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Pesquisa : D08.811.682.667.750.750 [Categoria DeCS]
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[PMID]:28414076
[Au] Autor:Bu L; Li W; Ming Z; Shi J; Fang P; Yang S
[Ad] Endereço:Department of Respiratory Medicine, The Second Affiliated Hospital of Xi'an Jiaotong University, Xi'an 710003, Shaanxi, China; Department of Respiratory Medicine, Xi'an No.3 Hospital, Xi'an, 710018, Shaanxi, China.
[Ti] Título:Inhibition of TrxR2 suppressed NSCLC cell proliferation, metabolism and induced cell apoptosis through decreasing antioxidant activity.
[So] Source:Life Sci;178:35-41, 2017 Jun 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIMS: This study aims to analyze the effect of thioredoxin reductase 2 (TrxR2) on lung cancer cell proliferation, apoptosis, invasion and migration in vitro. MAIN METHODS: Real-time PCR was used to measure the expression of TrxR2 in NSCLC tumor tissues. After pAd-TrxR2 or shRNA-TrxR2 was transfected into A549 or NCI-H1299 cells, the cell proliferation was measured by CCK-8 method; cell apoptosis was measured by flow cytometry; cell invasion and migration was measured by Transwell method. The production of ROS was measured by DCFH-DA method; the activity of SOD, CAT and GSH-Px was measured by relative ELISA kit. KEY FINDINGS: The results showed that TrxR2 was up-regulated in NSCLC tumor tissues. Inhibition of TrxR2 suppressed NSCLC cell proliferation and induced apoptosis, and inhibited cell invasion and migration. However, overexpression of TrxR2 showed the opposite effect. Furthermore, when cells were transfected with shRNA-TrxR2, the production of ROS was significantly increased, and SOD, CAT and GSH-Px activity was decreased. Conversely, pAd-TrxR2 transfection showed the opposite effect. SIGNIFICANCE: Taken together, our results suggest that TrxR2 acts as an oncogenic gene in the context of lung cancer progression. The inhibition of TrxR2 suppressed lung cancer cell proliferation, invasion and migration and induced cell apoptosis by inducing ROS production and decreasing antioxidant activity. TrxR2 may be a potential target for NSCLC treatment.
[Mh] Termos MeSH primário: Apoptose/genética
Carcinoma Pulmonar de Células não Pequenas/genética
Proliferação Celular/genética
Neoplasias Pulmonares/genética
Tiorredoxina Redutase 2/genética
[Mh] Termos MeSH secundário: Carcinoma Pulmonar de Células não Pequenas/patologia
Linhagem Celular Tumoral
Movimento Celular/genética
Progressão da Doença
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Neoplasias Pulmonares/patologia
Invasividade Neoplásica/genética
RNA Interferente Pequeno/administração & dosagem
Espécies Reativas de Oxigênio/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Transfecção
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); EC 1.8.1.9 (TXNRD2 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 2)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE


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[PMID]:27866984
[Au] Autor:Park SJ; Kim HB; Piao C; Kang MY; Park SG; Kim SW; Lee JH
[Ad] Endereço:Laboratory of Genomic Instability and Cancer Therapeutics, Cancer Mutation Research Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju 61452, Republic of Korea; Department of Premedical Sciences, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju 61452, Republic of Ko
[Ti] Título:p53R2 regulates thioredoxin reductase activity through interaction with TrxR2.
[So] Source:Biochem Biophys Res Commun;482(4):706-712, 2017 Jan 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ribonucleotide reductase small subunit p53R2 is a member of the ribonucleotide reductase family that supplies dNTPs for nuclear and mitochondrial DNA replication and repair. Here, we have identified a mitochondrial thioredoxin reductase 2 (TrxR2) as a novel p53R2-binding protein. We demonstrated a direct interaction between the two, and observed that p53R2 stimulated the enzymatic activity of TrxR in vitro. Moreover, TrxR2 activity was significantly lower in p53R2 knockdown cells, and increased when p53R2 was overexpressed, effects that were independent of p53. Furthermore, p53R2 knockdown suppressed UV-induced TrxR activity. These findings suggest that p53R2 acts as a positive regulator of TrxR2 activity in mitochondria both under normal physiological conditions and during the cellular response to DNA damage.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Regulação Enzimológica da Expressão Gênica
Ribonucleotídeo Redutases/metabolismo
Tiorredoxina Redutase 2/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Dano ao DNA
Reparo do DNA
DNA Mitocondrial/metabolismo
Vetores Genéticos
Seres Humanos
Mitocôndrias/metabolismo
Plasmídeos/metabolismo
Ligação Proteica
RNA Interferente Pequeno/metabolismo
Proteínas Recombinantes/metabolismo
Raios Ultravioleta
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (DNA, Mitochondrial); 0 (RNA, Small Interfering); 0 (Recombinant Proteins); EC 1.17.4.- (RRM2B protein, human); EC 1.17.4.- (Ribonucleotide Reductases); EC 1.8.1.9 (TXNRD2 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 2)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161122
[St] Status:MEDLINE


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[PMID]:27117068
[Au] Autor:Lee JC; Park JH; Kim IH; Cho GS; Ahn JH; Tae HJ; Choi SY; Cho JH; Kim DW; Kwon YG; Kang IJ; Won MH; Kim YM
[Ad] Endereço:Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, South Korea.
[Ti] Título:Neuroprotection of ischemic preconditioning is mediated by thioredoxin 2 in the hippocampal CA1 region following a subsequent transient cerebral ischemia.
[So] Source:Brain Pathol;27(3):276-291, 2017 May.
[Is] ISSN:1750-3639
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Preconditioning by brief ischemic episode induces tolerance to a subsequent lethal ischemic insult, and it has been suggested that reactive oxygen species are involved in this phenomenon. Thioredoxin 2 (Trx2), a small protein with redox-regulating function, shows cytoprotective roles against oxidative stress. Here, we had focused on the role of Trx2 in ischemic preconditioning (IPC)-mediated neuroprotection against oxidative stress followed by a subsequent lethal transient cerebral ischemia. Animals used in this study were randomly assigned to six groups; sham-operated group, ischemia-operated group, IPC plus (+) sham-operated group, IPC + ischemia-operated group, IPC + auranofin (a TrxR2 inhibitor) + sham-operated group and IPC + auranofin + ischemia-operated group. IPC was subjected to a 2 minutes of sublethal transient ischemia 1 day prior to a 5 minutes of lethal transient ischemia. A significant loss of neurons was found in the stratum pyramidale (SP) of the hippocampal CA1 region (CA1) in the ischemia-operated-group 5 days after ischemia-reperfusion; in the IPC + ischemia-operated-group, pyramidal neurons in the SP were well protected. In the IPC + ischemia-operated-group, Trx2 and TrxR2 immunoreactivities in the SP and its protein level in the CA1 were not significantly changed compared with those in the sham-operated-group after ischemia-reperfusion. In addition, superoxide dismutase 2 (SOD2) expression, superoxide anion radical ( O2-) production, denatured cytochrome c expression and TUNEL-positive cells in the IPC + ischemia-operated-group were similar to those in the sham-operated-group. Conversely, the treatment of auranofin to the IPC + ischemia-operated-group significantly increased cell damage/death and abolished the IPC-induced effect on Trx2 and TrxR2 expressions. Furthermore, the inhibition of Trx2R nearly cancelled the beneficial effects of IPC on SOD2 expression, O2- production, denatured cytochrome c expression and TUNEL-positive cells. In brief, this study shows that IPC conferred neuroprotection against ischemic injury by maintaining Trx2 and suggests that the maintenance or enhancement of Trx2 expression by IPC may be a legitimate strategy for therapeutic intervention of cerebral ischemia.
[Mh] Termos MeSH primário: Isquemia Encefálica/metabolismo
Região CA1 Hipocampal/metabolismo
Precondicionamento Isquêmico
Neurônios/metabolismo
Neuroproteção/fisiologia
Tiorredoxinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Auranofina/farmacologia
Isquemia Encefálica/patologia
Isquemia Encefálica/prevenção & controle
Região CA1 Hipocampal/efeitos dos fármacos
Região CA1 Hipocampal/patologia
Morte Celular/efeitos dos fármacos
Morte Celular/fisiologia
Citocromos c/metabolismo
Inibidores Enzimáticos/farmacologia
Gerbillinae
Precondicionamento Isquêmico/métodos
Masculino
Neurônios/efeitos dos fármacos
Neurônios/patologia
Neuroproteção/efeitos dos fármacos
Estresse Oxidativo/fisiologia
Distribuição Aleatória
Superóxido Dismutase/metabolismo
Superóxidos/metabolismo
Tiorredoxina Redutase 2/antagonistas & inibidores
Tiorredoxina Redutase 2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 11062-77-4 (Superoxides); 3H04W2810V (Auranofin); 52500-60-4 (Thioredoxins); 9007-43-6 (Cytochromes c); EC 1.15.1.1 (Superoxide Dismutase); EC 1.15.1.1 (superoxide dismutase 2); EC 1.8.1.9 (Thioredoxin Reductase 2)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160428
[St] Status:MEDLINE
[do] DOI:10.1111/bpa.12389


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[PMID]:27924803
[Au] Autor:Hu B; Wu Y; Liu J; Shen X; Tong F; Xu G; Shen R
[Ad] Endereço:Department of Pathology and Nephrology, Jiaxing Hospital of Traditional Chinese Medicine, Zhejiang Chinese Medical University, Jiaxing, Zhejiang Province, P.R.China.
[Ti] Título:GSK-3beta Inhibitor Induces Expression of Nrf2/TrxR2 Signaling Pathway to Protect against Renal Ischemia/Reperfusion Injury in Diabetic Rats.
[So] Source:Kidney Blood Press Res;41(6):937-946, 2016.
[Is] ISSN:1423-0143
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Diabetes mellitus (DM) can lead to renal damage and dysfunction, and exacerbate renal ischemia/reperfusion injury (RI/RI). The aim of this study was to investigate the protective effect of GSK-3ß inhibitor TDZD-8 against RI/RI through Nrf2/TrxR2 signaling pathway in a rat DM model. METHODS: A DM rat model was established by a single injection of streptozocin. Diabetic rats were pretreated with TDZD-8 (1 mg/kg bw) or TDZD-8+auranofin (10 nmol/L, 5ml/kg bw), and then subjected to 45-min ischemia and 24-h reperfusion. Rats were equally randomized into four groups: a Sham-operated group, a RI/RI group, a TDZD-8 group, and a TDZD-8+auranofin group. Serum levels of BUN and Scr were measured. SOD activity, MDA content, and Nrf2, TrxR2 and caspase-3 expressions in rat kidney tissues were determined. RESULTS: Renal function was improved, oxidative stress and cell apoptosis were reduced, and the expression of Nrf2 and TrxR2 was up-regulated in TDZD-8 treated rats as compared with those in auranofin treated rats. CONCLUSION: TDZD-8 may exert its protective effect against RI/RI by regulating the Nrf2/TrxR2 signaling pathway in the kidney tissue in DM.
[Mh] Termos MeSH primário: Glicogênio Sintase Quinase 3 beta/antagonistas & inibidores
Traumatismo por Reperfusão/prevenção & controle
Transdução de Sinais/efeitos dos fármacos
Tiadiazóis/farmacologia
[Mh] Termos MeSH secundário: Animais
Auranofina/farmacologia
Diabetes Mellitus Experimental
Modelos Animais de Doenças
Fator 2 Relacionado a NF-E2/efeitos dos fármacos
Fator 2 Relacionado a NF-E2/metabolismo
Ratos
Traumatismo por Reperfusão/tratamento farmacológico
Tiorredoxina Redutase 2/efeitos dos fármacos
Tiorredoxina Redutase 2/metabolismo
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-benzyl-2-methyl-1,2,4-thiadiazolidine-3,5-dione); 0 (NF-E2-Related Factor 2); 0 (Nfe2l2 protein, rat); 0 (Thiadiazoles); 3H04W2810V (Auranofin); EC 1.8.1.9 (Thioredoxin Reductase 2); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161208
[St] Status:MEDLINE
[do] DOI:10.1159/000452598


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[PMID]:27505139
[Au] Autor:Tian B; Maidana DE; Dib B; Miller JB; Bouzika P; Miller JW; Vavvas DG; Lin H
[Ad] Endereço:Retina Service, Angiogenesis Laboratory, Department of Ophthalmology, Massachusetts Eye and Ear Infirmary, Harvard Medical School, Boston, MA, United States of America.
[Ti] Título:miR-17-3p Exacerbates Oxidative Damage in Human Retinal Pigment Epithelial Cells.
[So] Source:PLoS One;11(8):e0160887, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxidative stress has been shown to contribute to the development of age-related macular degeneration (AMD). MicroRNAs (miRNA) are small non-coding RNA molecules that function in RNA silencing and post-transcriptional regulation of gene expression. We showed miR-17-3p to be elevated in macular RPE cells from AMD patients and in ARPE-19 cells under oxidative stress. Transfection of miR-17-3p mimic in ARPE-19 induced cell death and exacerbated oxidative lethality that was alleviated by miR-17-3p inhibitor. The expression of antioxidant enzymes manganese superoxide dismutase (MnSOD) and thioredoxin reductase-2 (TrxR2) were suppressed by miR-17-3p mimic and reversed by miR-17-3p inhibitor. These results suggest miR-17-3p aggravates oxidative damage-induced cell death in human RPE cells, while miR-17-3p inhibitor acts as a potential protector against oxidative stress by regulating the expression of antioxidant enzymes.
[Mh] Termos MeSH primário: MicroRNAs/genética
Estresse Oxidativo/genética
Epitélio Pigmentado da Retina/metabolismo
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Antioxidantes/metabolismo
Sobrevivência Celular/genética
Regulação Enzimológica da Expressão Gênica/genética
Seres Humanos
Degeneração Macular/genética
Degeneração Macular/patologia
Epitélio Pigmentado da Retina/enzimologia
Superóxido Dismutase/metabolismo
Tiorredoxina Redutase 2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (MIRN17 microRNA, human); 0 (MicroRNAs); EC 1.15.1.1 (Superoxide Dismutase); EC 1.8.1.9 (Thioredoxin Reductase 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0160887


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[PMID]:27386940
[Au] Autor:Kirsch J; Schneider H; Pagel JI; Rehberg M; Singer M; Hellfritsch J; Chillo O; Schubert KM; Qiu J; Pogoda K; Kameritsch P; Uhl B; Pircher J; Deindl E; Müller S; Kirchner T; Pohl U; Conrad M; Beck H
[Ad] Endereço:From the Walter Brendel Centre of Experimental Medicine, Ludwig-Maximilians-University, Munich, Germany (J.K., H.S., J.-I.P., M.R., M.S., J.H., O.C., K.M.S., J.Q., K.P., P.K., B.U., J.P., E.D., U.P., H.B.); Stress and Immunity Lab, Department of Anesthesiology, Ludwig-Maximilians-University Hospital
[Ti] Título:Endothelial Dysfunction, and A Prothrombotic, Proinflammatory Phenotype Is Caused by Loss of Mitochondrial Thioredoxin Reductase in Endothelium.
[So] Source:Arterioscler Thromb Vasc Biol;36(9):1891-9, 2016 Sep.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Although the investigation on the importance of mitochondria-derived reactive oxygen species (ROS) in endothelial function has been gaining momentum, little is known on the precise role of the individual components involved in the maintenance of a delicate ROS balance. Here we studied the impact of an ongoing dysregulated redox homeostasis by examining the effects of endothelial cell-specific deletion of murine thioredoxin reductase 2 (Txnrd2), a key enzyme of mitochondrial redox control. APPROACH AND RESULTS: We analyzed the impact of an inducible, endothelial cell-specific deletion of Txnrd2 on vascular remodeling in the adult mouse after femoral artery ligation. Laser Doppler analysis and histology revealed impaired angiogenesis and arteriogenesis. In addition, endothelial loss of Txnrd2 resulted in a prothrombotic, proinflammatory vascular phenotype, manifested as intravascular cellular deposits, as well as microthrombi. This phenotype was confirmed by an increased leukocyte response toward interleukin-1 in the mouse cremaster model. In vitro, we could confirm the attenuated angiogenesis measured in vivo, which was accompanied by increased ROS and an impaired mitochondrial membrane potential. Ex vivo analysis of femoral arteries revealed reduced flow-dependent vasodilation in endothelial cell Txnrd2-deficient mice. This endothelial dysfunction could be, at least partly, ascribed to inadequate nitric oxide signaling. CONCLUSIONS: We conclude that the maintenance of mitochondrial ROS via Txnrd2 in endothelial cells is necessary for an intact vascular homeostasis and remodeling and that Txnrd2 plays a vitally important role in balancing mitochondrial ROS production in the endothelium.
[Mh] Termos MeSH primário: Endotélio Vascular/enzimologia
Artéria Femoral/enzimologia
Inflamação/enzimologia
Isquemia/enzimologia
Mitocôndrias/enzimologia
Tiorredoxina Redutase 2/deficiência
Trombose/enzimologia
Remodelação Vascular
Vasodilatação
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Modelos Animais de Doenças
Células Progenitoras Endoteliais/enzimologia
Células Progenitoras Endoteliais/patologia
Endotélio Vascular/patologia
Endotélio Vascular/fisiopatologia
Artéria Femoral/patologia
Artéria Femoral/fisiopatologia
Artéria Femoral/cirurgia
Predisposição Genética para Doença
Inflamação/genética
Inflamação/patologia
Inflamação/fisiopatologia
Isquemia/genética
Isquemia/patologia
Isquemia/fisiopatologia
Ligadura
Potencial da Membrana Mitocondrial
Camundongos Knockout
Mitocôndrias/patologia
Neovascularização Fisiológica
Óxido Nítrico/metabolismo
Oxirredução
Fenótipo
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais
Tiorredoxina Redutase 2/genética
Trombose/genética
Trombose/patologia
Trombose/fisiopatologia
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 31C4KY9ESH (Nitric Oxide); EC 1.8.1.9 (Thioredoxin Reductase 2); EC 1.8.1.9 (Txnrd2 protein, mouse)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.116.307843


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[PMID]:27344592
[Au] Autor:Zhang LB; Tang L; Ying SH; Feng MG
[Ad] Endereço:Institute of Microbiology, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, People's Republic of China.
[Ti] Título:Distinct roles of two cytoplasmic thioredoxin reductases (Trr1/2) in the redox system involving cysteine synthesis and host infection of Beauveria bassiana.
[So] Source:Appl Microbiol Biotechnol;100(24):10363-10374, 2016 Dec.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Two thioredoxin (Trx) reductases (Trr1/2) are known to play overlapping roles in the yeast Trx-Trr redox system but are generally unexplored in filamentous fungi, which possess multiple Trx homologues. This study seeks to characterize the functions of Trr1 and Trr2 in Beauveria bassiana, a filamentous fungal insect pathogen, and to probe their Trx partners. Both Trr1 and Trr2 were evidently localized in the cytoplasm of B. bassiana, unlike the two yeast homologues that have been reported to localize in the cytoplasm and mitochondria, respectively. Most of the six trx genes were greatly upregulated at the transcriptional level in the absence of trr1 instead of trr2 in B. bassiana, in which the trr1/2 double deletion failed in many attempts. Deletion of trr1 resulted in increased Trx activity, severe cysteine auxotrophy, and drastically reduced activities of peroxidases and superoxide dismutases under normal or oxidative conditions despite little change in catalase activity. Such changes disappeared in the absence of trr2 and were completely restored by complementation of trr1/2 or overexpression of trx1/6 in the Δtrr1 mutant, but were not restored at all by overexpression of trx2/3/4/5 or trr2 in the same mutant. All of these mutants exhibited similar trends of changes in the antioxidant response, conidiation, germination, thermotolerance, UV-B resistance, and virulence. Taken together, the findings indicate that Trr1 could reduce Trx2-5 and hence dominate the intracellular redox state, profoundly affecting the potential of B. bassiana against arthropod pests. Trr2 could reduce Trx1/6 but function only in the absence of Trr1.
[Mh] Termos MeSH primário: Artrópodes/microbiologia
Beauveria/enzimologia
Beauveria/crescimento & desenvolvimento
Cisteína/biossíntese
Tiorredoxina Redutase 1/metabolismo
Tiorredoxina Redutase 2/metabolismo
Fatores de Virulência/metabolismo
[Mh] Termos MeSH secundário: Animais
Beauveria/genética
Citoplasma/enzimologia
Deleção de Genes
Teste de Complementação Genética
Oxirredução
Tiorredoxina Redutase 1/genética
Tiorredoxina Redutase 2/genética
Virulência
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Virulence Factors); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 1.8.1.9 (Thioredoxin Reductase 2); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170124
[Lr] Data última revisão:
170124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160627
[St] Status:MEDLINE


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[PMID]:27107686
[Au] Autor:Yan J; Xu J; Fei Y; Jiang C; Zhu W; Han Y; Lu S
[Ad] Endereço:Department of Human Anatomy, Histology and Embryology, School of Basic Medical Sciences, Xi'an Jiaotong University Health Science Center, Xi'an, Shaanxi 710061, China.
[Ti] Título:TrxR2 deficiencies promote chondrogenic differentiation and induce apoptosis of chondrocytes through mitochondrial reactive oxygen species.
[So] Source:Exp Cell Res;344(1):67-75, 2016 May 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thioredoxin reductase 2 (TrxR2) is a selenium (Se) containing protein. Se deficiency is associated with an endemic osteoarthropathy characterized by impaired cartilage formation. It is unclear whether TrxR2 have roles in cartilage function. We examined the effects of TrxR2 on chondrogenic ATDC5 cells through shRNA-mediated gene silencing of TrxR2. We demonstrated TrxR2 deficiencies could enhance chondrogenic differentiation and apoptosis of ATDC5 cells. TrxR2 deficiencies increased accumulation of cartilage glycosaminoglycans (GAGs) and mineralization. TrxR2 deficiencies also stimulated expression of extracellular (ECM) gene including Collagen II and Aggrecan. The enhanced chondrogenic properties were further confirmed by activation of Akt signaling which are required for chondrogenesis. In addition, TrxR2 deficiencies promoted chondrocyte proliferation through acceleration of cell cycle progression by increase in both S and G2/M phase cell distribution accompanied with induction of parathyroid hormone-related protein (PTHrP). Moreover, TrxR2 deficiencies induced chondrocyte death via apoptosis and increased cell sensitivity to exogenous oxidative stress. Furthermore, TrxR2 deficiencies induced emission of mitochondrial reactive oxygen species (ROS) without alteration of mitochondrial membrane potential and intracellular ATP content. Finally, treatment of TrxR2 deficiency cells with N-acetylcysteine (NAC) inhibited mitochondrial ROS production and chondrocyte apoptosis. NAC also prevented chondrogenic differentiation of TrxR2 deficiency cells by suppression of ECM gene expression, GAGs accumulation and mineralization, as well as attenuation of Akt signaling. Thus, TrxR2-mediated mitochondrial integrity is indispensable for chondrogenic differentiation of ATDC5 cells. TrxR2 deficiency-induced impaired proliferation and death of chondrocytes may be the pathological mechanism of the osteoarthropathy due to Se deficiency. Notably, this study also uncover the roles of mitochondrial ROS which could stimulate cartilage ECM synthesis that offer novel insights for development of therapeutic agent to prevent cartilage degeneration in human disease.
[Mh] Termos MeSH primário: Apoptose
Diferenciação Celular
Condrócitos/citologia
Condrogênese
Mitocôndrias/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Tiorredoxina Redutase 2/deficiência
[Mh] Termos MeSH secundário: Acetilcisteína/farmacologia
Apoptose/efeitos dos fármacos
Diferenciação Celular/efeitos dos fármacos
Linhagem Celular
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Condrócitos/efeitos dos fármacos
Condrócitos/metabolismo
Condrogênese/efeitos dos fármacos
Seres Humanos
Mitocôndrias/efeitos dos fármacos
Tiorredoxina Redutase 2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); EC 1.8.1.9 (TXNRD2 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 2); WYQ7N0BPYC (Acetylcysteine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170806
[Lr] Data última revisão:
170806
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160425
[St] Status:MEDLINE


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[PMID]:27002142
[Au] Autor:Duan D; Zhang J; Yao J; Liu Y; Fang J
[Ad] Endereço:From the State Key Laboratory of Applied Organic Chemistry and College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou 730000 and the Shannxi Key Laboratory of Phytochemistry, Baoji University of Arts and Sciences, Baoji 721013, China.
[Ti] Título:Targeting Thioredoxin Reductase by Parthenolide Contributes to Inducing Apoptosis of HeLa Cells.
[So] Source:J Biol Chem;291(19):10021-31, 2016 May 06.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Parthenolide (PTL), a major active sesquiterpene lactone from the herbal plant Tanacetum parthenium, has been applied in traditional Chinese medicine for centuries. Although PTL demonstrates potent anticancer efficacy in numerous types of malignant cells, the cellular targets of PTL have not been well defined. We reported here that PTL interacts with both cytosolic thioredoxin reductase (TrxR1) and mitochondrial thioredoxin reductase (TrxR2), two ubiquitous selenocysteine-containing antioxidant enzymes, to elicit reactive oxygen species-mediated apoptosis in HeLa cells. PTL selectively targets the selenocysteine residue in TrxR1 to inhibit the enzyme function, and further shifts the enzyme to an NADPH oxidase to generate superoxide anions, leading to reactive oxygen species accumulation and oxidized thioredoxin. Under the conditions of inhibition of TrxRs in cells, PTL does not cause significant alteration of cellular thiol homeostasis, supporting selective target of TrxRs by PTL. Importantly, overexpression of functional TrxR1 or Trx1 confers protection, whereas knockdown of the enzymes sensitizes cells to PTL treatment. Targeting TrxRs by PTL thus discloses an unprecedented mechanism underlying the biological activity of PTL, and provides deep insights to understand the action of PTL in treatment of cancer.
[Mh] Termos MeSH primário: Antineoplásicos Fitogênicos/farmacologia
Apoptose/efeitos dos fármacos
Proteínas de Neoplasias/antagonistas & inibidores
Neoplasias/tratamento farmacológico
Sesquiterpenos/farmacologia
Tiorredoxina Redutase 1/antagonistas & inibidores
[Mh] Termos MeSH secundário: Antineoplásicos Fitogênicos/química
Células HeLa
Seres Humanos
NADPH Oxidases/metabolismo
Neoplasias/enzimologia
Sesquiterpenos/química
Superóxidos/metabolismo
Tanacetum parthenium/química
Tiorredoxina Redutase 1/metabolismo
Tiorredoxina Redutase 2/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents, Phytogenic); 0 (Neoplasm Proteins); 0 (Sesquiterpenes); 11062-77-4 (Superoxides); 2RDB26I5ZB (parthenolide); EC 1.6.3.- (NADPH Oxidases); EC 1.8.1.9 (TXNRD1 protein, human); EC 1.8.1.9 (TXNRD2 protein, human); EC 1.8.1.9 (Thioredoxin Reductase 1); EC 1.8.1.9 (Thioredoxin Reductase 2)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160323
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.700591


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[PMID]:26975474
[Au] Autor:Folda A; Citta A; Scalcon V; Calì T; Zonta F; Scutari G; Bindoli A; Rigobello MP
[Ad] Endereço:Department of Biomedical Sciences, University of Padova, via Ugo Bassi 58/b, 35131 Padova, Italy.
[Ti] Título:Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State.
[So] Source:Sci Rep;6:23071, 2016 Mar 15.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mitochondrial thioredoxin system (NADPH, thioredoxin reductase, thioredoxin) is a major redox regulator. Here we have investigated the redox correlation between this system and the mitochondrial enzyme cyclophilin D. The peptidyl prolyl cis-trans isomerase activity of cyclophilin D was stimulated by the thioredoxin system, while it was decreased by cyclosporin A and the thioredoxin reductase inhibitor auranofin. The redox state of cyclophilin D, thioredoxin 1 and 2 and peroxiredoxin 3 was measured in isolated rat heart mitochondria and in tumor cell lines (CEM-R and HeLa) by redox Western blot analysis upon inhibition of thioredoxin reductase with auranofin, arsenic trioxide, 1-chloro-2,4-dinitrobenzene or after treatment with hydrogen peroxide. A concomitant oxidation of thioredoxin, peroxiredoxin and cyclophilin D was observed, suggesting a redox communication between the thioredoxin system and cyclophilin. This correlation was further confirmed by i) co-immunoprecipitation assay of cyclophilin D with thioredoxin 2 and peroxiredoxin 3, ii) molecular modeling and iii) depleting thioredoxin reductase by siRNA. We conclude that the mitochondrial thioredoxin system controls the redox state of cyclophilin D which, in turn, may act as a regulator of several processes including ROS production and pro-apoptotic factors release.
[Mh] Termos MeSH primário: Ciclofilinas/metabolismo
Mitocôndrias Cardíacas/metabolismo
Peroxirredoxina III/metabolismo
Tiorredoxinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Auranofina/farmacologia
Western Blotting
Linhagem Celular Tumoral
Ciclofilinas/antagonistas & inibidores
Ciclofilinas/química
Ciclosporina/farmacologia
Células HeLa
Seres Humanos
Peróxido de Hidrogênio/metabolismo
Peróxido de Hidrogênio/farmacologia
Mitocôndrias Cardíacas/genética
Modelos Moleculares
Oxidantes/metabolismo
Oxidantes/farmacologia
Oxirredução/efeitos dos fármacos
Peroxirredoxina III/química
Ligação Proteica/efeitos dos fármacos
Domínios Proteicos
Interferência de RNA
Ratos Wistar
Espécies Reativas de Oxigênio/metabolismo
Tiorredoxina Redutase 2/antagonistas & inibidores
Tiorredoxina Redutase 2/genética
Tiorredoxina Redutase 2/metabolismo
Tiorredoxinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oxidants); 0 (Reactive Oxygen Species); 3H04W2810V (Auranofin); 52500-60-4 (Thioredoxins); 83HN0GTJ6D (Cyclosporine); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.15 (Peroxiredoxin III); EC 1.8.1.9 (Thioredoxin Reductase 2); EC 5.2.1.- (Cyclophilins); EC 5.2.1.8 (cyclophilin D)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160316
[St] Status:MEDLINE
[do] DOI:10.1038/srep23071



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