The enzyme may also transfer the -glutamyl moiety of GSH to amino acids and peptides. This book contains an overview focusing on the research area of enzyme inhibitor and activator, enzyme-catalyzed biotransformation, usage of microbial enzymes, enzymes associated with programmed cell death, natural products as potential GSH can interact with certain metal ions. Peroxynitrite is a product of the interaction between nitric oxide and superoxide anion radical and is known to be a powerful nitrosating agent [190]. Here, I will mention just a few important aspects of the mGSH system. Regulation, Structure And Function Of Glutathione Thus, there is no need for in depth coverage of this field, and interested readers are directed instead to several excellent recent reviews [21, 22, 86, 166, 195198]. As a result several experimental models of human pathologies have been developed in D. melanogaster, making it a very useful biomedical tool. By protecting cardiolipin from oxidative damage, GSH prevents changes in the physicochemical properties of the mitochondrial inner membrane that lead to membrane destabilization and the dissociation of cytochrome . Another is the fact that many organs consist of multiple cell types which can possess different glutathione levels and forms. B. Table of Contents1 [] Volumes in this widely revered series present comprehensive reviews of drug substances and additional materials, with critical review chapters that summarize information related to the characterization of drug substances and excipients. B. Wang, X. Q. Zhang, J. Ren, and C. M. Zeng, Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins,, A. Ouchi, M. Ishikura, K. Konishi, S. I. Nagaoka, and K. Mukai, Kinetic study of the prooxidant effect of, V. Lushchak, H. Semchyshyn, O. Lushchak, and S. Mandryk, Diethyldithiocarbamate inhibits, V. Lushchak, H. Semchyshyn, S. Mandryk, and O. Lushchak, Possible role of superoxide dismutases in the yeast, V. Lips, G. Celedn, J. Escobar, and E. A. Lissi, Thiol-induced hemoglobin oxidation,, I. Rebrin and R. S. Sohal, Pro-oxidant shift in glutathione redox state during aging,, V. Sampath and W. S. Caughey, Prooxidant effects of glutathione in aerobic hemoglobin solutions. Since the use of oxidants to deplete GSH pools in the treatment of different pathologies usually causes many side effects, BSO was soon tested not only for basic research purposes, but also for clinical investigations in cancer research. A. Kumar et al., Transcriptional upregulation of Nrf2-dependent phase II detoxification genes in the involved epidermis of vitiligo vulgaris,, G. Shen, C. Xu, R. Hu et al., Modulation of nuclear factor E2-related factor 2-mediated gene expression in mice liver and small intestine by cancer chemopreventive agent curcumin,, S. A. Rushworth, R. M. Ogborne, C. A. Charalambos, and M. A. O'Connell, Role of protein kinase C, M. Kim, A. Murakami, and H. Ohigashi, Modifying effects of dietary factors on (, J. K. Kundu and Y. J. Surh, Epigallocatechin Gallate inhibits phorbol ester-induced activation of NF-, T. Zhang, D. Yang, Y. Now how can i resume the pH to 7, to use this water in PCR and other solutions preparation? Abstract. Hence, there is a need to introduce new techniques for the proper evaluation of the operation of the mitochondrial GSH system. Planning to prepare an emulsion of natural oil in water. How to explain DSC results having two endothermic peak obtained at 51.19 and 65.44 of an ester prepared from triazine ring based compound? Secondly, the affinity of GPx for H2O2 is one to two orders of magnitude higher than that of catalase. the first results and prospects,, H. J. Schmahl, L. Dencker, C. Plum, I. Chahoud, and H. Nau, Stereoseleetive distribution of the teratogenic thalidomide analogue EM12 in the early embryo of marmoset monkey, Wistar rat and NMRI mouse,, D. Plano, Y. Baquedano, E. Ibnez et al., Antioxidant-prooxidant properties of a new organoselenium compound library,, G. P. Sykiotis and D. Bohmann, Keap1/Nrf2 signaling regulates oxidative stress tolerance and lifespan in Drosophila,, M. Kobayashi and M. Yamamoto, Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species,, M. Kobayashi, N. Iwamoto, Y. Nakajima-Takagi et al., The antioxidant defense system Keap1-Nrf2 comprises a multiple sensing mechanism for responding to a wide range of chemical compounds,. Significance of Glutathione to Plant Adaptation to the The plant glutathione transferase gene family: genomic Igor Azevedo Silva (Editor) Series: Medical Procedures, Testing and Technology. However, by analogy with copper, GSH may be involved in iron reduction, transportation, mobilization from different stores, and incorporation into certain target molecules. . Antioxidants and Antioxidant Enzymes in Higher Plants - Page i These included cytoskeletal proteins (vimentin, myosin, tropomyosin, cofilin, profilin, and actin), metabolic enzymes (enolase, aldolase, 6-phosphoglucolactonase, adenylate kinase, ubiquitin-conjugating enzyme, phosphoglycerate kinase, triose phosphate isomerase and pyrophosphatase), redox enzymes (peroxiredoxin 1, protein disulfide isomerase, and cytochrome c oxidase), cyclophilin, stress proteins (HSP70 and HSP60), nucleophosmin, transgelin, galectin, and fatty acid binding protein. At least two systems are believed to be involved in GSH import into the mitochondria across the inner membrane. The functions of glutathione are manif old but notably . Special sections will deal with GSH functions, such as antioxidant properties and relationship to specific enzymes. GSH has a very complicated pattern of involvement in diverse biological processes. One more important point related to mGSH should also be mentioned here. It is the goal of this project to understand the role of glutathione transferases and their homologues in the biology of both prokaryotes and eukaryotes. In this case, GSH is involved in (i) reduction of Cu2+ to Cu+, (ii) mobilization of copper ions from stores, and (iii) delivery of copper ions during the formation of mature proteins. Clostridium butyricum and Bacillus subtilis, as probiotic bacteria, have been widely used in animal production. This decrease in GSH levels may contribute to chronic diseases such as diabetes mellitus, pulmonary fibrosis, liver fibrosis, cholestatic (reduction in bile flow) liver injury, endotoxemia (microbial products circulating in the blood to cause toxicity), and drug-resistant tumor cells. Glutathione effectively detoxifies heavy metals, pesticides, food preservatives and environmental pollutants other toxic substances, after the liver initially detoxifies them by changing them into free radicals. This emphasizes the need for a clear understanding of the molecular mechanisms of both drug and phytochemical action for the development of new medical strategies. Their key roles in metabolism and defense against oxidative damage have led to thousands of studies over several decades. Glutathione - Wikipedia Sugimoto, M & Takeda, K 2003, ' Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley ', Journal of Molecular Catalysis B: Enzymatic, vol. If the cellular antioxidant potential is high enough, acutely increased ROS levels can be quickly reduced again back to the initial (control) range. 1), is the most important low molecular weight antioxidant synthesized in cells.It is synthesized by the sequential addition of cysteine to glutamate followed by the addition of glycine. Mammalian isoenzymes GPx-1, GPx-2, and GPx-3 reduce H2O2 and peroxides of free fatty acids, whereas GPx-4 reduces peroxides of phospholipids and cholesterol [137]. My Tools, Glutathione Explaining Composition, Forms, and Functions of GSH, The Ratio of GSH to GSSG Changes with Age, Glutathione Regulates the Growth & Division of Cells, Cardamom Elettaria - Identification, Uses, Medicinal, Mercury - Toxicity, Exposure, Body Burden,, Exercise & Fitness: Energy Pathways, Cognition, and Mood, glutathione protects cells from being damaged by free radicals, Glutathione effectively detoxifies heavy metals, amyloid diseases such as Alzheimers disease, BulkSupplements Pure Glutathione Reduced Powder (10 grams), Source Naturals Glutathione Complex 50 mg Tabs, 100 ct, Designs for Health N-Acetyl-L-Cysteine 900mg NAC, Antioxidant Glutathione Precursor for Detox Support, 120 Capsules. Plant cytosolic glutathione transferases (EC 2.5.1.18, GSTs) are essential enzymes involved in multiple and diverse functions which are crucial to xenobiotic detoxification, hormone signalling, redox homeostasis, plant metabolism, growth regulation and adaptation to abiotic and biotic stresses. Many other toxic metabolites are produced as side-products of the normal cellular metabolism. Locally produced extensively modifies specific target proteins, particularly protein disulfide isomerase (PDI). GSH is produced in two steps. D'Autreaux et al., Glutathione revisited: a vital function in iron metabolism and ancillary role in thiol-redox control,, A. Holmgren and R. Sengupta, The use of thiols by ribonucleotide reductase,, M. Mar, A. Morales, A. Colell, C. Garca-Ruiz, and J. C. Fernndez-Checa, Mitochondrial glutathione, a key survival antioxidant,, O. Coll, A. Colell, C. Garca-Ruiz, N. Kaplowitz, and J. C. Fernndez-Checa, Sensitivity of the 2-oxoglutarate carrier to alcohol intake contributes to mitochondrial glutathione depletion,, J. Hu, L. Dong, and C. E. Outten, The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix,, L. H. Lash, Mitochondrial glutathione transport: physiological, pathological and toxicological implications,, A. Meister, Mitochondrial changes associated with glutathione deficiency,, Q. Zhong, D. A. Putt, F. Xu, and L. H. Lash, Hepatic mitochondrial transport of glutathione: studies in isolated rat liver mitochondria and H4IIE rat hepatoma cells,, A. K. Zimmermann, F. A. Loucks, E. K. Schroeder, R. J. Bouchard, K. L. Tyler, and D. A. Linseman, Glutathione binding to the Bcl-2 homology-3 domain groove: a molecular basis for BCL-2 antioxidant function at mitochondria,, L. H. Lash, D. A. Putt, and L. H. Matherly, Protection of NRK-52E cells, a rat renal proximal tubular cell line, from chemical-induced apoptosis by overexpression of a mitochondrial glutathione transporter,, F. Palmieri, Mitochondrial carrier proteins,, A. Colell, C. Garca-Ruiz, M. Miranda et al., Selective glutathione depletion of mitochondria by ethanol sensitizes hepatocytes to tumor necrosis factor,, J. M. Lluis, A. Morales, C. Blasco et al., Critical role of mitochondrial glutathione in the survival of hepatocytes during hypoxia,, H. Rottenberg, D. E. Robertson, and E. Rubin, The effect of temperature and chronic ethanol feeding on the proton electrochemical potential and phosphate potential in rat liver mitochondria,, W. S. Thayer, Effects of ethanol on proteins of mitochondrial membranes,, M. W. Fariss, C. B. Chan, M. Patel, B. Experimentally, the overexpression of certain genes involved in GSH production also may enhance its level. Here we review our recent crystallographic studies of glutathione S-transferases (GSTs) with a particular emphasis on human class pi and theta enzymes. Most information on these mechanisms is associated with the pi-type GSTs (GST). The role of GSH in the function of living organisms is clearly reflected by a phrase coined by Sies [4]the term inevitable GSH. The great importance of GSH has been revealed in multiple experiments either by depletion or repletion of cellular GSH reserves. The major oxidized form of glutathione (i.e., glutathione disulfide, GSSG) consists of two residues of GSH that have been oxidized in such a fashion as to be connected by an intermolecular disulfide bond (Figure 1(b)). Nontoxic biological effects of chromium are also associated with GSH-related transformation of Cr6+. This system is tightly regulated in cells (Figure 5). The remainder of this section focuses only on GSH involvement in the metabolism of chromium, copper, and iron ions. GLUTATHIONE TRANSFERASES John D. Hayes, Jack U. Flanagan, and Ian R. Jowsey Annual Review of Pharmacology and Toxicology THE FUNCTIONS AND REGULATION OF GLUTATHIONE S-TRANSFERASES IN PLANTS Kathleen A. Marrs Annual Review of Plant Physiology and Plant Molecular Biology GLUTATHIONE Alton Meister and Mary E. Anderson The uptake of xenobiotics and their interaction with biomolecules in living organisms depend on various factors such as their chemical and physical properties, type of organism, and its physiological state. Three forms of glutathione, namely, GSH, GSSG, and GSH-conjugates, can be excreted into extracellular spaces. In 1979, a specific inhibitor of GLCL was synthesizedbuthionine sulfoximine (BSO) [13, 14], that when introduced into cells depletes GSH reserves [16, 17, 242]. I want to check melting point of the compound. Glutamate and glycine residues are usually recovered, but the cysteine residues remain conjugated and are lost. This topic is covered in an excellent recent review of Mari et al. Without sufficient levels of active glutathione, our cells and our DNA are likely to be damaged by free radicals. Pungent vanilloids such as capsaicin (trans-8-methyl-N-vanillyl-6-nonenamide), a major pungent of hot chili pepper (Capsicum annuum) [206, 223], and -shogaol from ginger (Zingiber officinale) also activate phase II detoxification enzyme expression in a Nrf2-dependent manner [207]. Certainly, clinical trials in human populations are the final step before introduction of certain drugs. Abstract. Exposure of cysteine residues of proteins to ROS leads to their oxidation with the consequent formation of stable sulfenic, sulfinic, or sulfonic acid derivatives and unstable transient forms (Figure 6). In other words, global analysis of the whole tissue may give incorrect assessments of glutathione status in different cell types. Most of the time, more GSH is built in the liver, the organ of our body responsible for detoxification. They are frequently regulated at the transcriptional level via enhanced Nrf2 binding to ARE/EpRE DNA elements. Its chemical formula is HO 2 CCH (NH 2 )CH 2 SH. Other pathologies, such as several diseases of the lungs (e.g., chronic pulmonary disease, acute respiratory distress syndrome, neonatal lung damage, and asthma) and of the immune system are also associated with a compromised mitochondrial GSH system [6062]. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily Biochem J . It should be noted that GSNO and other nitrosothiols can be used for storage and transportation of because as unstable compounds they can be decomposed easily to generate and GSSG. As an electrophile, sulforaphane directly interacts with protein thiols forming thionoacyl adducts. Activation of the transcription of genes encoding enzymes that combat xenobiotics is one of the main pharmacological strategies for treating xenobiotic-induced diseases. Phase II detoxification enzymes catalyze conjugation reactions that add glutathione, amino acids, sulphate, glucuronic, acetyl, or methyl residues to activated xenobiotics. GSH is formed from glutamate, cysteine, and glycine (Figure 1(a)), but it possesses an unusual peptide bond. As mentioned above, GPx catalyzes the GSH-dependent reduction of many peroxides (reaction (6)). OxyR-related regulatory protein was described in bacteria about 20 years ago (reviewed in [153158]). Many proteins are subject to glutathionylation and some of them lose biological activity as the result, whereas others may be activated [182]. Cysteine is sulphur containing semi-essential amino acid which is significant for making protein, and for performing other metabolic functions. Glutathione s-transferases (GSTs) are a class of enzymes that perform a wide array of biological functions. The products, namely, amino acids and -glutamyl amino acids, may be transported back into cells and used for GSH resynthesis or other needs. GSH-dependent reduction of results in the formation of Cr3+, effectively converting the ion from an anionic form (or ) to a cationic form [82, 120]. Glutathione is a tripeptide of 3 amino acids Glutamic acid Cysteine glycineIt is synthesised in the cytosol. Giulivi C, Zhang Y, Omanska-Klusek A, Ross-Inta C, Wong S, Hertz-Picciotto I, Tassone F, Pessah IN. The above compounds are used as precursors for GSH biosynthesis, both experimentally and in some therapies; for example, NAC is broadly used in therapies that combat HIV [259261] and other infections [262264]. They allow rapid testing of diverse potential compounds at low cost. These two enzymes are not the only cellular NADPH producers. Phase I enzymes are represented by hydroxylases such as endoplasmic reticulum members of the cytochrome P450 family, which introduce oxygen onto molecules of hydrophobic xenobiotics and endogenous compounds, transforming them in more hydrophilic forms. GSH was not required for iron adsorption, delivery to mitochondria, maintenance of mitochondrial Fe,S-proteins, or for their maturation. Glutathione S-Transferase Basics. Mammalian GSTO1-1 has been found to play a previously unappreciated role in the glutathionylation cycle that is emerging as significant mechanism regulating protein function. Higher eukaryotes mainly utilize GGT for glutathione degradation, and mammalian GGTs have implications in many physiological disorders also. Do note that it was observed that old people who live longer than other old people generally had higher levels of GSH than normal for their age group. An increase in cellular levels of mixed disulfides formed between GSH and protein thiols, a process called glutathionylation, was demonstrated to be caused by oxidative stress about three decades ago [169171]. Glutathione (GSH) participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. A broad spectrum of substances have been reported that exhibit chemopreventive potential, and it is noticeable that many of these substances were identified in plants, particularly those that are medicinal and/or edible. how I can determine this enthalpy??? Glutathione is a substance that acts as an antioxidant in the body to deter and protect from free radicals, molecules that can damage the cell. Because of the above caveats, modern pharmacology research has refocused on natural products, mainly of plant origin, although bacteria, fungi, and animal sources cannot be ignored. students Structure And Function Of Glutathione S Transferases|Bengt Mannervik and making them come back for more essays. Glutathione: characteristics, structure, functions, biosynthesis The glutathione (GH) i a mall tripeptide molecule (with only three amino acid reidue) non-protein that participate in many biological phenomena uch a enzyme mechanic, macromolecule bioynthei, intermed This issue is not so straightforward, because formation of this dithiol can be implicated in the regulation of some metabolic pathways. The goal of this text is to focus readers attention on three major areas; the origin and localization of GSH in the nervous system; the multiple effects of GSH on neural health activity; and the potential for alterations on GSH status to Technically N-L-gamma-glutamyl-cysteinyl glycine or L-glutathione, the molecule has a sulfhydryl (SH) group on the cysteinyl portion, which accounts for its . Specifically, glutathione protects cells from being damaged by free radicals that are produced as a by-product of chemical oxidation. Orders of are accepted for higher levels only (University, Master's, PHD). Arthropod Glutathione S-transferases (GSTs) constitute a large family of multifunctional enzymes that are mainly associated with xenobiotic or stress adaptation. structural communications Acta Crystallographica Section F Structural Biology The role of a topologically conserved isoleucine in and Crystallization glutathione transferase structure, stability and Communications function ISSN 1744-3091 Ikechukwu Achilonu,a Samantha The common fold shared by members of the glutathione-transferase (GST) Gildenhuys,a Loren Fisher,a family has a topologically . The development of molecular biological tools and production of lines with deleted genes or chimeric lines may also provide some additional information. It prevents our cellular components from being damaged by free radicals and substances that generate free radicals, such as heavy metals. Many details of GSH involvement in these processes including regulation of GSH-related enzymes were discussed above. For example, CoASSG was found to inhibit GR [185], phosphofructokinase [186], and fatty acid synthase [187], whereas fructose-1,6-bisphosphatase was activated by CoASSG [188]. Firstly, they are mainly localized in different cellular compartmentsGPxs are cytosolic residents, whereas catalases are found mainly in peroxisomes. Not surprisingly, therefore, a decrease in mGSH levels is closely associated with certain pathologies in both humans and animals. Overall, glutathione peroxidase is not required for cell survival. It has been coined by Dr. Mark Hyman as "the mother of all antioxidants" as it plays a role in neutralizing free radicals eliminating toxins from the body.1 Glutathione is highly concentrated in . Due to the pivotal role of mitochondria in programmed cell death (apoptosis) as well as extensive ROS involvement in this process, and adding the fact that mitochondria produce over 90% of cellular ROS, the role of GSH in cell protection cannot be overestimated. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. There is a large body of data indicating that this is an important role of GSH in normal intestinal function. One of its racemates was teratogenic [275]. Some phytochemicals also directly interact with electrophiles, but their action may also be realized through activation of GSH synthesis/resynthesis and reduction. The sulfhydryl group (SH) of the cysteine is involved in reduction and conjugation reactions that are . [Europe PMC free article] [Google Scholar] Animal models also have some limitations, both technical and ethical. General strategies involve specific inhibition of GLCL, a key enzyme of GSH biosynthesis, and depletion of cellular reserves by externally added electrophiles (usually for research purposes). Does an SSD or HDD Consume More Power for Your Computer? For example, in many solid tumors enhanced resistance to drugs is associated with the increased activity of GSTs that detoxify xenobiotics [27, 146]. However, more frequently the oxidation may inhibit certain proteins if the oxidized cysteine residues are important for protein function. [38] and readers are directed to this review for extensive details. Since mitochondria have a very small volume, the local GSH concentration in these organelles is usually higher than that in the cytosol. A very potent vasoconstrictory effect of CoASSG has also been described [189]. 1. However, under various circumstances the steady-state ROS level increases leading to oxidative damage to the cell, called oxidative stress, the term first defined by Sies [83] Oxidative stress came to denote a disturbance in the prooxidant-antioxidant balance in favor of the former. The definition was later expanded to An imbalance between oxidants and antioxidants in favour of the oxidants, potentially leading to damage, is termed oxidative stress to emphasize the damage to certain cellular components [84]. Upregulation of this process provides an additional mechanism for GSH maintenance in the cell. A total of 330 TaGST genes were identified from the wheat genome and named according to the . Many biological processes and their regulation are highly conserved in eukaryotes, particularly from yeasts through insects and to vertebrates. It is a thermostable protein as it retains 100% of its function up to 65 degrees Celsius attributing to the importance of its function in the cell . I believe that NAC has a wide range of action for neurological problems. The omega class of glutathione transferases (GSTs) is a relatively ancient member of the cytosolic GST superfamily, and the omega-class GSTs are found in plants, animals, and some microbial species. The present book mainly deals with the information gained through the cross-talks and inter-relationship studies on the physiological, biochemical and molecular aspects of the cumulative response of various components of AsA-GSH pathway to They include activation of GSH biosynthesis via supplementation of substrates and energy, increased enzymatic potential to produce GSH and reduce GSSG, increased activities of detoxification enzymes that use GSH, and activation of routes for extrusion of GSSG and glutathione S-conjugates from cells. The tripeptide, -l-glutamyl-l-cysteinyl-glycine known as glutathione (GSH) (Fig. When there is a decrease in the level of GSH inside & outside of our cells, our cells detect this and respond by producing more enzymes that increase the synthesis of glutathione & glutathione peroxide. A. Ross, O. J. Figure 7 shows general routes of enhanced ROS levels and/or the presence of xenobiotics associated with various pathologies. In this second edition, Edwin Frankel has updated and extended his now well-known book Lipid oxidation which has come to be regarded as the standard work on the subject since the publication of the first edition seven years previously. Glutathione is our body's master antioxidant. Glutathione is an important reduc. These GSTs do not possess a selenocysteine residue in their active site. Structure And Function Of Glutathione S Transferases|Bengt Mannervik, The Maya Forest Garden: Eight Millennia of Sustainable Cultivation of the Tropical Woodlands (New Frontiers in Historical Ecology)|Ronald Nigh, Bequest for Nathan|Lois Casto, The cancellations of Hungarian post offices on the first five issues of Austrian stamps, 1850-67, during the Austrian administration|G. GSH can interact directly with ROS to reduce their levels and in this manner delay the development of pathologies. Conjugation with endogenous and exogenous electrophiles consumes a substantial portion of cellular GSH. Innumerable studies have shown that GSH is an antioxidant. Under control conditions, steady-state ROS levels fluctuate over a certain range [81, 82, 85]. Although the full range of biological functions of catalase still remains unclear, its main function is the decomposition of hydrogen peroxide into water and oxygen. These approaches have helped researchers investigate the function of cellular GSH. Many potential effectors can exist in several forms and chemical synthesis may lead to the production of, for example, mixtures of different racemates or diastereoisomers, some of which may be pharmaceutically effective, but others of which may cause deleterious effects such as what occurred with thalidomide. The routes leading to the formation of mixed disulfides are interactions between: (i) sulfenic acid derivatives and GSH, (ii) GSSG and protein cysteine residues, (iii) protein cysteine residues and glutathione sulfenate, and, finally (iv) protein cysteine residues and glutathione disulfide S-oxide. 2008-2021 ResearchGate GmbH. Glutathione is a naturally occurring tripeptide comprised of three amino acids (cysteine, glutamic acid, and glycine) acts as an antioxidant, a free radical scavenger and a detoxifying agent. In the cell, GSH is synthesized and mostly distributed in the cytoplasm, while in less amount, it is also found in the . This provides the basis for recycling of excreted GSH and GSSG (salvage cycle) by the cell of origin or by other cells [34]. Carnosol, an orthophenolic diterpene found in rosemary (Rosmarinus officinalis), also enhances the expression of phase II detoxification enzyme genes in an Nrf2-related manner [228]. and electrophiles or by operating as a cofactor for various enzymes . The potential of various phytochemicals to disrupt this link between ROS elevation and increased pathology may be related to the inherent antioxidant activity possessed by various plant components. B. Owen, A. T. Dinkova-Kostova, and D. A. Butterfield, Nitric oxide in cell survival: a Janus molecule,, H. L. Chang, P. C. Dedon, and W. M. Deen, Kinetic Analysis of Intracellular Concentrations of Reactive Nitrogen Species,, B. Kalyanaraman, H. Karoui, R. J. Singh, and C. C. Felix, Detection of thiyl radical adducts formed during hydroxyl radical- and peroxynitrite-mediated oxidation of thiolsa high resolution ESR spin- trapping study at Q-band (35 Ghz),, M. J. Meredith, C. L. Cusick, S. Soltaninassab, K. S. Sekhar, S. Lu, and M. L. Freeman, Expression of Bcl-2 increases intracellular glutathione by inhibiting methionine-dependent GSH efflux,, A. J. L. Cooper and M. H. Hanigan, 4.17Enzymes involved in processing glutathione conjugates, in, A. J. L. Cooper, W. A. Pulsinelli, and T. E. Duffy, Glutathione and ascorbate during ischemia and postischemic reperfusion in rat brain,, C. Kumar, A. Igbaria, B. The primary GSH function here is directed to detoxification of injurious external agents to prevent damage to the organism.
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