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[PMID]:29302025
[Au] Autor:Guéant JL; Chéry C; Oussalah A; Nadaf J; Coelho D; Josse T; Flayac J; Robert A; Koscinski I; Gastin I; Filhine-Tresarrieu P; Pupavac M; Brebner A; Watkins D; Pastinen T; Montpetit A; Hariri F; Tregouët D; Raby BA; Chung WK; Morange PE; Froese DS; Baumgartner MR; Benoist JF; Ficicioglu C; Marchand V; Motorin Y; Bonnemains C; Feillet F; Majewski J; Rosenblatt DS
[Ad] Endereço:INSERM, UMR_S954 Nutrition-Genetics-Environmental Risk Exposure and Reference Centre of Inborn Metabolism Diseases, University of Lorraine and University Hospital Centre of Nancy (CHRU Nancy), 54505, Nancy, France. jean-louis.gueant@univ-lorraine.fr.
[Ti] Título:APRDX1 mutant allele causes a MMACHC secondary epimutation in cblC patients.
[So] Source:Nat Commun;9(1):67, 2018 01 04.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To date, epimutations reported in man have been somatic and erased in germlines. Here, we identify a cause of the autosomal recessive cblC class of inborn errors of vitamin B metabolism that we name "epi-cblC". The subjects are compound heterozygotes for a genetic mutation and for a promoter epimutation, detected in blood, fibroblasts, and sperm, at the MMACHC locus; 5-azacytidine restores the expression of MMACHC in fibroblasts. MMACHC is flanked by CCDC163P and PRDX1, which are in the opposite orientation. The epimutation is present in three generations and results from PRDX1 mutations that force antisense transcription of MMACHC thereby possibly generating a H3K36me3 mark. The silencing of PRDX1 transcription leads to partial hypomethylation of the epiallele and restores the expression of MMACHC. This example of epi-cblC demonstrates the need to search for compound epigenetic-genetic heterozygosity in patients with typical disease manifestation and genetic heterozygosity in disease-causing genes located in other gene trios.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
Epistasia Genética
Erros Inatos do Metabolismo/genética
Mutação
Peroxirredoxinas/genética
Vitamina B 12/metabolismo
[Mh] Termos MeSH secundário: Alelos
Azacitidina/farmacologia
Sequência de Bases
Inibidores Enzimáticos/farmacologia
Saúde da Família
Feminino
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Heterozigoto
Seres Humanos
Masculino
Erros Inatos do Metabolismo/metabolismo
Linhagem
Sequenciamento Completo do Genoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Enzyme Inhibitors); 0 (MMACHC protein, human); EC 1.11.1.15 (PRDX1 protein, human); EC 1.11.1.15 (Peroxiredoxins); M801H13NRU (Azacitidine); P6YC3EG204 (Vitamin B 12)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02306-5


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[PMID]:29275566
[Au] Autor:Qi MC; Chen H; Wang LP; Zhang M; Tang XF
[Ad] Endereço:Institute of Dental Research, Capital Medical University School of Stomatology, Beijing 100050, China.
[Ti] Título:[Interaction between transcriptional factor E26 transformation specific 1 and peroxiredoxin 1 in nicotine-induced oral precancerous lesion cells].
[So] Source:Zhonghua Kou Qiang Yi Xue Za Zhi;52(12):729-734, 2017 Dec 09.
[Is] ISSN:1002-0098
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To investigate the interaction between nuclear transcriptional factor E26 transformation specific 1 (Ets1) and peroxiredoxin 1 (Prx1) in nicotine-induced oral precancerous lesion cells. Human oral precancerous lesion dysplastic oral keratinocyte (DOK) cells were cultured and divided into nicotine group, control group, knockdown group and knockdown control group. The nicotine group, knockdown group and knockdown control group were treated with 1 µmol/L nicotine for 7 days while the control group was untreated. Western blotting, co-immunoprecipitation (Co-IP) and chromatin immunoprecipitation (ChIP) were performed to detect Prx1 and Ets1 protein expression, Prx1 and Ets1 protein interaction, combined activity of Ets1 with PRDX1 gene promoter region in nicotine group and control group DOK cells. In nicotine group, DOK cells were transfected with siRNA or lentivirus to knockdown Ets1 and Prx1 expression. Prx1 and Ets1 protein expression was examined by Western blotting. Nicotine increased the expression of Prx1 and Ets1 protein in DOK cells. The relative expression of Prx1 and Ets1 was 0.71±0.02, 0.12±0.01 in nicotine group and 0.53±0.06, 0.01±0.01 in control group ( 0.009, 0.000). Co-IP showed that Prx1 could form protein complex with Ets1. The expression of Prx1 and Ets1 complex protein was increased in nicotine group. ChIP revealed that nicotine upregulated the combination of transcriptional factor Ets1 with PRDX1 gene promoter region, and the enrichment fold was 80.9±19.7 in nicotine group and 13.8±1.2 in control group ( 0.004). Ets1 and Prx1 protein expression was knocked down. The relative expression of Ets1 and Prx1 was 0.60±0.06, 0.48±0.03 in knockdown group and 0.83±0.08, 0.80±0.06 in knockdown control group ( 0.016, 0.002). Ets1 knockdown suppressed the expression of Prx1 ( 0.002). Conversely, Prx1 knockdown also inhibited the expression of Ets1 significantly ( 0.000). In oral precancerous lesion cells, Ets1 directly regulates Prx1 expression and nicotine might promote the development of oral precancerous lesion by magnifying the positive feedback signal pathway between Ets1 and Prx1.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Neoplasias Bucais/metabolismo
Proteínas Nucleares/metabolismo
Peroxirredoxinas/metabolismo
Lesões Pré-Cancerosas/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Carcinógenos
Técnicas de Silenciamento de Genes
Seres Humanos
Neoplasias Bucais/induzido quimicamente
Nicotina
Proteínas Nucleares/genética
Peroxirredoxinas/genética
Lesões Pré-Cancerosas/induzido quimicamente
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
Ativação Transcricional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Carcinogens); 0 (DAXX protein, human); 0 (Nuclear Proteins); 0 (RNA, Small Interfering); 6M3C89ZY6R (Nicotine); EC 1.11.1.15 (Peroxiredoxins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:171226
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1002-0098.2017.12.004


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[PMID]:29227081
[Au] Autor:Rakhmetov AD; Pil LS; Ostapchenko LI; Zoon CH
[Ti] Título:Prx II and CKBB proteins interaction under physiologic al and thermal stress conditions in A549 and HeLa cells.
[So] Source:Ukr Biochem J;88(1):61-8, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Peroxiredoxins (Prxs) are versatile enzymes that demonstrate various cell functions as peroxidases, protein chaperones, functions of signal modulators and binding partners. It is well established that Prxs can interact with multiple proteins in cells, such as ASK1, Cdk5-p35, JNK, MIF, PDGF, TK R4 and others. In this study, we attempted to evaluate a possible association between ubiquitous Prx II and ATP/ADP buffering enzyme - brain-type creatine kinase (CK BB). Our co-immunoprecipitation (Co-IP) results from the A549 and HeLa cell lysates with overexpressed HA-Prx II and Flag-CK BB have demonstrated strong association between two proteins under non-stressed conditions. This protein interaction was enhanced by the heat treatment with further HA-Prx II precipitation to the immobilized Flag-CK BB depending on the temperature increase. Temperature induced oligomerization of Prx II may contribute to the formation of Prx II conglomerates, which in turn, can associate with CK BB and increase signal intensities on the blotted membranes. Thus, such association and oligomerization of Prx II could take part in recovery and protection of the CK BB enzyme activity from inactivation during heat-induced stress.
[Mh] Termos MeSH primário: Creatina Quinase Forma BB/metabolismo
Peroxirredoxinas/metabolismo
Proteínas Recombinantes de Fusão/metabolismo
Estresse Fisiológico/genética
[Mh] Termos MeSH secundário: Células A549
Creatina Quinase Forma BB/genética
Expressão Gênica
Células HeLa
Hemaglutininas/genética
Hemaglutininas/metabolismo
Temperatura Alta
Seres Humanos
Imunoprecipitação
Oligopeptídeos/genética
Oligopeptídeos/metabolismo
Peroxirredoxinas/genética
Ligação Proteica
Multimerização Proteica
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemagglutinins); 0 (Oligopeptides); 0 (Recombinant Fusion Proteins); 98849-88-8 (FLAG peptide); EC 1.11.1.15 (PRDX2 protein, human); EC 1.11.1.15 (Peroxiredoxins); EC 2.7.3.2 (Creatine Kinase, BB Form)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.061


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[PMID]:28903064
[Au] Autor:Gong F; Wang J; Li J
[Ad] Endereço:School of Pharmacy, Wenzhou Medical University, Wenzhou, China; The First Affiliated Hospital, Zhengzhou University, Zhengzhou 450052, China. Electronic address: gongwenheng@wmu.edu.cn.
[Ti] Título:Isolation and characterization of peroxiredoxin 1 gene of Dunaliella salina.
[So] Source:Gene;635:39-45, 2017 Nov 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Peroxiredoxin 1 (Prdx1) is a ubiquitously expressed protein in eukaryotic cells, and plays an important role in cell proliferation, differentiation, apoptosis, and redox signaling. Although Prdx1 has been better studied in yeasts and humans, only few Prdx1 genes have been cloned in green algae. The microalga Dunaliella salina (D. salina) is a model for the study of a variety of human cilia-related diseases. In this study, a suppression subtractive hybridization cDNA library of D. salina was constructed, and 6 flagellum-associated genes including D. salina Prdx1 (DsPrdx1) were isolated and identified. A 956bp full-length cDNA of DsPrdx1 was cloned using rapid amplification of cDNA end (RACE). The open reading frame (ORF) of this DNA sequence encodes a polypeptide of 201 amino acids with a predicted molecular weight of 22kDa and a theoretical isoelectric point (pI) of 5.27. Sequence comparison showed that Prdx1 is highly evolutionarily conserved from the unicellular green alga D. salina to human. To our knowledge, this is the first reported full-length sequence of Prdx1 in D. salina. Interestingly, the protein expression of DsPrdx1 was obviously increased during flagellar disassembly in D. salina. Additionally, a yeast two-hybrid assay showed interaction between Prdx1 and RNA, and suggested that DsPrdx1 can protect RNA from degradation by RNase. Taken together, DsPrdx1 not only participates in flagellar disassembly, but also protects RNA from degradation.
[Mh] Termos MeSH primário: Sequência de Aminoácidos/genética
Peroxirredoxinas/genética
Filogenia
Volvocida/genética
[Mh] Termos MeSH secundário: Clorófitas/genética
Clonagem Molecular
DNA Complementar/genética
Seres Humanos
Peroxirredoxinas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Complementary); EC 1.11.1.15 (Peroxiredoxins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE


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[PMID]:28659575
[Au] Autor:Kang DH; Lee DJ; Lee S; Lee SY; Jun Y; Kim Y; Kim Y; Lee JS; Lee DK; Lee S; Jho EH; Yu DY; Kang SW
[Ad] Endereço:Department of Life Science, Ewha Womans University, Seoul, 120-750, Korea.
[Ti] Título:Interaction of tankyrase and peroxiredoxin II is indispensable for the survival of colorectal cancer cells.
[So] Source:Nat Commun;8(1):40, 2017 06 28.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mammalian 2-Cys peroxiredoxin (Prx) enzymes are overexpressed in most cancer tissues, but their specific signaling role in cancer progression is poorly understood. Here we demonstrate that Prx type II (PrxII) plays a tumor-promoting role in colorectal cancer by interacting with a poly(ADP-ribose) polymerase (PARP) tankyrase. PrxII deletion in mice with inactivating mutation of adenomatous polyposis coli (APC) gene reduces intestinal adenomatous polyposis via Axin/ß-catenin axis and thereby promotes survival. In human colorectal cancer cells with APC mutations, PrxII depletion consistently reduces the ß-catenin levels and the expression of ß-catenin target genes. Essentially, PrxII depletion hampers the PARP-dependent Axin1 degradation through tankyrase inactivation. Direct binding of PrxII to tankyrase ARC4/5 domains seems to be crucial for protecting tankyrase from oxidative inactivation. Furthermore, a chemical compound targeting PrxII inhibits the expansion of APC-mutant colorectal cancer cells in vitro and in vivo tumor xenografts. Collectively, this study reveals a redox mechanism for regulating tankyrase activity and implicates PrxII as a targetable antioxidant enzyme in APC-mutation-positive colorectal cancer.2-Cys peroxiredoxin (Prx) enzymes are highly expressed in most cancers but how they promote cancer progression is unclear. Here the authors show that in colorectal cancers with APC mutation, PrxII binds to tankyrase and prevents its oxidative inactivation, thereby preventing Axin1-dependent degradation of ²b-catenin.
[Mh] Termos MeSH primário: Neoplasias Colorretais/metabolismo
Regulação Enzimológica da Expressão Gênica/fisiologia
Regulação Neoplásica da Expressão Gênica/fisiologia
Peroxirredoxinas/metabolismo
Tanquirases/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Neoplasias Colorretais/genética
Seres Humanos
Camundongos
Neoplasias Experimentais
Peroxirredoxinas/genética
Tanquirases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.11.1.15 (Peroxiredoxins); EC 2.4.2.30 (Tankyrases); EC 2.4.4.30 (TNKS protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00054-0


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[PMID]:28640807
[Au] Autor:Boronat S; Domènech A; Carmona M; García-Santamarina S; Bañó MC; Ayté J; Hidalgo E
[Ad] Endereço:Oxidative Stress and Cell Cycle Group, Universitat Pompeu Fabra, Barcelona, Spain.
[Ti] Título:Lack of a peroxiredoxin suppresses the lethality of cells devoid of electron donors by channelling electrons to oxidized ribonucleotide reductase.
[So] Source:PLoS Genet;13(6):e1006858, 2017 Jun.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The thioredoxin and glutaredoxin pathways are responsible of recycling several enzymes which undergo intramolecular disulfide bond formation as part of their catalytic cycles such as the peroxide scavengers peroxiredoxins or the enzyme ribonucleotide reductase (RNR). RNR, the rate-limiting enzyme of deoxyribonucleotide synthesis, is an essential enzyme relying on these electron flow cascades for recycling. RNR is tightly regulated in a cell cycle-dependent manner at different levels, but little is known about the participation of electron donors in such regulation. Here, we show that cytosolic thioredoxins Trx1 and Trx3 are the primary electron donors for RNR in fission yeast. Unexpectedly, trx1 transcript and Trx1 protein levels are up-regulated in a G1-to-S phase-dependent manner, indicating that the supply of electron donors is also cell cycle-regulated. Indeed, genetic depletion of thioredoxins triggers a DNA replication checkpoint ruled by Rad3 and Cds1, with the final goal of up-regulating transcription of S phase genes and constitutive RNR synthesis. Regarding the thioredoxin and glutaredoxin cascades, one combination of gene deletions is synthetic lethal in fission yeast: cells lacking both thioredoxin reductase and cytosolic dithiol glutaredoxin. We have isolated a suppressor of this lethal phenotype: a mutation at the Tpx1-coding gene, leading to a frame shift and a loss-of-function of Tpx1, the main client of electron donors. We propose that in a mutant strain compromised in reducing equivalents, the absence of an abundant and competitive substrate such as the peroxiredoxin Tpx1 has been selected as a lethality suppressor to favor RNR function at the expense of the non-essential peroxide scavenging function, to allow DNA synthesis and cell growth.
[Mh] Termos MeSH primário: Transporte de Elétrons/genética
Peroxirredoxinas/genética
Ribonucleotídeo Redutases/genética
Proteínas de Schizosaccharomyces pombe/genética
Tiorredoxinas/genética
[Mh] Termos MeSH secundário: Catálise
Quinase do Ponto de Checagem 2/genética
Replicação do DNA/genética
Glutarredoxinas/metabolismo
Oxirredução
Peróxidos/metabolismo
Peroxirredoxinas/metabolismo
Ribonucleotídeo Redutases/metabolismo
Schizosaccharomyces/enzimologia
Schizosaccharomyces/crescimento & desenvolvimento
Proteínas de Schizosaccharomyces pombe/metabolismo
Tiorredoxinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glutaredoxins); 0 (Peroxides); 0 (Schizosaccharomyces pombe Proteins); 0 (Trx1 protein, S pombe); 52500-60-4 (Thioredoxins); EC 1.11.1.15 (Peroxiredoxins); EC 1.17.4.- (Ribonucleotide Reductases); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.11.1 (Cds1 protein, S pombe); EC 2.7.11.1 (rad3 protein, S pombe)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006858


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[PMID]:28552528
[Au] Autor:Jeon HJ; Park YS; Cho DH; Kim JS; Kim E; Chae HZ; Chun SY; Oh JS
[Ad] Endereço:Department of Genetic Engineering, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, South Korea.
[Ti] Título:Peroxiredoxins are required for spindle assembly, chromosome organization, and polarization in mouse oocytes.
[So] Source:Biochem Biophys Res Commun;489(2):193-199, 2017 Jul 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peroxiredoxins (Prxs) are highly conserved antioxidant enzymes and are implicated in multiple biological processes; however, their function in oocyte meiosis has not been studied. Here we show that inhibition of Prx I and II results in spindle defects, chromosome disorganization, and impaired polarization in mouse oocytes. Prx I was specifically localized at the spindle, whereas Prx II was enriched at the oocyte cortex and chromosomes. Inhibition of Prx activity with conoidin A disturbed assembly of the microtubule organizing center (MTOC) through Aurora A regulation, leading to defects in spindle formation. Moreover, conoidin A impaired actin filament and cortical granule (CG) distribution, disrupting actin cap and CG formation, respectively. Conoidin A also increased DNA damage without significantly increasing reactive oxygen species (ROS) levels, suggesting that the effects of conoidin A on meiotic maturation are not likely associated with ROS scavenging pathways. Therefore, our data suggest that Prxs are required for spindle assembly, chromosome organization, and polarization during meiotic maturation.
[Mh] Termos MeSH primário: Polaridade Celular/efeitos dos fármacos
Cromossomos de Mamíferos/efeitos dos fármacos
Oócitos/efeitos dos fármacos
Peroxirredoxinas/farmacologia
Fuso Acromático/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Cromossomos de Mamíferos/metabolismo
Relação Dose-Resposta a Droga
Feminino
Meiose/efeitos dos fármacos
Camundongos
Oócitos/metabolismo
Peroxirredoxinas/genética
Quinoxalinas/farmacologia
Fuso Acromático/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Quinoxalines); 0 (conoidin A); EC 1.11.1.15 (Peroxiredoxins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170530
[St] Status:MEDLINE


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[PMID]:28551405
[Au] Autor:Lee S; Jeong H; Lee JH; Chung JM; Kim R; Yun HJ; Won J; Jung HS
[Ad] Endereço:Department of Biochemistry, College of Natural Sciences, Kangwon National University, 1 Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Republic of Korea. Electronic address: taeinlee2011@kangwon.ac.kr.
[Ti] Título:Characterisation of conformational and functional features of alkyl hydroperoxide reductase E-like protein.
[So] Source:Biochem Biophys Res Commun;489(2):217-222, 2017 Jul 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alkyl hydroperoxide reductase E (AhpE) is a member of the peroxidase family of enzymes that catalyse the reduction of peroxides, however its structural and functional roles are still unclear in details. In this study, we used the Thermococcus kodakarensis AhpE-like protein as a model to investigate structure-function relationships including the molecular properties of DNA binding activity. Multiple sequence alignment, structural comparison and biochemical analyses revealed that TkAhpE includes conserved peroxidase residues in the active site, and exhibits peroxidase activity with structure-dependent holdase chaperone function. Following electrophoretic mobility shift assays and electron microscopy analysis demonstrated distinctive binding features of TkAhpE to the DNA showing that their dimeric conformer can bind to the double-stranded DNA, but not to the single-stranded DNA, indicating its striking molecular features to double-stranded DNA-specific interactions. Based on our results, we provided that TkAhpE is a multifunctional peroxidase displaying structure-dependent molecular chaperone and DNA binding activities.
[Mh] Termos MeSH primário: Peroxirredoxinas/química
Peroxirredoxinas/metabolismo
Thermococcus/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Modelos Moleculares
Conformação Proteica
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.11.1.15 (Peroxiredoxins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


  9 / 2483 MEDLINE  
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[PMID]:28506882
[Au] Autor:Slade L; Chalker J; Kuksal N; Young A; Gardiner D; Mailloux RJ
[Ad] Endereço:Memorial University of Newfoundland, Department of Biochemistry, St. John's, Newfoundland, Canada.
[Ti] Título:Examination of the superoxide/hydrogen peroxide forming and quenching potential of mouse liver mitochondria.
[So] Source:Biochim Biophys Acta;1861(8):1960-1969, 2017 08.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pyruvate dehydrogenase (PDHC) and α-ketoglutarate dehydrogenase complex (KGDHC) are important sources of reactive oxygen species (ROS). In addition, it has been found that mitochondria can also serve as sinks for cellular hydrogen peroxide (H O ). However, the ROS forming and quenching capacity of liver mitochondria has never been thoroughly examined. Here, we show that mouse liver mitochondria use catalase, glutathione (GSH), and peroxiredoxin (PRX) systems to quench ROS. Incubation of mitochondria with catalase inhibitor 3-amino-1,2,4-triazole (triazole) induced a significant increase in pyruvate or α-ketoglutarate driven O /H O formation. 1-Choro-2,4-dinitrobenzene (CDNB), which depletes glutathione (GSH), elicited a similar effect. Auranofin (AF), a thioredoxin reductase-2 (TR2) inhibitor which disables the PRX system, did not significantly change O /H O formation. By contrast catalase, GSH, and PRX were all required to scavenging extramitochondrial H O . In this study, the ROS forming potential of PDHC, KGDHC, Complex I, and Complex III was also profiled. Titration of mitochondria with 3-methyl-2-oxovaleric acid (KMV), a specific inhibitor for O /H O production by KGDHC, induced a ~86% and ~84% decrease in ROS production during α-ketoglutarate and pyruvate oxidation. Titration of myxothiazol, a Complex III inhibitor, decreased O /H O formation by ~45%. Rotenone also lowered ROS production in mitochondria metabolizing pyruvate or α-ketoglutarate indicating that Complex I does not contribute to ROS production during forward electron transfer from NADH. Taken together, our results indicate that KGDHC and Complex III are high capacity sites for O /H O production in mouse liver mitochondria. We also confirm that catalase plays a role in quenching either exogenous or intramitochondrial H O .
[Mh] Termos MeSH primário: Peróxido de Hidrogênio/metabolismo
Mitocôndrias Hepáticas/metabolismo
Superóxidos/metabolismo
[Mh] Termos MeSH secundário: Animais
Caprilatos/farmacologia
Catalase/fisiologia
Complexo III da Cadeia de Transporte de Elétrons/fisiologia
Glutationa/metabolismo
Complexo Cetoglutarato Desidrogenase/fisiologia
Masculino
Metacrilatos/farmacologia
Camundongos
Camundongos Endogâmicos C57BL
Peroxirredoxinas/fisiologia
Espécies Reativas de Oxigênio/metabolismo
Sulfetos/farmacologia
Tiazóis/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CPI 613); 0 (Caprylates); 0 (Methacrylates); 0 (Reactive Oxygen Species); 0 (Sulfides); 0 (Thiazoles); 11062-77-4 (Superoxides); 76706-55-3 (myxothiazol); BBX060AN9V (Hydrogen Peroxide); EC 1.10.2.2 (Electron Transport Complex III); EC 1.11.1.15 (Peroxiredoxins); EC 1.11.1.6 (Catalase); EC 1.2.4.2 (Ketoglutarate Dehydrogenase Complex); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE


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[PMID]:28506771
[Au] Autor:Sperandio M; Demasi APD; Martinez EF; Saad SO; Pericole FV; Vieira KP; Freitas NS; Araújo VC; Brown AL; Clemente-Napimoga JT; Napimoga MH
[Ad] Endereço:Laboratory of Immunology and Molecular Biology, São Leopoldo Mandic Institute of Medicine & Dentistry and Research Center (SLMANDIC), Campinas, SP, Brazil.
[Ti] Título:15d-PGJ as an endoplasmic reticulum stress manipulator in multiple myeloma in vitro and in vivo.
[So] Source:Exp Mol Pathol;102(3):434-445, 2017 Jun.
[Is] ISSN:1096-0945
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Multiple myeloma (MM) is characterised by intense protein folding and, consequently endoplasmic reticulum (ER) stress. The prostaglandin 15d-PGJ is able to raise oxidative stress levels within the cell and potentially trigger cell death. The aim of this study was to evaluate the antineoplastic effect of 15d-PGJ on MM in vitro and in vivo via ER and oxidative stress pathways. MM.1R and MM.1S cell lines were treated with 15d-PGJ at 1-10µM and evaluated with regard to proliferation, mRNA expression of PRDX1, PRDX4, GRP78, GRP94, CHOP, BCL-2 and BAX. Stress data was validated via oxidized glutathione assays. MM.1R cells were inoculated into NOD/SCID mice, which were subsequently treated daily with 15d-PGJ at 4mg/kg or vehicle (control), with tumour volume being monitored for 14days. 15d-PGJ reduced cell proliferation, induced cell death and apoptosis at 5µM and 10µM and Stress-related genes were upregulated at the same doses. Oxidized glutathione levels were also increased. 15d-PGJ2 at 4mg/kg in vivo halted tumour growth. In conclusion, 15d-PGJ induced myeloma cell death via ER stress in vitro. 15d-PGJ2 in vivo also inhibited tumour growth.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Mieloma Múltiplo/tratamento farmacológico
Prostaglandina D2/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Regulação para Baixo
Proteínas de Choque Térmico/genética
Proteínas de Choque Térmico/metabolismo
Seres Humanos
Masculino
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos NOD
Camundongos SCID
Estresse Oxidativo/efeitos dos fármacos
Peroxirredoxinas/genética
Peroxirredoxinas/metabolismo
Prostaglandina D2/farmacologia
Proteínas Proto-Oncogênicas c-bcl-2/genética
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Reprodutibilidade dos Testes
Fator de Transcrição CHOP/genética
Fator de Transcrição CHOP/metabolismo
Regulação para Cima
Proteína X Associada a bcl-2/genética
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (15-deoxyprostaglandin J2); 0 (Antineoplastic Agents); 0 (BAX protein, human); 0 (BCL2 protein, human); 0 (DDIT3 protein, human); 0 (Heat-Shock Proteins); 0 (Membrane Glycoproteins); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (RNA, Messenger); 0 (bcl-2-Associated X Protein); 0 (endoplasmin); 0 (molecular chaperone GRP78); 147336-12-7 (Transcription Factor CHOP); EC 1.11.1.15 (PRDX1 protein, human); EC 1.11.1.15 (PRDX4 protein, human); EC 1.11.1.15 (Peroxiredoxins); RXY07S6CZ2 (Prostaglandin D2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE



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