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thioredoxin and thioredoxin-interacting protein as prognostic markers for gastric cancer recurrence

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World Journal of Gastroenterology 2012年第39期18卷 5581-5588页

作者： Jae Yun Lim Sun Och Yoo Soon Won Hong Jong Won Kim Seung Ho Choi Jae Yong Cho Department of Medical Oncology Gangnam Severance Cancer HospitalYonsei University College of MedicineSeoul 135-720South Korea Department of Pathology Gangnam Severance Cancer HospitalYonsei University College of MedicineSeoul 135-720South Korea Department of Surgery Gangnam Severance Cancer HospitalYonsei University College of MedicineSeoul 135-720South Korea

AIM:To evaluate the potential of thioredoxin (TXN) and thioredoxin-interacting protein (TXNIP) expression as biomarkers for predicting gastric cancer recurrence. METHODS:TXN and TXNIP expression levels were acquired from gene expression microarray data for 65 human gastric cancer tissues. We determined whether each gene expression level was associated with cancer recurrence and investigated the relationship between the two genes. For validation, the expression levels of TXN and TXNIP were measured by quantitative real- time reverse transcription polymerase chain reaction in 68 independent stage Ⅲ gastric cancer patients. The correlation between gene expression and cancer prognosis was evaluated. Immunohistochemical staining was performed to investigate the protein expression levels of TXN and TXNIP and to characterize the expression patterns of each protein. RESULTS:TXN was a prognosis-related gene (P = 0.009), whereas TXNIP, a TXN inhibitor, demonstrated a negative correlation with TXN in the gene expression microarray data. In the 68 stage Ⅲ patients, the expression levels of both TXN and TXNIP had a statistically significant effect on recurrence-free survival (RFS, P = 0.008 and P = 0.036, respectively). The low TXN and high TXNIP expression group exhibited a better prognosis than the other groups, and the high TXN and low TXNIP expression group exhibited a poorer prognosis (P < 0.001 for RFS and P = 0.001 for overall survival). More than half of the patients in the simulta-neously high TXN and low TXNIP expression group ex- perienced a recurrence within 1 year after curative surgery, and the 5-year survival rate of the patients in this group was 29%, compared with 89% in the low TXN and high TXNIP expression group. The TXN protein was overexpressed in 65% of the gastric cancer tissues, whereas the TXNIP protein was underexpressed in 85% of the cancer cells. In a correlation analysis, TXN and TXNIP were highly correlated with many oncogenes and tumor suppressors

关键词： Gastric cancer thioredoxin thioredoxin-interacting protein Biomarker Prognosis

thioredoxin and impaired spatial learning and memory in the rats exposed to intermittent hypoxia

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Chinese Medical Journal 2012年第17期125卷 3074-3080页

作者： YANG Xiu-hong LIU Hui-guo LIU Xue CHEN Jun-nan Department of Respiratory and Critical Care Medicine Tongji HospitalTong3i Medical CollegeHuazhong University of Science and Technology Key Laboratory of Respiratory Disease of the Ministry of Health WuhanHubei 430030China

Background Obstructive sleep apnea （OSA） can cause cognitive dysfunction and may be a reversible cause of cognitive loss in patients with Alzheimer＇s disease （AD）. Chronic exposure to intermittent hypoxia （IH）, such as encountered in OSA, is marked by neurodegenerative changes in rat brain. We investigated the change of thioredoxin （Trx）, spatial learning and memory in rats exposed to chronic intermittent hypoxia （CIH）. Methods Forty healthy male Sprague-Dawley （SD） rats were randomly divided into four groups of ten each： a CIH＋normal saline （CIH＋NS group）, a N-acetylcystein-treated CIH （CIH＋NAC） group, a sham CIH group （sham CIH＋NS）, and a sham NAC-treated sham CIH （CIH＋NAC） group. Spatial learning and memory in each group was assessed with the Morris water maze. Real-time PCR and Western blotting were used to examine mRNA and protein expression of Trx in the hippocampus tissue. The terminal deoxynucleotidyl transferase-mediated dUTP-nick end-labeling （TUNEL） method was used to detect the apoptotic cells of the hippocampus CA1 region. Results CIH-rats showed impaired spatial learning and memory in the Morris water maze, including longer mean latencies for the target platform, reduced numbers of passes over the previous target platform and a smaller percentage of time spent in the target quadrant. Trx mRNA and protein levels were significantly decreased in the CIH-hippocampus, meanwhile, an elevated apoptotic index revealed apoptosis of hippocampal neurons of rats exposed to CIH. The rats, which acted better in the Morris water maze, showed higher levels of the Trx mRNA and protein in the hippocampus; apoptotic index of the neurons in the hippocampus of each group was negatively correlated with the Trx mRNA and protein levels. Conclusion The Trx deficit likely plays an important role in the impaired spatial learning and memory in the rats exposed to CIH and may work through the apoptosis of neurons in the hippocampus.

关键词： intermittent hypoxia thioredoxin spatial learning oxidative stress sleep apnea

A reciprocal inhibitory relationship between adiponectin and mammalian cytosolic thioredoxin

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Science Bulletin 2016年第19期61卷 1513-1521,1470页

作者：刘金生许建英黄琎赵勇叶菲钟良玮 Savaid School of Medicine University of Chinese Academy of Sciences Department of Respiratory Medicine Dayi Hospital Affiliated to Shanxi Medical University State Key Laboratory of Membrane Biology Institute of Zoology Chinese Academy of Sciences Institute of Materia Medica Chinese Academy of Medical Sciences & Peking Union Medical College

thioredoxin is a redox protein while adiponectin is an adipokine. Their relationship has been less appreciated. Here we show that in serum of patients with acute exacerbations of chronic obstructive Pulmonary Disease,decreased activity of thioredoxin coexists with increased level of adiponectin as partial pressure of arterial oxygen decreases. From the results with adiponectin-knockout mice and in vitro experiments, we have found a reciprocal inhibitory relationship, by which adiponectin inhibits cytosolic thioredoxin(Trx1) expression, whereas serum Trx1 influences adiponectin multimerization. The association between extracellular Trx1 and adiponectin attenuates their functions. This relationship is dynamic, and correlated with a body's physiological conditions.

关键词： Adiponectin Chronic obstructive pulmonary disease Protein–protein interaction Reciprocal regulation thioredoxin

Molecular cloning, characterization and expression profiles of thioredoxin 1 and thioredoxin 2 genes in Mytilus galloprovincialis

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Chinese Journal of Oceanology and Limnology 2013年第3期31卷 493-503页

作者：王清宁璇璇裴东赵建民由丽萍王春艳吴惠丰 Key Laboratory of Coastal Zone Environmental Processes Chinese Academy of Science Shandong Provincial Key Laboratory of Coastal Zone Environmental Processes Yantai Institute of Coastal Zone ResearchChinese Academy of Sciences Yantai Oceanic Environmental Monitoring Central Station of SOA China Agriculture University(Yantai)

thioredoxin （Trx） proteins are involved in many biological processes especially the regulation of cellular redox homeostasis. In this study, two Trx cDNAs were cloned from the mussel Mytilus galloprovincialis using rapid amplification of cDNA ends-polymerase chain reaction （RACE-PCR）. The two cDNAs were named MgTrxl and MgTrx2, respectively. The open reading frames of MgTrxl and MgTrx2 were 318 and 507 base pairs （bp） and they encoded proteins of 105 and 168 amino acids with estimated molecular masses of 11.45 and 18.93 kDa, respectively. Sequence analysis revealed that both proteins possessed the conserved active site dithiol motif Cys-Gly-Pro-Cys. In addition, MgTrx2 also possessed a putative mitochondrial targeting signal suggesting that it is located in the mitochondria. Quantitative real-time polymerase chain reaction （qPCR） revealed that both MgTrxl and MgTrx2 were constitutively expressed in all tissues examined. The MgTrxl transcript was most abundant in hemocytes and gills, whereas the MgTrx2 transcript was most abundant in gonad, hepatopancreas, gill and hemocytes. Following Vibrio anguillarum challenge, the expression of MgTrxl was up-regulated and reached its peak, at a value 10-fold the initial value, at 24 h. Subsequently, expression returned back to the original level. In contrast, the expression level of MgTrx2 was down-regulated following bacterial stimulation, with one fifth of the control level evident at 12 h post challenge. These results suggest that MgTrxl and MgTrx2 may play important roles in the response ofM. galloprovincialis to bacterial challenge.

关键词： thioredoxin mussel bacterial challenge antioxidant

Human thioredoxin exerts cardioprotective effect and attenuates reperfusion injury in rats partially via inhibiting apoptosis

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Chinese Medical Journal 2008年第9期121卷 819-826页

作者： WU Xiao-wei TENG Zong-yan JIANG Li-hong FAN Ying ZHANG Yu-hua LI Xiu-rong ZHANG Yi-na Department of Geriatrics Second Affiliated Hospital Harbin Medical University Harbin Heilongjiang 150086 China Department of Pathology Harbin Medical University Harbin Heilongjiang 150086 China

Background thioredoxin is one of the most important redox regulating proteins. Although thioredoxin has been shown to protect cells against different kinds of oxidative stress, the role of thioredoxin in myocardial ischemia and reperfusion injury has not been fully understood. This study was conducted to explore the protective role of human thioredoxin on myocardial ischemia and reperfusion injury and its potential mechanisms. Methods Purified human thioredoxin was injected into adult Wister rats, which were subjected to 30 minutes of myocardial ischemia followed by 2 or 24 hours of reperfusion. We detected 1） the infarct size; 2） the level of malondisldehyde （MDA） in serum; 3） the expression of caspase-9, and cytochrome c in/out of mitochondia by Western blotting; 4） apoptosis by terminal-deoxynucleotidyl transferase mediated nick end labeling （TUNEL） assay and caspase-3 and its protein by reverse transcriptase polymerase chain reaction （RT-PCR） and Western blotting; 5） the expression of bcl-2 and bax in cardium by immunohistochemical （IHC） assay. Results Human thioredoxin reduced myocardial ischemia/reperfusion injury as evidenced by significant decrease of myocardial infarct size （P〈0.01）, notable reduction of myocyte apoptosis （P 〈0.01）, lower systemic oxidative stress level （P 〈0.01） after reperfusion for 2 hours, and few inflammatory cell infiltration after reperfusion for 24 hours in rats. Furthermore, treatment with human thioredoxin significantly reduced the release of mitochonddal cytochrome C （P〈0.05） and inhibited the activity of caspase-9 （P 〈0.05） and caspase-3 （P 〈0.01 in mRNA and P 〈0.05 at protein level）. Meanwhile, human thioredoxin markedly increased bcl-2 expression （P 〈0.05）. Conclusions These results strongly suggest that human thioredoxin has cardioprotective effects on myocardial ischemia/reperfusion and its anti-apoptotic role may be mediated by modulating bcl-2 and the mitochondria-dependent apoptotic signaling pathway.

关键词： thioredoxin reperfusion cardioprotection mitochondria apoptosis

AtECB1/MRL7, a thioredoxin-Like Fold Protein with Disulfide Reductase Activity, Regulates Chloroplast Gene Expression and Chloroplast Biogenesis in Arabidopsis thaliana

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Molecular Plant 2014年第1期7卷 206-217页

作者： Qing-Bo Yu Qian Ma Meng-Meng Kong Tuan-Tuan Zhao Xiao-Lei Zhang Que Zhou Chao Huang Kang Chong Zhong-Nan Yang Biology Department Life and Environmental College Shanghai Normal University Shanghai 200234 China National Laboratory of Plant Molecular Genetics Institute of Plant Physiology and Ecology Shanghai Institutes for Biological Sciences the Chinese Academy of Sciences Shanghai 200032 China Research Center for Molecular and Developmental Biology Key Laboratory of Photosynthesis and Environmental Molecular Physiology Institute of Botany the Chinese Academy of Sciences 100093 Beijing China

Plastid-encoded RNA polymerase （PEP） is closely associated with numerous factors to form PEP complex for plastid gene expression and chloroplast development. However, it is not clear how PEP complex are regulated in chloroplast. Here, one thioredoxin-like fold protein, Arabidopsis early chloroplast biogenesis 1 （AtECB1）, an allele of MRL7, was identified to regulate PEP function and chloroplast biogenesis. The knockout lines for AtECB1 displayed albino phenotype and impaired chloroplast development. The transcripts of PEP-dependent plastid genes were barely detected, suggesting that the PEP activity is almost lost in atecbl-1. Although AtECB1 was not identified in PEP complex, a yeast two-hybrid assay and pull-down experiments demonstrated that it can interact with Trx Z and FSD3, two intrinsic subunits of PEP complex, respectively. This indicates that AtECB1 may play a regulatory role for PEP-dependent plastid gene expression through these two subunits. AtECB1 contains a βαβαββα structure in the thioredoxin-like fold domain and lacks the typical C-X-X-C active site motif. Insulin assay demonstrated that AtECB1 harbors disulfide reductase activity in vitro using the purified recombinant AtECB1 protein. This showed that this thioredoxin-like fold protein, AtECB1 also has the thioredoxin activity. AtECB1 may play a role in thioredoxin signaling to regulate plastid gene expression and chloroplast development.

关键词： Arabidopsis thioredoxin disulfide reductase activity chloroplast transcription chloroplast biogenesis.

NADPH thioredoxin Reductase C Controls the Redox Status of Chloroplast 2-Cys Peroxiredoxins in Arabidopsis thaliana

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Molecular Plant 2009年第2期2卷 298-307页

作者： Kerstin Kirchsteiger Pablo Pulido Maricruz Gonzalez Francisco Javier Cejudo Instituto de Bioquimica Vegetal y Fotosintesis Universidad de Sevilla and CSIC Avda Americo Vespucio 49 41092-Sevilla Spain

Chloroplast 2-Cys peroxiredoxins （2-Cys Prxs） are efficiently reduced by NADPH thioredoxin reductase C （NTRC）. To investigate the effect of light/darkness on NTRC function, the content of abundant plastidial enzymes, Rubisco, glutamine synthetase （GS）, and 2-Cys Prxs was analyzed during two consecutive days in Arabidopsis wild-type and ntrc mutant plants. No significant difference of the content of these proteins was observed during the day or the night in wildtype and mutant plants. NTRC deficiency caused a lower content of fully reduced 2-Cys Prxs, which was undetectable in darkness, suggesting that NTRC is the most important pathway for 2-Cys Prx reduction, probably the only one during the night. Arabidopsis contains two plastidial 2-Cys Prxs, A and B, for which T-DNA insertion lines were characterized showing the same phenotype as wild-type plants. Two-dimensional gel analysis of leaf extracts from these mutants allowed the identification of basic and acidic isoforms of 2-Cys Prx A and B. In-vitro assays and mass spectrometry analysis showed that the acidic isoform of both proteins is produced by overoxidation of the peroxidatic Cys residue to sulfinic acid. 2-Cys Prx overoxidation was lower in the NTRC mutant. These results show the important function of NTRC to maintain the redox equilibrium of chloroplast 2-Cys Prxs.

关键词： Chloroplast peroxiredoxin NADPH thioredoxin reductase C overoxidation thioredoxin Arabidopsis.

NTR/NRX Define a New thioredoxin System in the Nucleus of Arabidopsis thaliana Cells

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Molecular Plant 2014年第1期7卷 30-44页

作者： Corinne Marchal Valerie Delorme-Hinoux Laetitia Bariat Wafi Siala Christophe Belin Julio Saez-Vasquez Christophe Riondet Jean-Philippe Reichheld Universite Perpignan Via Domitia CNRS Laboratoire Genome et Developpement des Plantes UMR 5096 58 Avenue Paul Alduy-Bat T F-66860 Perpignan France Pharmacologie cellulaire et moleculaire Louvain Drug Research Institute Universite catholique de Louvain Brussels Belgium

thioredoxins （TRX） are key components of cellular redox balance, regulating many target proteins through thiol/disulfide exchange reactions. In higher plants, TRX constitute a complex multigenic family whose members have been found in almost all cellular compartments. Although chloroplastic and cytosolic TRX systems have been largely studied, the presence of a nuclear TRX system has been elusive for a long time. Nucleoredoxins （NRX） are potential nuclear TRX found in most eukaryotic organisms. In contrast to mammals, which harbor a unique NRX, angiosperms gen- erally possess multiple NRX organized in three subfamilies. Here, we show thatArabidopsis thaliana has two NRXgenes （AtNRX1 and AtNRX2）, respectively, belonging to subgroups I and III. While NRX1 harbors typical TRX active sites （WCG/ PPC）, NRX2 has atypical active sites （WCRPC and WCPPF）. Nevertheless, both NRXl and NRX2 have disulfide reduction capacities, although NRX1 alone can be reduced by the thioredoxin reductase NTRA. We also show that both NRX1 and NRX2 have a dual nuclear/cytosolic localization. Interestingly, we found that NTRA, previously identified as a cytosolic protein, is also partially localized in the nucleus, suggesting that a complete TRX system is functional in the nucleus. We show that NRX1 is mainly found as a dimer in vivo. nrxl and nrx2 knockout mutant plants exhibit no phenotypic perturbations under standard growth conditions. However, the nrxl mutant shows a reduced pollen fertility phenotype, suggesting a specific role of NRX1 at the haploid phase.

关键词： thioredoxin nucleoredoxin nucleus Arabidopsis.

An alternative splice variant of human thioredoxin

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Chinese Science Bulletin 1998年第4期43卷 292-295页

作者： Wang Ying Wang Yugang Zhang Yingmei Yuan Yong Ma Dalong Beijing Med Univ Dept Immunol Beijing 100083 Peoples R China

An alternative splice variant of human thioredoxin (hTRX) has been identified by using reverse transcription_polymerase chain reaction, cloning and expressing of hTRX_encoding gene, and DNA sequencing. This variant contains hTRX exons 1, 2, 4 and 5. The entire protein encoding region of this variant, named hTRXδ3, is identical to hTRX except for the omission of exon 3. Human TRX and TRXδ3 cDNA has been expressed in \%***\%. The catalytic activity of rhTRXδ3 on DTT_dependent insulin reduction is lower than that of rhTRX, although hTRXδ3 still contains the active site.

关键词： human thioredoxin alternative splicing variant isoform \%E.coli.