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Glutathione - or L-Glutathione - is a powerful antioxidant found within every cell. Glutathione plays a role in nutrient metabolism, and regulation of cellular events (including gene expression, DNA and protein synthesis, cell growth, buffering acids and immune response).
Three amino acids (cysteine, glutamate, and glycine) combine to form part of the powerful natural antioxidant Glutathione peroxidase that in turn is found in every cell in our body. Glutathione peroxidase plays a variety of roles in cells, including DNA synthesis and repair, metabolism of toxins/acids and carcinogens, enhancement of the immune system, and prevention of fat oxidation.
Glutathione is predominantly known as the super antioxidant protecting our cells from damage caused by free radicals, pollutants or toxins we come in contact with every day. Glutathione also helps other supporting antioxidants found in cells stay in their active form and unlike other antioxidants Glutathione actually recycles itself after removing toxins from our cells.
Glutathione levels have been found to be lower in patients suffering from most serious chronic diseases. Researchers understand that there is a direct link between over all health and high Glutathione levels and new research continues to find the best avenues to increase Glutathione levels in our bodies.
Over 100,000 research studies at PubMed.gov on how Glutathione affects a myriad of diseases.
Study of Glutathione, Vitamin C and Cysteine in Children With Autism and Severe Behavior Problems
Sponsor: University of Louisville
Collaborators: Kosair Children’s Hospital Foundation,
Cumberland Pharmaceuticals
Start date April 2009
Estimated Study Completion Date: December 2012
PRIMARY OUTCOME MEASURES:
Improvement in both developmental skills and behavior with either glutathione or glutathione, Vitamin C and N-acetylcysteine therapy as compared to placebo therapy. Subjects will also be monitored using clinical and laboratory safety parameters. [ Time Frame: 4 months ] [ Designated as safety issue: Yes ]
Improvement in both developmental skills and behavior measured using validated scales in subjects receiving either glutathione, glutathione/Vitamin C/N-acetylcysteine or placebo measured at baseline, 9 weeks and at the end of study in a double-blind cross-over design.
Blood glutathione as a marker of cardiac allograft vasculopathy in heart transplant recipients.
De Chiara B1, Bigi R, Campolo J, Parolini M, Turazza F, Masciocco G, Frigerio M, Fiorentini C, Parodi O.
BACKGROUND:
Cardiac allograft vasculopathy (CAV) limits survival after heart transplantation (HTx). Between immunologic and non-immunologic factors, reactive oxygen species generation has been proposed as pathogenetic mechanism. This study was aimed at evaluating redox status in HTx recipients and verifying whether it could be independently associated with CAV.
METHODS:
Fifty-five consecutive male HTx recipients, median [interquartile range] age 60 yr [50, 64], underwent angiography 67 months [21, 97] after HTx to assess CAV, defined as significant stenosis in >or=1 epicardial vessel or any distal vessel attenuation. All patients underwent blood sampling 89 months [67, 119] after HTx for biochemical (glucose, creatinine, total and LDL cholesterol, and cyclosporin levels) and redox evaluation [plasma reduced and total homocysteine, cysteine, cysteinylglycine, glutathione, blood reduced glutathione (GSH(bl)) and vitamin E]. Univariate Odds Ratios (OR) with 95% confidence interval (95% CI, highest vs. lowest quartile) were estimated on the basis of a logistic regression analysis between clinical, conventional biochemical and redox data. Only the significant variables at univariate entered into multivariate analysis.
RESULTS:
CAV was documented in 15 (27%) patients. Univariate analysis showed that time from HTx to angiography (OR 3.97, 95% CI 1.15-14, p = 0.03) and GSH(bl) (OR 0.31, 95% CI: 0.14-0.70, p = 0.005) were significantly associated with CAV. However, multivariate analysis revealed GSH(bl) as the only independent predictor of CAV (OR 0.31, 95% CI: 0.13-0.74, p = 0.008).
CONCLUSIONS:
In HTx recipients reduced levels of GSH(bl) are independently associated with CAV. Given its potent intracellular scavenger properties, GSH(bl) may serve as a marker of antioxidant defence consumption, favouring CAV development.
Beta-amyloidolysis and glutathione in Alzheimer's disease
Lasierra-Cirujeda J, Coronel P, Aza M, Gimeno M.
Source
CM Hematológico SC, Logroño, La Rioja, Spain.
Acetaminophen-InducedHepatotoxicity
James LP, Mayeux PR, Hinson JA.
Source Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.jameslaurap@uams.edu
ABSTRACT:
The analgesic acetaminophen causes a potentially fatal, hepatic centrilobular necrosis when taken in overdose. The initial phases of toxicity were described in Dr. Gillette's laboratory in the 1970s. These findings indicated that acetaminophen was metabolically activated by cytochrome P450 enzymes to a reactive metabolite that depleted glutathione (GSH) and covalently bound to protein. It was shown that repletion of GSH prevented the toxicity. This finding led to the development of the currently used antidote N-acetylcysteine. The reactive metabolite was subsequently identified to be N-acetyl-p-benzoquinone imine (NAPQI). Although covalent binding has been shown to be an excellent correlate of toxicity, a number of other events have been shown to occur and are likely important in the initiation and repair of toxicity. Recent data have shown that nitrated tyrosine residues as well as acetaminophen adducts occur in the necrotic cells following toxic doses of acetaminophen. Nitrotyrosine was postulated to be mediated by peroxynitrite, a reactive nitrogen species formed by the very rapid reaction of superoxide and nitric oxide (NO). Peroxynitrite is normally detoxified by GSH, which is depleted in acetaminophen toxicity. NO synthesis (serum nitrate plus nitrite) was dramatically increased following acetaminophen. In inducible nitric oxide synthase (iNOS) knockout mice, acetaminophen did not increase NO synthesis or tyrosine nitration; however, histological evidence indicated no difference in toxicity. Acetaminophen did not cause hepatic lipid peroxidation in wild-type mice but did cause lipid peroxidation in iNOS knockout mice. These data suggest that NO may play a role in controlling lipid peroxidation and that reactive nitrogen/oxygen species may be important in toxicity. The source of the superoxide has not been identified, but our recent finding that NADPH oxidase knockout mice were equally sensitive to acetaminophen and had equal nitration of tyrosine suggests that the superoxide is not from the activation of Kupffer cells. It was postulated that NAPQI-mediated mitochondrial injury may be the source of the superoxide. In addition, the significance of cytokines and chemokines in the development of toxicity and repair processes has been demonstrated by several recent studies. IL-1beta is increased early in acetaminophen toxicity and may be important in iNOS induction. Other cytokines, such as IL-10, macrophage inhibitory protein-2 (MIP-2), and monocyte chemoattractant protein-1 (MCP-1), appear to be involved in hepatocyte repair and the regulation of proinflammatory cytokines.
Redox Control of Cell Death
Ueda S, Masutani H, Nakamura H, Tanaka T, Ueno M, Yodoi J.
Source: Department of Biological Responses, Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.
ABSTRACT:
Cellular redox is controlled by the thioredoxin (Trx) and glutathione (GSH) systems that scavenge harmful intracellular reactive oxygen species (ROS). Oxidative stress also evokes many intracellular events including apoptosis. There are two major pathways through which apoptosis is induced; one involves death receptors and is exemplified by Fas-mediated caspase-8 activation, and another is the stress- or mitochondria-mediated caspase-9 activation pathway. Both pathways converge on caspase-3 activation, resulting in nuclear degradation and cellular morphological change. Oxidative stress induces cytochrome c release from mitochondria and activation of caspases, p53, and kinases, including apoptosis signal-regulating kinase 1 (ASK1), c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase. Trx inhibits apoptosis signaling not only by scavenging intracellular ROS in cooperation with the GSH system, but also by inhibiting the activity of ASK1 and p38. Mitochondria-specific thioredoxin (Trx-2) and Trx peroxidases (peroxiredoxins) are suggested to regulate cytochrome c release from mitochondria, which is a critical early step in the apoptotis-signaling pathway. dATP/ATP and reducing factors including Trx determine the manifestation of cell death, apoptosis or necrosis, by regulating the activation process and the activity of redox-sensitive caspases. As mitochondria are the most redox-active organelle and indispensable for cells to initiate or inhibit the apoptosis process, the regulation of mitochondrial function is the central focus in the research field of apoptosis and redox.
Signalling Apoptosis:
A Radical Approach
Carmody RJ, Cotter TG.
Source: Department of Molecular and Cellular Engineering, Institute for Human Gene Therapy, University of Pennsylvania School of Medicine, Philadelphia 19104, USA
ABSTRACT:
Reactive oxygen species (ROS) are frequently associated with cytotoxicity, often being described as damaging, harmful or toxic. It is generally assumed that, under pathological circumstances, ROS elicit wide-spread and random acts of oxidation. This passive attack of cellular components by ROS, in conditions where oxidative stress is the initiating stimulus for apoptosis, is assumed to simply trigger cell death as a result of cumulative oxidative damage. However, accumulating evidence now suggests that ROS may act as signalling molecules for the initiation and execution of the apoptotic death programme in many, if not all, current models of apoptotic cell death. Signalling by ROS would not appear to be random, as previously assumed, but targeted at specific metabolic and signal transduction cellular components. There is also evidence that the enzymatic generation of ROS may not simply be an unwanted by-product of the primary reaction catalysed, but that ROS may be used as signalling molecules to regulate cellular processes including apoptosis. This view of ROS as signalling molecules (as opposed to toxic metabolites) has been further bolstered by the findings that cellular antioxidants such as glutathione and thioredoxin not only serve to regulate ROS levels but also act as reversible redox modifiers of enzyme function. This review will attempt to delineate the involvement of ROS in apoptosis in light of these recent discoveries and provide evidence for a crucial role for ROS in the initiation and execution of the death process.
Redox Regulation of
Hepatocyte Apoptosis
Garcia-Ruiz C, Fernández-Checa JC.
Source: Liver Unit, Hospital Clínic, C/Villarroel, Barcelona, Spain. checa229@yahoo.com
Erratum in: J Gastroenterol Hepatol. 2008 Mar;23(3):501-2.
ABSTRACT:
Cell death can be regulated by the sensitivity of proteins with a functional role in death pathways to redox environment. The antioxidant glutathione (GSH) regulates cell death pathways by modulating the redox state of specific thiol residues of target proteins including transcription factors, stress kinases and caspases, which participate in tumor necrosis factor (TNF)-induced apoptosis. The TNF signals, upon its binding to its type 1 receptor, two simultaneous pathways with opposing functions, promoting cell survival through NF-kappaB activation or cell death through mitochondria. As a consequence, hepatocytes are resistant to TNF unless the survival arm is neutralized, therefore, rendering hepatocytes sensitive to TNF. Cytosol GSH regulates TNF hepatocyte apoptosis by modulating caspase 8 activation or NF-kappaB-dependent gene expression. However, mitochondrial GSH controls hepatocyte susceptibility to TNF through modulation of reactive oxygen species, without inactivation of NF-kappaB-dependent survival pathways. So, understanding the role of mitochondrial reactive oxygen species in TNF-induced hepatocyte death may have broad implications in the pathogenesis of acute and chronic liver diseases.
Glutathione in Liver Diseases
and Hepatotoxicity
Yuan L, Kaplowitz N.
Source: Internal Medicine, University of Southern California, USA.
ABSTRACT:
Glutathione (GSH) is a major antioxidant as well as redox and cell signaling regulator. GSH guards cells against oxidative injury by reducing H(2)O(2) and scavenging reactive oxygen and nitrogen radicals. In addition, GSH-induced redox shift with or without ROS subjects some cellular proteins to varied forms of oxidation, altering the function of signal transduction and transcription factor molecules. Increasing evidence supports the important role of ROS and GSH in modulating multiple signaling pathways. TNF-alpha and Fas signaling, NF-kappaB, JNK and mitochondrial apoptotic pathways are the focus of this review. The redox regulation either can switch on/off or regulate the threshold for some crucial events in these pathways. Notably, mitochondrial GSH depletion induces increased mitochondrial ROS exposure which impairs bioenergetics and promotes mitochondrial permeability transition pore opening which is critical for cell death. Depending on the extent of mitochondrial damage, NF-kappaB inhibition and JNK activation, hepatocytes may either undergo different modes of cell death (apoptosis or necrosis) or be sensitized to cell-death stimuli (i.e. TNF-alpha). These processes have been implicated in the pathogenesis of many liver diseases.
Glutathione in Health and Disease: Pharmacotherapeutic Issues
Ann Pharmacother. 1995 Dec;29(12):1263-73.
Lomaestro BM, Malone M.
Source: Department of Pharmacy, Albany Medical Center, Hospital, NY 12208, USA.
OBJECTIVE:
To review the current research and importance of glutathione (GSH) therapy in health and disease and to provide a basic overview of the widespread use and interest in this compound.
DATA IDENTIFICATION:
Articles were obtained via a MEDLINE search of the term glutathione in conjunction with specific disease states mentioned, and via extensive review of references found in articles identified by computer search.
STUDY SELECTION:
Emphasis was placed on the most recent research, human research, and in discussing multiple disease states.
DATA EXTRACTION:
The literature was reviewed for methodology, quality, and practical aspects of interest to clinical pharmacists.
DATA SYNTHESIS:
GSH is a tripeptide of extreme importance as a catalyst, reductant, and reactant. It continues to be investigated in diverse areas such as acute respiratory distress syndrome, toxicology, AIDS, aging, oncology, and liver disease. Despite the widespread clinical interest in GSH, we were not able to identify an in-depth review of this compound in the pharmacy literature.
CONCLUSIONS:
The list of potential indications for modulation of GSH is extensive and broad. This review introduces clinicians to what GSH is, its basic chemistry, and some areas of active research.
Evidence of Oxidative Damage and Inflammation Associated With Low Glutathione Redox Status in the Autism Brain
Transl Psychiatry. 2012 Jul 10;2:e134. doi: 10.1038/tp.2012.61.
Rose S, Melnyk S, Pavliv O, Bai S, Nick TG, Frye RE, James SJ.
Source: Department of Pediatrics, University of Arkansas for Medical Sciences, Arkansas Children's Hospital Research Institute, Little Rock, AR 72202, USA. srose@uams.edu
Despite increasing evidence of oxidative stress in the pathophysiology of autism, most studies have not evaluated biomarkers within specific brain regions, and the functional consequences of oxidative stress remain relatively understudied. We examined frozen samples from the cerebellum and temporal cortex (Brodmann area 22 (BA22)) from individuals with autism and unaffected controls (n=15 and n=12 per group, respectively).
Biomarkers of oxidative stress, including reduced glutathione (GSH), oxidized glutathione (GSSG) and glutathione redox/antioxidant capacity (GSH/GSSG), were measured. Biomarkers of oxidative protein damage (3-nitrotyrosine; 3-NT) and oxidative DNA damage (8-oxo-deoxyguanosine; 8-oxo-dG) were also assessed. Functional indicators of oxidative stress included relative levels of 3-chlorotyrosine (3-CT), an established biomarker of a chronic inflammatory response, and aconitase activity, a biomarker of mitochondrial superoxide production.
Consistent with previous studies on plasma and immune cells, GSH and GSH/GSSG were significantly decreased in both autism cerebellum (P<0.01) and BA22 (P<0.01). There was a significant increase in 3-NT in the autism cerebellum and BA22 (P<0.01). Similarly, 8-oxo-dG was significantly increased in autism cerebellum and BA22 (P<0.01 and P=0.01, respectively), and was inversely correlated with GSH/GSSG in the cerebellum (P<0.01). There was a significant increase in 3-CT levels in both brain regions (P<0.01), whereas aconitase activity was significantly decreased in autism cerebellum (P<0.01), and was negatively correlated with GSH/GSSG (P=0.01).
Together, these results indicate that decreased GSH/GSSG redox/antioxidant capacity and increased oxidative stress in the autism brain may have functional consequence in terms of a chronic inflammatory response, increased mitochondrial superoxide production, and oxidative protein and DNA damage.
ABSTRACT:
In this review, we hypothesized the importance of the interaction between the brain glutathione (GSH) system, the proteolytic tissue plasminogen activator (t-PA)/plasminogen/ plasmin system, regulated by plasminogen activator inhibitor (PAI-1), and neuroserpin in the pathogenesis of Alzheimer's disease. The histopathological characteristic hallmark that gives personality to the diagnosis of Alzheimer's disease is the accumulation of neurofibroid tangles located intracellularly in the brain, such as the protein tau and extracellular senile plaques made primarily of amyloidal substance. These formations of complex etiology are intimately related to GSH, brain protective antioxidants, and the proteolytic system, in which t-PA plays a key role. There is scientific evidence that suggests a relationship between aging, a number of neurodegenerative disorders, and the excessive production of reactive oxygen species and accompanying decreased brain proteolysis. The plasminogen system in the brain is an essential proteolytic mechanism that effectively degrades amyloid peptides ("beta-amyloidolysis") through action of the plasmin, and this physiologic process may be considered to be a means of prevention of neurodegenerative disorders. In parallel to the decrease in GSH levels seen in aging, there is also a decrease in plasmin brain activity and a progressive decrease of t-PA activity, caused by a decrease in the expression of the t-PA together with an increase of the PAI-1 levels, which rise to an increment in the production of amyloid peptides and a lesser clearance of them. Better knowledge of the GSH mechanism and cerebral proteolysis will allow us to hypothesize about therapeutic practices.
KEYWORDS:
Alzheimer’s disease, PAI-1, glutathione, plasminogen, t-PA
Enzymatic Product-Mediated Stabilization of CdS Quantum Dots Produced In Situ: Application for Detection of Reduced Glutathione, NADPH, and Glutathione Reductase Activity
Garai-Ibabe G, Saa L, Pavlov V.
Source
CICbiomaGUNE, Parque Tecnológico de San Sebastián, Paseo Miramón 182, 20009, Donostia-San Sebastián, Spain.
ABSTRACT:
Glutathione is the most abundant nonprotein molecule in the cell and plays an important role in many biological processes, including the maintenance of intracellular redox states, detoxification, and metabolism. Furthermore, glutathione levels have been linked to several human diseases, such as AIDS, Alzheimer disease, alcoholic liver disease, cardiovascular disease, diabetes mellitus, and cancer. A novel concept in bioanalysis is introduced and applied to the highly sensitive and inexpensive detection of reduced glutathione (GSH), over its oxidized form (GSSG), and glutathione reductase (GR) in human serum. This new fluorogenic bioanalytical system is based on the GSH-mediated stabilization of growing CdS nanoparticles. The sensitivity of this new assay is 5 pM of GR, which is 3 orders of magnitude better than other fluorogenic methods previously reported.
Glutathione Depletion
and Oxidative Stress
Parkinsonism Relat Disord. 2002 Sep;8(6):385-7.
Mytilineou C, Kramer BC, Yabut JA.
Source: Department of Neurology, Mount Sinai School of Medicine, Box 1137, New York, NY 10029, USA.catherine.mytilneou@mssm.edu
Oxidative stress is believed to contribute to the pathogenesis of Parkinson's disease. One of the indices of oxidative stress is the depletion of the antioxidant glutathione (GSH), which may occur early in the development of Parkinson's disease. To study the role of GSH depletion in the survival of dopamine neurons we treated mesencephalic cultures with the GSH synthesis inhibitor L-buthionine sulfoximine.
Our studies have shown that the depletion of GSH causes a cascade of events, which ultimately may result in cell death. An early event following GSH depletion is a phospholipase A(2)-dependent release of arachidonic acid. Arachidonic acid can cause damage to the GSH-depleted cells through its metabolism by lipoxygenase. The generation of superoxide radicals during the metabolism of arachidonic acid is likely to play an important role in the toxic events that follow GSH depletion.
Glutathione Metabolism and its Implications for Health
J Nutr. 2004 Mar;134(3):489-92.
Wu G, Fang YZ, Yang S, Lupton JR, Turner ND.
Source: Faculty of Nutrition, Texas A&M University, College Station, TX, 77843, USA. g-wu@tamu.edu
Glutathione (gamma-glutamyl-cysteinyl-glycine; GSH) is the most abundant low-molecular-weight thiol, and GSH/glutathione disulfide is the major redox couple in animal cells. The synthesis of GSH from glutamate, cysteine, and glycine is catalyzed sequentially by two cytosolic enzymes, gamma-glutamylcysteine synthetase and GSH synthetase.
Compelling evidence shows that GSH synthesis is regulated primarily by gamma-glutamylcysteine synthetase activity, cysteine availability, and GSH feedback inhibition. Animal and human studies demonstrate that adequate protein nutrition is crucial for the maintenance of GSH homeostasis.
In addition, enteral or parenteral cystine, methionine, N-acetyl-cysteine, and L-2-oxothiazolidine-4-carboxylate are effective precursors of cysteine for tissue GSH synthesis. Glutathione plays important roles in antioxidant defense, nutrient metabolism, and regulation of cellular events (including gene expression, DNA and protein synthesis, cell proliferation and apoptosis, signal transduction, cytokine production and immune response, and protein glutathionylation).
Glutathione deficiency contributes to oxidative stress, which plays a key role in aging and the pathogenesis of many diseases (including kwashiorkor, seizure, Alzheimer's disease, Parkinson's disease, liver disease, cystic fibrosis, sickle cell anemia, HIV, AIDS, cancer, heart attack, stroke, and diabetes). New knowledge of the nutritional regulation of GSH metabolism is critical for the development of effective strategies to improve health and to treat these diseases.
A Clinical Trial of Glutathione Supplementation in Autism Spectrum Disorders
Med Sci Monit. 2011 Dec;17(12):CR677-82.
Kern JK, Geier DA, Adams JB, Garver CR, Audhya T, Geier MR.
Source: Genetic Consultants of Dallas, Allen, TX, USA.
BACKGROUND:
Recent evidence shows that subjects diagnosed with an autism spectrum disorder (ASD) have significantly lower levels of glutathione than typically developing children. The purpose of this study was to examine the use of two commonly used glutathione supplements in subjects diagnosed with an ASD to determine their efficacy in increasing blood glutathione levels in subjects diagnosed with an ASD.
MATERIAL/METHODS:
The study was an eight-week, open-label trial using oral lipoceutical glutathione (n=13) or transdermal glutathione (n=13) in children, 3-13 years of age, with a diagnosis of an ASD. Subjects underwent pre- and post-treatment lab testing to evaluate plasma reduced glutathione, oxidized glutathione, cysteine, taurine, free and total sulfate, and whole-blood glutathione levels.
RESULTS:
The oral treatment group showed significant increases in plasma-reduced glutathione, but not whole-blood glutathione levels following supplementation. Both the oral and transdermal treatment groups showed significant increases in plasma sulfate, cysteine, and taurine following supplementation.
CONCLUSIONS:
The results suggest that oral and transdermal glutathione supplementation may have some benefit in improving some of the transsulfuration metabolites. Future studies among subjects diagnosed with an ASD should further explore the pharmacokinetics of glutathione supplementation and evaluate the potential effects of glutathione supplementation upon clinical symptoms.
Increased Skin Papilloma Formation in Mice Lacking Glutathione Transferase GSTP
Cancer Res. 2011 Nov 15;71(22):7048-60. Epub 2011 Oct 5.
Henderson CJ, Ritchie KJ, McLaren A, Chakravarty P, Wolf CR.
Source: Cancer Research UK Molecular Pharmacology Unit, Medical Research Institute, Ninewells Hospital & Medical School, Dundee, United Kingdom.
The glutathione S-transferase GSTP is overexpressed in many human cancers and chemotherapy-resistant cancer cells, where there is evidence that GSTP may have additional functions beyond its known catalytic role. On the basis of evidence that Gstp-deficient mice have a comparatively higher susceptibility to skin carcinogenesis, we investigated whether this phenotype reflected an alteration in carcinogen detoxification or not. For this study, Gstp(-/-) mice were interbred with Tg.AC mice that harbor initiating H-ras mutations in the skin. Gstp(-/-)/Tg.AC mice exposed to the proinflammatory phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) exhibited higher tumor incidence and multiplicity with a significant thickening of skin after treatment, illustrating hyperproliferative growth.
Unexpectedly, we observed no difference in cellular proliferation or apoptosis or in markers of oxidative stress, although higher levels of the inflammatory marker nitrotyrosine were found in Gstp(-/-)/Tg.AC mice. Instead, gene set enrichment analysis of microarray expression data obtained from skin revealed a more proapoptotic and proinflammatory environment shortly after TPA treatment. Within 4 weeks of TPA treatment, Gstp(-/-)/Tg.AC mice displayed altered lipid/sterol metabolism and Wnt signaling along with aberrant processes of cytoskeletal control and epidermal morphogenesis at both early and late times.
In extending the evidence that GSTP has a vital role in normal homeostatic control and cancer prevention, they also strongly encourage the emerging concept that GSTP is a major determinant of the proinflammatory character of the tumor microenvironment. This study shows that the GSTP plays a major role in carcinogenesis distinct from its role in detoxification and provides evidence that the enzyme is a key determinant of the proinflammatory tumor environment.
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