere shortening, and epigenetic regulation are discussed. Lastly, the current stance of targeting these pathways using antioxidant therapies in preclinical and clinical trials is examined.

scholarly journals The Emerging Role of TXNIP in Ischemic and Cardiovascular Diseases; A Novel Marker and Therapeutic Target

2021 ◽  
Vol 22 (4) ◽  
pp. 1693
Author(s):  
Alison Domingues ◽  
Julia Jolibois ◽  
Perrine Marquet de Rougé ◽  
Valérie Nivet-Antoine
Keyword(s):  
Oxidative Stress ◽  
Cardiovascular Diseases ◽  
Therapeutic Target ◽  
Redox Status ◽  
Interacting Protein ◽  
Cellular Redox ◽  
Thioredoxin Interacting Protein ◽  
Potential Biomarker ◽  
Ischemic Diseases

Thioredoxin interacting protein (TXNIP) is a metabolism- oxidative- and inflammation-related marker induced in cardiovascular diseases and is believed to represent a possible link between metabolism and cellular redox status. TXNIP is a potential biomarker in cardiovascular and ischemic diseases but also a novel identified target for preventive and curative medicine. The goal of this review is to focus on the novelties concerning TXNIP. After an overview in TXNIP involvement in oxidative stress, inflammation and metabolism, the remainder of this review presents the clues used to define TXNIP as a new marker at the genetic, blood, or ischemic site level in the context of cardiovascular and ischemic diseases.

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