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  1 / 298 MEDLINE  
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PMID:28471109
Autor:Ye SF; Yang Y; Wu L; Ma WW; Zeng HH
Dirección:State Key Laboratory of Natural and Biomimetic Drugs, Peking University, Beijing 100191, China.
Título:Ethaselen: a novel organoselenium anticancer agent targeting thioredoxin reductase 1 reverses cisplatin resistance in drug-resistant K562 cells by inducing apoptosis.
Fuente:J Zhejiang Univ Sci B; 18(5):373-382, 2017 May.
ISSN:1862-1783
País de publicación:China
Idioma:eng
Resumen:It has been reported that Ethaselen shows inhibitory effects on thioredoxin reductase (TrxR) activity and human tumor cell growth. In order to find an efficient way to reverse cisplatin resistance, we investigated the reversal effects of Ethaselen on cisplatin resistance in K562/cisplatin (CDDP) cells that were established by pulse-inducing human erythrocyte leukemic cell line K562, which are fivefold more resistant to cisplatin compared to K562 cells. The morphology and growth showed that the adhesion of K562/CDDP further decreased while the cell volume increased. The proliferation of K562/CDDP is strengthened. The antitumor activities in vitro were assessed by MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) assay and combination index (CI), showing the significant synergic effects of cisplatin and Ethaselen. Focusing on apoptosis, a series of comparisons was made between K562 and K562/CDDP. Cisplatin induced higher reactive oxygen species (ROS) generation in K562 and subsequently induced the formation of mitochondrial permeability transition pores (PTPs). In addition, cisplatin increased the ratio of Bax to Bcl-2 in K562, which can influence the mitochondrial membrane permeability. PTP formation and mitochondrial membrane permeabilization eventually resulted in the release of cytochrome c and activation of the Caspase pathway. However, these effects were not clearly seen in K562/CDDP, which may be the reason for the acquired CDDP resistance. However, Ethaselen can induce a high level of ROS in K562/CDDP by TrxR activity inhibition and increased ratio of Bax to Bcl-2 in K562/CDDP by nuclear factor κB (NF-κB) suppression, which subsequently induces the release of cytochrome c in K562/CDDP. This response is partly responsible for the reversal of the cisplatin resistance in K562/CDDP cells.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 ((1,2-bis(1,2-benzisoselenazolone-3(2H)-ketone))ethane); 0 (Antineoplastic Agents); 0 (Bridged Bicyclo Compounds, Heterocyclic); 0 (Organoselenium Compounds); EC 1.8.1.9 (TXNRD1 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 1); Q20Q21Q62J (Cisplatin)


  2 / 298 MEDLINE  
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PMID:29037867
Autor:Zhuge W; Chen R; Vladimir K; Dong X; Zia K; Sun X; Dai X; Bao M; Shen X; Liang G
Dirección:Chemical Biology Research Center, School of Pharmaceutical Sciences, Wenzhou Medical University, Wenzhou, Zhejiang 325035, China; Department of Gastrointestinal Surgery, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, Zhejiang 325035, China.
Título:Costunolide specifically binds and inhibits thioredoxin reductase 1 to induce apoptosis in colon cancer.
Fuente:Cancer Lett; 412:46-58, 2018 Jan 01.
ISSN:1872-7980
País de publicación:Ireland
Idioma:eng
Resumen:Colon cancer is one of the leading causes of cancer-related deaths. A natural sesquiterpene lactone, costunolide (CTD), showed inhibition of cancer development. However, the underlying mechanisms are not known. Here, we have examined the therapeutic activity and novel mechanisms of the anti-cancer activities of CTD in colon cancer cells. Using SPR analysis and enzyme activity assay on recombinant TrxR1 protein, our results show that CTD directly binds and inhibits the activity of TrxR1, which caused enhanced generation of ROS and led to ROS-dependent endoplasmic reticulum stress and cell apoptosis in colon cancer cells. Overexpression of TrxR1 in HCT116 cells reversed CTD-induced cell apoptosis and ROS increase. CTD treatment of mice implanted with colon cancer cells showed tumor growth inhibition and reduced TrxR1 activity and ROS level. In addition, it was observed that TrxR1 was significantly up-regulated in existing colon cancer gene database and clinically obtained colon cancer tissues. Our studies have uncovered the mechanism underlying the biological activity of CTD in colon cancer and suggest that targeting TrxR1 may prove to be beneficial as a treatment option.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (ATF4 protein, human); 0 (Antineoplastic Agents, Phytogenic); 0 (Reactive Oxygen Species); 0 (Sesquiterpenes); 145891-90-3 (Activating Transcription Factor 4); 4IK578SA7Z (costunolide); EC 1.8.1.9 (Thioredoxin Reductase 1)


  3 / 298 MEDLINE  
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PMID:28931237
Autor:Singh V; Prakhar P; Rajmani RS; Mahadik K; Borbora SM; Balaji KN
Dirección:Department of Microbiology and Cell Biology, Indian Institute of Science.
Título:Histone Methyltransferase SET8 Epigenetically Reprograms Host Immune Responses to Assist Mycobacterial Survival.
Fuente:J Infect Dis; 216(4):477-488, 2017 Aug 15.
ISSN:1537-6613
País de publicación:United States
Idioma:eng
Resumen:NQO1 and TRXR1 are important host reductases implicated in the regulation of inflammation and apoptosis. Although the transcriptional machinery governing these processes have been extensively investigated, the associated epigenetic regulatory events remain unclear. Here, we report that SET8, a histone H4 lysine 20 monomethylase (H4K20me1), is highly induced during Mycobacterium tuberculosis infection that orchestrates immune evasion strategies through the induction of NQO1 and TRXR1 in vivo. SET8, along with FoxO3a, mediates an active NQO1-PGC1-α complex, which promotes the anti-inflammatory M2 macrophage phenotype, and assists TRXR1-regulated arrest of tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis. Strikingly, the loss-of-function analysis in an in vivo mouse tuberculosis model further corroborated the pivotal role of SET8-responsive NQO1 and TRXR1 in mycobacterial survival. Thus, augmenting host immune responses against Mycobacterium tuberculosis by harnessing the SET8-NQO1/TRXR1 axis with its specific and potent inhibitors could lead to promising host-directed therapeutic adjuvants for tuberculosis treatment.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Forkhead Box Protein O3); 0 (FoxO3 protein, mouse); EC 1.6.5.2 (NAD(P)H Dehydrogenase (Quinone)); EC 1.6.5.2 (Nqo1 protein, mouse); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 1.8.1.9 (Txnrd1 protein, mouse); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (SET8 protein, mouse)


  4 / 298 MEDLINE  
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PMID:28684416
Autor:Dagnell M; Pace PE; Cheng Q; Frijhoff J; Östman A; Arnér ESJ; Hampton MB; Winterbourn CC
Dirección:From the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8041, New Zealand.
Título:Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H O exposure.
Fuente:J Biol Chem; 292(35):14371-14380, 2017 Sep 01.
ISSN:1083-351X
País de publicación:United States
Idioma:eng
Resumen:Regulation of growth factor signaling involves reversible inactivation of protein tyrosine phosphatases (PTPs) through the oxidation and reduction of their active site cysteine. However, there is limited mechanistic understanding of these redox events and their co-ordination in the presence of cellular antioxidant networks. Here we investigated interactions between PTP1B and the peroxiredoxin 2 (Prx2)/thioredoxin 1 (Trx1)/thioredoxin reductase 1 (TrxR1) network. We found that Prx2 becomes oxidized in PDGF-treated fibroblasts, but only when TrxR1 has first been inhibited. Using purified proteins, we also found that PTP1B is relatively insensitive to inactivation by H O but found no evidence for a relay mechanism in which Prx2 or Trx1 facilitates PTP1B oxidation. Instead, these proteins prevented PTP1B inactivation by H O Intriguingly, we discovered that TrxR1/NADPH directly protects PTP1B from inactivation when present during the H O exposure. This protection was dependent on the concentration of TrxR1 and independent of Trx1 and Prx2. The protection was blocked by auranofin and required an intact selenocysteine residue in TrxR1. This activity likely involves reduction of the sulfenic acid intermediate form of PTP1B by TrxR1 and is therefore distinct from the previously described reactivation of end-point oxidized PTP1B, which requires both Trx1 and TrxR1. The ability of TrxR1 to directly reduce an oxidized phosphatase is a novel activity that can help explain previously observed increases in PTP1B oxidation and PDGF receptor phosphorylation in TrxR1 knockout cells. The activity of TrxR1 is therefore of potential relevance for understanding the mechanisms of redox regulation of growth factor signaling pathways.
Tipo de publicación:COMPARATIVE STUDY; JOURNAL ARTICLE
Nombre de substancia:0 (Homeodomain Proteins); 0 (Oxidants); 0 (PRRX2 protein, human); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (TXN protein, human); 0CH9049VIS (Selenocysteine); 3H04W2810V (Auranofin); 52500-60-4 (Thioredoxins); 53-59-8 (NADP); BBX060AN9V (Hydrogen Peroxide); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 1.8.1.9 (Txnrd1 protein, rat); EC 3.1.3.48 (PTPN1 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 1); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 3)


  5 / 298 MEDLINE  
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PMID:28653098
Autor:Lee JR; Roh JL; Lee SM; Park Y; Cho KJ; Choi SH; Nam SY; Kim SY
Dirección:Department of Otolaryngology, Asan Medical Centre, University of Ulsan College of Medicine, 88 Olympic-ro, 43-gil, Songpa-gu, Seoul, 05505, Republic of Korea.
Título:Overexpression of glutathione peroxidase 1 predicts poor prognosis in oral squamous cell carcinoma.
Fuente:J Cancer Res Clin Oncol; 143(11):2257-2265, 2017 Nov.
ISSN:1432-1335
País de publicación:Germany
Idioma:eng
Resumen:PURPOSE: Intracellular antioxidant enzymes are commonly upregulated in various cancer types and are associated with treatment outcomes. Because the relationship has rarely been examined in oral squamous cell carcinoma (OSCC), we aimed to evaluate the association between the levels of glutathione peroxidase (GPX)1, GPX4, and thioredoxin reductase (TrxR)1 expression and prognosis in patients with OSCC who underwent curative surgical resection. METHODS: This study included 233 patients who underwent curative surgery for previously untreated OSCC between 2000 and 2012. Tumour GPX1, GPX4, and TrxR1 expression was evaluated by immunohistochemistry and was dichotomised to low and high values according to defined expression levels. The association between GPX1, GPX4, and TrxR1 expression and clinicopathological results was analysed. Univariate and multivariate analyses using the Cox proportional hazards model were conducted to assess the significance of differences in recurrence or survival outcomes between variables. RESULTS: High GPX1, GPX4, and TrxR1 expression was observed in 99 (42.5%), 133 (57.1%), and 46 (19.7%) patients, respectively. GPX1 overexpression was significantly correlated with nodal metastasis, advanced overall stage, depth of invasion of >10 mm, high grade and perineural invasion (P < 0.05). High GPX4 expression was also related to nodal metastasis, overall advanced stage and high grade (P < 0.05). Univariate and multivariate analyses showed that increased GPX1 expression was significantly associated with poor disease-free, cancer-specific and overall survival (all P < 0.05), while increased GPX4 or TrxR1 expression was not (all P > 0.1). CONCLUSIONS: Tumour GPX1 expression is a useful biomarker predictive of recurrence and survival in OSCC patients.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Biomarkers, Tumor); EC 1.11.1.- (glutathione peroxidase GPX1); EC 1.11.1.12 (phospholipid-hydroperoxide glutathione peroxidase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.8.1.9 (TXNRD1 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 1)


  6 / 298 MEDLINE  
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PMID:28624622
Autor:Allison SJ; Sadiq M; Baronou E; Cooper PA; Dunnill C; Georgopoulos NT; Latif A; Shepherd S; Shnyder SD; Stratford IJ; Wheelhouse RT; Willans CE; Phillips RM
Dirección:School of Applied Sciences, University of Huddersfield, Queensgate, Huddersfield HD1 3DH, UK.
Título:Preclinical anti-cancer activity and multiple mechanisms of action of a cationic silver complex bearing N-heterocyclic carbene ligands.
Fuente:Cancer Lett; 403:98-107, 2017 Sep 10.
ISSN:1872-7980
País de publicación:Ireland
Idioma:eng
Resumen:Organometallic complexes offer the prospect of targeting multiple pathways that are important in cancer biology. Here, the preclinical activity and mechanism(s) of action of a silver-bis(N-heterocyclic carbine) complex (Ag8) were evaluated. Ag8 induced DNA damage via several mechanisms including topoisomerase I/II and thioredoxin reductase inhibition and induction of reactive oxygen species. DNA damage induction was consistent with cytotoxicity observed against proliferating cells and Ag8 induced cell death by apoptosis. Ag8 also inhibited DNA repair enzyme PARP1, showed preferential activity against cisplatin resistant A2780 cells and potentiated the activity of temozolomide. Ag8 was substantially less active against non-proliferating non-cancer cells and selectively inhibited glycolysis in cancer cells. Ag8 also induced significant anti-tumour effects against cells implanted intraperitoneally in hollow fibres but lacked activity against hollow fibres implanted subcutaneously. Thus, Ag8 targets multiple pathways of importance in cancer biology, is less active against non-cancer cells and shows activity in vivo in a loco-regional setting.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Antigens, Neoplasm); 0 (Antineoplastic Agents); 0 (DNA-Binding Proteins); 0 (Imidazoles); 0 (Organometallic Compounds); 0 (Poly(ADP-ribose) Polymerase Inhibitors); 0 (Reactive Oxygen Species); 0 (Topoisomerase I Inhibitors); 0 (Topoisomerase II Inhibitors); 7GR28W0FJI (Dacarbazine); EC 1.8.1.9 (TXNRD1 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 2.4.2.30 (PARP1 protein, human); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1); EC 5.99.1.2 (DNA Topoisomerases, Type I); EC 5.99.1.2 (TOP1 protein, human); EC 5.99.1.3 (DNA Topoisomerases, Type II); Q20Q21Q62J (Cisplatin); YF1K15M17Y (temozolomide)


  7 / 298 MEDLINE  
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PMID:28551108
Autor:Chen W; Tuladhar A; Rolle S; Lai Y; Rodriguez Del Rey F; Zavala CE; Liu Y; Rein KS
Dirección:Department of Chemistry and Biochemistry, Florida International University, 11200 SW 8th Street, Miami, FL 33199, United States.
Título:Brevetoxin-2, is a unique inhibitor of the C-terminal redox center of mammalian thioredoxin reductase-1.
Fuente:Toxicol Appl Pharmacol; 329:58-66, 2017 Aug 15.
ISSN:1096-0333
País de publicación:United States
Idioma:eng
Resumen:Karenia brevis, the Florida red tide dinoflagellate produces a suite of neurotoxins known as the brevetoxins. The most abundant of the brevetoxins PbTx-2, was found to inhibit the thioredoxin-thioredoxin reductase system, whereas the PbTx-3 has no effect on this system. On the other hand, PbTx-2 activates the reduction of small disulfides such as 5,5'-dithio-bis-(2-nitrobenzoic acid) by thioredoxin reductase. PbTx-2 has an α, ß-unsaturated aldehyde moiety which functions as an efficient electrophile and selenocysteine conjugates are readily formed. PbTx-2 blocks the inhibition of TrxR by the inhibitor curcumin, whereas curcumin blocks PbTx-2 activation of TrxR. It is proposed that the mechanism of inhibition of thioredoxin reduction is via the formation of a Michael adduct between selenocysteine and the α, ß-unsaturated aldehyde moiety of PbTx-2. PbTx-2 had no effect on the rates of reactions catalyzed by related enzymes such as glutathione reductase, glutathione peroxidase or glutaredoxin.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Enzyme Inhibitors); 0 (Marine Toxins); 0 (Oxocins); 0 (brevetoxin 2); 0CH9049VIS (Selenocysteine); EC 1.8.1.9 (TXNRD1 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 1.8.1.9 (Txnrd1 protein, rat); IT942ZTH98 (Curcumin)


  8 / 298 MEDLINE  
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PMID:28442342
Autor:Singh MP; Kwak GH; Kim KY; Kim HY
Dirección:Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu, Republic of Korea; School of Bioengineering and Biosciences, Department of Zoology, Lovely Professional University, Phagwara 144411, Punjab, India.
Título:Methionine sulfoxide reductase A protects hepatocytes against acetaminophen-induced toxicity via regulation of thioredoxin reductase 1 expression.
Fuente:Biochem Biophys Res Commun; 487(3):695-701, 2017 Jun 03.
ISSN:1090-2104
País de publicación:United States
Idioma:eng
Resumen:Thioredoxin reductase 1 (TXNRD1) is associated with susceptibility to acetaminophen (APAP)-induced liver damage. Methionine sulfoxide reductase A (MsrA) is an antioxidant and protein repair enzyme that specifically catalyzes the reduction of methionine S-sulfoxide residues. We have previously shown that MsrA deficiency exacerbates acute liver injury induced by APAP. In this study, we used primary hepatocytes to investigate the underlying mechanism of the protective effect of MsrA against APAP-induced hepatotoxicity. MsrA gene-deleted (MsrA ) hepatocytes showed higher susceptibility to APAP-induced cytotoxicity than wild-type (MsrA ) cells, consistent with our previous in vivo results. MsrA deficiency increased APAP-induced glutathione depletion and reactive oxygen species production. APAP treatment increased Nrf2 activation more profoundly in MsrA than in MsrA hepatocytes. Basal TXNRD1 levels were significantly higher in MsrA than in MsrA hepatocytes, while TXNRD1 depletion in both MsrA and MsrA cells resulted in increased resistance to APAP-induced cytotoxicity. In addition, APAP treatment significantly increased TXNRD1 expression in MsrA hepatocytes, while no significant change was observed in MsrA cells. Overexpression of MsrA reduced APAP-induced cytotoxicity and TXNRD1 expression levels in APAP-treated MsrA hepatocytes. Collectively, our results suggest that MsrA protects hepatocytes from APAP-induced cytotoxicity through the modulation of TXNRD1 expression.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Analgesics, Non-Narcotic); 362O9ITL9D (Acetaminophen); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 1.8.1.9 (Txnrd1 protein, mouse); EC 1.8.4.- (Methionine Sulfoxide Reductases); EC 1.8.4.11 (methionine sulfoxide reductase)


  9 / 298 MEDLINE  
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PMID:28300829
Autor:Oh BM; Lee SJ; Cho HJ; Park YS; Kim JT; Yoon SR; Lee SC; Lim JS; Kim BY; Choe YK; Lee HG
Dirección:Immunotherapy Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
Título:Cystatin SN inhibits auranofin-induced cell death by autophagic induction and ROS regulation via glutathione reductase activity in colorectal cancer.
Fuente:Cell Death Dis; 8(3):e2682, 2017 Mar 16.
ISSN:2041-4889
País de publicación:England
Idioma:eng
Resumen:Cystatin SN (CST1) is a specific inhibitor belonging to the cystatin superfamily that controls the proteolytic activities of cysteine proteases such as cathepsins. Our previous study showed that high CST1 expression enhances tumor metastasis and invasiveness in colorectal cancer. Recently, auranofin (AF), a gold(I)-containing thioredoxin reductase 1 (TrxR1) inhibitor, has been used clinically to treat rheumatoid arthritis. AF is a proteasome-associated deubiquitinase inhibitor and can act as an anti-tumor agent. In this study, we investigated whether CST1 expression induces autophagy and tumor cell survival. We also investigated the therapeutic effects of AF as an anti-tumor agent in colorectal cancer (CRC) cells. We found that CRC cells expressing high levels of CST1 undergo increased autophagy and exhibit chemotherapeutic resistance to AF-induced cell death, while those expressing low levels of CST1 are sensitive to AF. We also observed that knockdown of CST1 in high-CST1 CRC cells using CST1-specific small interfering RNAs attenuated autophagic activation and restored AF-induced cell mortality. Conversely, the overexpression of CST1 increased autophagy and viability in cells expressing low levels of CST1. Interestingly, high expression of CST1 attenuates AF-induced cell death by inhibiting intracellular reactive oxygen species (ROS) generation, as demonstrated by the fact that the blockage of ROS production reversed AF-induced cell death in CRC cells. In addition, upregulation of CST1 expression increased cellular glutathione reductase (GR) activity, reducing the cellular redox state and inducing autophagy in AF-treated CRC cells. These results suggest that high CST1 expression may be involved in autophagic induction and protects from AF-induced cell death by inhibition of ROS generation through the regulation of GR activity.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (CST1 protein, human); 0 (Proteasome Inhibitors); 0 (Reactive Oxygen Species); 0 (Salivary Cystatins); 3H04W2810V (Auranofin); EC 1.8.1.7 (Glutathione Reductase); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 3.4.- (Cathepsins); EC 3.4.25.1 (Proteasome Endopeptidase Complex)


  10 / 298 MEDLINE  
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PMID:28218609
Autor:Kang JS; Kim GY; Kim BW; Choi YH
Dirección:Anti-Aging Research Center and Blue-Bio Industry RIC, Dongeui University, 176 Eomgwangno Busanjin-gu, Busan 614-714, Republic of Korea. choiyh@deu.ac.kr.
Título:Antioxidative effects of diallyl trisulfide on hydrogen peroxide-induced cytotoxicity through regulation of nuclear factor-E2-related factor-mediated thioredoxin reductase 1 expression in C2C12 skeletal muscle myoblast cells.
Fuente:Gen Physiol Biophys; 36(2):129-139, 2017 Apr.
ISSN:0231-5882
País de publicación:Slovakia
Idioma:eng
Resumen:Diallyl trisulfide (DATS) is one of the major sulfur-containing compounds in garlic oil. In this study, we analyzed the effects of DATS against hydrogen peroxide (H2O2)-induced oxidative stress in C2C12 myoblasts. DATS preconditioning significantly attenuated H2O2-induced growth inhibition and DNA damage, as well as apoptosis by decreasing the generation of ROS. Treatment with DATS alone effectively upregulated the expression of nuclear factor-erythroid 2-related factor 2 (Nrf2) and thioredoxin reductase 1 (TrxR1), which was associated with the increased phosphorylation of Nrf2. However, the protective effects of DATS against H2O2-induced growth reduction and ROS accumulation were significantly abolished by auranofin, an inhibitor of TrxR activity. Moreover, DATS-mediated phosphorylation of Nrf2 and induction of TrxR1 were markedly reduced by genetic silencing of Nrf2. DATS treatment also induced the phosphorylation extracellular signal-regulating kinase (ERK), and analysis using specific inhibitors of cellular signaling pathways demonstrated that only ERK activation was involved in Nrf2 phosphorylation and TrxR1 induction. In addition, the cytoprotective potentials were abrogated in C2C12 cells pretreated with an ERK specific inhibitor. The results demonstrate that DATS protects against oxidative stress-induced DNA damage and apoptosis in C2C12 cells in part through the activation of Nrf2-mediated TrxR1 induction via the ERK signaling pathway.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Allyl Compounds); 0 (Antioxidants); 0 (NF-E2-Related Factor 2); 0 (Nfe2l2 protein, mouse); 0 (Reactive Oxygen Species); 0 (Sulfides); 0ZO1U5A3XX (diallyl trisulfide); BBX060AN9V (Hydrogen Peroxide); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 1.8.1.9 (Txnrd1 protein, mouse)



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