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https://www.readbyqxmd.com/read/29331374/alternative-pathway-of-h2s-and-polysulfides-production-from-sulfurated-catalytic-cysteine-of-reaction-intermediates-of-3-mercaptopyruvate-sulfurtransferase
#1
Noriyuki Nagahara, Shin Koike, Takashi Nirasawa, Hideo Kimura, Yuki Ogasawara
It has been known that hydrogen sulfide and/or polysulfides are produced from a (poly)sulfurated sulfur-acceptor substrate of 3-mercaptopyruvate sulfurtransferase (MST) via thioredoxin (Trx) reduction in vitro. In this study, we used thiosulfate as the donor substrate and the catalytic reaction was terminated on the formation of a persulfide or polysulfides. We can present alternative pathway of production of hydrogen sulfide and/or polysulfides from (poly)sulfurated catalytic-site cysteine of reaction intermediates of MST via Trx reduction...
January 10, 2018: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29328386/proteomics-based-investigation-of-multiple-stages-of-oscc-development-indicates-that-the-inhibition-of-trx-1-delays-oral-malignant-transformation
#2
Xijuan Chen, Qinchao Hu, Tong Wu, Chunyang Wang, Juan Xia, Linglan Yang, Bin Cheng, Xiaobing Chen
The majority of cases of oral squamous cell carcinoma (OSCC) develop from oral potentially malignant disorders, which have been confirmed to be involved in chronic oxidative stimulation. However, no effective treatment approaches have been used to prevent the development of dysplasia into cancerous lesions thus far. In the present study, a well-established OSCC model was used to detect proteomics profiles at different stages during oral malignant transformation. Of the 15 proteins that were found to be upregulated in both the dysplasia and carcinoma stages, the oxidative stress-associated proteins, thioredoxin-1 (Trx-1), glutaredoxin-1 and peroxiredoxin-2 were note as the proteins with significant changes in expression Trx-1 was identified to be the most significantly upregulated protein in the precancerous stage...
January 3, 2018: International Journal of Oncology
https://www.readbyqxmd.com/read/29327078/the-role-of-the-thioredoxin-thioredoxin-reductase-system-in-the-metabolic-syndrome-towards-a-possible-prognostic-marker
#3
REVIEW
Alexey A Tinkov, Geir Bjørklund, Anatoly V Skalny, Arne Holmgren, Margarita G Skalnaya, Salvatore Chirumbolo, Jan Aaseth
Mammalian thioredoxin reductase (TrxR) is a selenoprotein with three existing isoenzymes (TrxR1, TrxR2, and TrxR3), which is found primarily intracellularly but also in extracellular fluids. The main substrate thioredoxin (Trx) is similarly found (as Trx1 and Trx2) in various intracellular compartments, in blood plasma, and is the cell's major disulfide reductase. Thioredoxin reductase is necessary as a NADPH-dependent reducing agent in biochemical reactions involving Trx. Genetic and environmental factors like selenium status influence the activity of TrxR...
January 11, 2018: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/29320894/biomarkers-of-tumor-redox-status-in-response-to-modulations-of-glutathione-and-thioredoxin-antioxidant-pathways
#4
Julie Kengen, Jean-Philippe Deglasse, Marie-Aline Neveu, Lionel Mignion, Céline Desmet, Florian Gourgue, Jean-Christophe Jonas, Bernard Gallez, Bénédicte F Jordan
The ability of certain cancer cells to maintain a highly reduced intracellular environment is correlated with aggressiveness and drug resistance. Since the gluthathione (GSH) and thioredoxin (TRX) systems cooperate to a tight regulation of ROS in cell physiology, and to a stimulation of tumor initiation and progression, modulation of the GSH and TRX pathways are emerging as new potential targets in cancer. In vivo methods to assess changes in tumor redox status are critically needed to assess the relevance of redox-targeted agents...
January 10, 2018: Free Radical Research
https://www.readbyqxmd.com/read/29305423/endoplasmic-reticulum-resident-protein-57-erp57-oxidatively-inactivates-human-transglutaminase-2
#5
Michael C Yi, Arek V Melkonian, James A Ousey, Chaitan Khosla
Transglutaminase 2 (TG2) is a ubiquitously expressed, intracellular as well as extracellular protein with multiple modes of posttranslational regulation, including an allosteric disulfide bond between Cys370-Cys371 that renders the enzyme inactive in the extracellular matrix. Although recent studies have established that extracellular TG2 is switched "on" by the redox cofactor protein thioredoxin-1 (TRX), it is unclear how TG2 is switched "off". Here, we demonstrate that TG2 oxidation by biological small-molecule biological oxidants, including glutathione, cystine, and hydrogen peroxide, is unlikely to be the inactivation mechanism...
January 5, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29305108/evaluation-of-the-p53-and-thioredoxin-reductase-in-sperm-from-asthenozoospermic-males-in-comparison-to-normozoospermic-males
#6
Mohmmad-Nabi Moradi, Jamshid Karimi, Iraj Khodadadi, Iraj Amiri, Manoochehr Karami, Massoud Saidijam, Akram Vatannejad, Heidar Tavilani
Thioredoxin (Trx) system has a defensive role against the harmful effect of oxidative stress in sperm. p53 is an important regulator of apoptosis and normal process of spermatogenesis. Regulation of p53 by redox state of the cell and Thioredoxin system has been reported. The aim of this study was to evaluate the ROS level, Thioredoxin reductase (TrxR) activity and p53 protein levels in sperm of asthenozoospermic and normozoospermic males. Semen samples from 80 donors were divided into asthenozoospermic (n=40) and normozoospermic (n=40) groups using the WHO criteria...
January 2, 2018: Free Radical Biology & Medicine
https://www.readbyqxmd.com/read/29304480/mapping-the-phenotypic-repertoire-of-the-cytoplasmic-2-cys-peroxiredoxin-thioredoxin-system-1-understanding-commonalities-and-differences-among-cell-types
#7
Gianluca Selvaggio, Pedro M B M Coelho, Armindo Salvador
The system (PTTRS) formed by typical 2-Cys peroxiredoxins (Prx), thioredoxin (Trx), Trx reductase (TrxR), and sulfiredoxin (Srx) is central in antioxidant protection and redox signaling in the cytoplasm of eukaryotic cells. Understanding how the PTTRS integrates these functions requires tracing phenotypes to molecular properties, which is non-trivial. Here we analyze this problem based on a model that captures the PTTRS' conserved features. We have mapped the conditions that generate each distinct response to H2O2 supply rates (vsup), and estimated the parameters for thirteen human cell types and for Saccharomyces cerevisiae...
December 21, 2017: Redox Biology
https://www.readbyqxmd.com/read/29296890/the-lipid-peroxidation-product-4-hydroxy-2-nonenal-induces-tissue-factor-decryption-via-ros-generation-and-the-thioredoxin-system
#8
Shabbir A Ansari, Usha R Pendurthi, L Vijaya Mohan Rao
Many pathophysiologic agents transform cryptic tissue factor (TF) on cells to prothrombotic TF, and one such stimulus is 4-hydroxy-2-nonenal (HNE), the most abundant aldehyde produced by the oxidation of ω-6 polyunsaturated fatty acids. HNE was shown to induce reactive oxygen species (ROS) generation and p38 MAPK activation, but the link between them and their role in TF decryption are unclear. The present study was carried out to elucidate potential mechanisms involved in HNE-induced TF decryption in monocytic cells...
November 28, 2017: Blood Advances
https://www.readbyqxmd.com/read/29290907/morphological-alterations-and-redox-changes-associated-with-hepatic-warm-ischemia-reperfusion-injury
#9
Rim Jawad, Melroy D'souza, Lisa Arodin Selenius, Marita Wallenberg Lundgren, Olof Danielsson, Greg Nowak, Mikael Björnstedt, Bengt Isaksson
AIM: To study the effects of warm ischemia-reperfusion (I/R) injury on hepatic morphology at the ultrastructural level and to analyze the expression of the thioredoxin (TRX) and glutaredoxin (GRX) systems. METHODS: Eleven patients undergoing liver resection were subjected to portal triad clamping (PTC). Liver biopsies were collected at three time points; first prior to PTC (baseline), 20 min after PTC (post-ischemia) and 20 min after reperfusion (post-reperfusion)...
December 8, 2017: World Journal of Hepatology
https://www.readbyqxmd.com/read/29285268/reactive-oxygen-species-levels-control-nf-%C3%AE%C2%BAb-activation-by-low-dose-deferasirox-in-erythroid-progenitors-of-low-risk-myelodysplastic-syndromes
#10
Mathieu Meunier, Sarah Ancelet, Christine Lefebvre, Josiane Arnaud, Catherine Garrel, Mylène Pezet, Yan Wang, Patrice Faure, Gautier Szymanski, Nicolas Duployez, Claude Preudhomme, Denis Biard, Benoit Polack, Jean-Yves Cahn, Jean Marc Moulis, Sophie Park
Anemia is a frequent cytopenia in myelodysplastic syndromes (MDS) and most patients require red blood cell transfusion resulting in iron overload (IO). Deferasirox (DFX) has become the standard treatment of IO in MDS and it displays positive effects on erythropoiesis. In low risk MDS samples, mechanisms improving erythropoiesis after DFX treatment remain unclear. Herein, we addressed this question by using liquid cultures with iron overload of erythroid precursors treated with low dose of DFX (3μM), which corresponds to DFX 5 mg/kg/day, an unusual dose used for iron chelation...
December 1, 2017: Oncotarget
https://www.readbyqxmd.com/read/29278740/the-a-to-z-of-modulated-cell-patterning-by-mammalian-thioredoxin-reductases
#11
REVIEW
Markus Dagnell, Edward E Schmidt, Elias S J Arnér
Mammalian thioredoxin reductases (TrxRs) are selenocysteine-containing proteins (selenoproteins) that propel a large number of functions through reduction of several substrates including the active site disulfide of thioredoxins (Trxs). Well-known enzymatic systems that in turn are supported by Trxs and TrxRs include deoxyribonucleotide synthesis through ribonucleotide reductase, antioxidant defense through peroxiredoxins and methionine sulfoxide reductases, and redox modulation of a number of transcription factors...
December 23, 2017: Free Radical Biology & Medicine
https://www.readbyqxmd.com/read/29277606/characterization-of-2-cys-peroxiredoxin-3-and-4-in-common-carp-and-the-immune-response-against-bacterial-infection
#12
Yu Zhu Yang, Yan Zhao, Ling Yang, Lan Ping Yu, Hui Wang, Xiang Shan Ji
Accumulating evidence suggests that peroxiredoxins (Prxs) eliminate excessive cellular H2O2 and are important factors in redox signaling pathways. In this study, we cloned the full-length cDNAs and genomic sequences of Prx3 and Prx4 from common carp. The common carp Prx3 and Prx4 open reading frames were 753 base pairs (bp) and 783bp in length, respectively, and contained seven exons and six introns. Multiple sequence alignment and phylogenetic analyses revealed that the common carp Prx1-4 proteins share high identities and similar characteristics with other known animal Prxs...
December 19, 2017: Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
https://www.readbyqxmd.com/read/29262300/helicoverpa-inducible-thioredoxin-h-from-cicer-arietinum-structural-modeling-and-potential-targets
#13
Archana Singh, Chetna Tyagi, Onkar Nath, Indrakant K Singh
Thioredoxins are small and universal proteins, which are involved in the cell redox regulation. In plants, they participate in a broad range of biochemical processes like self-incompatibility, seed germination, pathogen & pest defense and oxidative stress tolerance. The h-type of thioredoxin (Trx-h) protein represents the largest Trx family. Herein, we characterized the Helicoverpa - inducible Trx h from an important legume, Cicer arietinum, CaHaTrx-h, 'CGFS' type Trxs, which encodes for a 113 amino acids long protein and possess characteristic motifs "FLKVDVDE" and "VVDFTASWCGPCRFIAPIL" and 73% sequence identity with AtTrx-h...
December 17, 2017: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/29228906/phylogenetic-relationship-and-domain-organisation-of-set-domain-proteins-of-archaeplastida
#14
Supriya Sarma, Mukesh Lodha
BACKGROUND: SET is a conserved protein domain with methyltransferase activity. Several genome and transcriptome data in plant lineage (Archaeplastida) are available but status of SET domain proteins in most of the plant lineage is not comprehensively analysed. RESULTS: In this study phylogeny and domain organisation of 506 computationally identified SET domain proteins from 16 members of plant lineage (Archaeplastida) are presented. SET domain proteins of rice and Arabidopsis are used as references...
December 11, 2017: BMC Plant Biology
https://www.readbyqxmd.com/read/29222842/kinetic-characterisation-of-wild-type-and-mutant-human-thioredoxin-glutathione-reductase-defines-its-reaction-and-regulatory-mechanisms
#15
Christina Brandstaedter, Karin Fritz-Wolf, Stine Weder, Marina Fischer, Beate Hecker, Stefan Rahlfs, Katja Becker
In most cells the thioredoxin (Trx) and glutathione systems are essentially involved in maintaining redox homeostasis. The selenoprotein thioredoxin glutathione reductase (TGR) is a hybrid enzyme in which a glutaredoxin (Grx) domain is linked to a thioredoxin reductase (TrxR). Notably, the protein is also capable of reducing glutathione disulfide (GSSG) thus representing an important link between the two redox systems. In this study, we recombinantly produced human TGR (hTGR wild type) by fusing its open reading frame with a bacterial SECIS element and co-expressing the construct in E...
December 8, 2017: FEBS Journal
https://www.readbyqxmd.com/read/29207979/a-propeptide-toolbox-for-secretion-optimization-of-flavobacterium-meningosepticum-endopeptidase-in-lactococcus-lactis
#16
Pei Yu Lim, Lee Ling Tan, Dave Siak-Wei Ow, Fong T Wong
BACKGROUND: Lactic acid bacteria are a family of "generally regarded as safe" organisms traditionally used for food fermentation. In recent years, they have started to emerge as potential chassis for heterologous protein production. And more recently, due to their beneficial properties in the gut, they have been examined as potential candidates for mucosal delivery vectors, especially for acid-sensitive enzymes. One such application would be the delivery of gluten-digesting endopeptidases for the treatment of celiac disease...
December 5, 2017: Microbial Cell Factories
https://www.readbyqxmd.com/read/29186683/trim48-promotes-ask1-activation-and-cell-death-through-ubiquitination-dependent-degradation-of-the-ask1-negative-regulator-prmt1
#17
Yusuke Hirata, Kazumi Katagiri, Keita Nagaoka, Tohru Morishita, Yuki Kudoh, Tomohisa Hatta, Isao Naguro, Kuniyuki Kano, Tsuyoshi Udagawa, Tohru Natsume, Junken Aoki, Toshifumi Inada, Takuya Noguchi, Hidenori Ichijo, Atsushi Matsuzawa
Apoptosis signal-regulating kinase 1 (ASK1) is an oxidative stress-responsive kinase that is regulated by various interacting molecules and post-translational modifications. However, how these molecules and modifications cooperatively regulate ASK1 activity remains largely unknown. Here, we showed that tripartite motif 48 (TRIM48) orchestrates the regulation of oxidative stress-induced ASK1 activation. A pull-down screen identified a TRIM48-interacting partner, protein arginine methyltransferase 1 (PRMT1), which negatively regulates ASK1 activation by enhancing its interaction with thioredoxin (Trx), another ASK1-negative regulator...
November 28, 2017: Cell Reports
https://www.readbyqxmd.com/read/29182243/targeting-the-thioredoxin-reductase-thioredoxin-system-from-staphylococcus-aureus-by-silver-ions
#18
Xiangwen Liao, Fang Yang, Hongyan Li, Pui-Kin So, Zhongping Yao, Wei Xia, Hongzhe Sun
The thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. In particular, this reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system. Although silver ions and silver-containing materials have been used as antibacterial agents for centuries, the antibacterial mechanism of silver is not well-understood...
November 28, 2017: Inorganic Chemistry
https://www.readbyqxmd.com/read/29180214/thioredoxin-1-attenuates-sepsis-induced-cardiomyopathy-after-cecal-ligation-and-puncture-in-mice
#19
Rickesha L Wilson, Vaithinathan Selvaraju, Rajesh Lakshmanan, Mahesh Thirunavukkarasu, Jacob Campbell, David W McFadden, Nilanjana Maulik
BACKGROUND: Sepsis is a leading cause of mortality among patients in intensive care units across the USA. Thioredoxin-1 (Trx-1) is an essential 12 kDa cytosolic protein that, apart from maintaining the cellular redox state, possesses multifunctional properties. In this study, we explored the possibility of controlling adverse myocardial depression by overexpression of Trx-1 in a mouse model of severe sepsis. METHODS: Adult C57BL/6J and Trx-1Tg/+ mice were divided into wild-type sham (WTS), wild-type cecal ligation and puncture (WTCLP), Trx-1Tg/+sham (Trx-1Tg/+S), and Trx-1Tg/+CLP groups...
December 2017: Journal of Surgical Research
https://www.readbyqxmd.com/read/29170489/prokaryotic-soluble-expression-and-purification-of-bioactive-human-fibroblast-growth-factor-21-using-maltose-binding-protein
#20
Anh Ngoc Nguyen, Jung-A Song, Minh Tan Nguyen, Bich Hang Do, Grace G Kwon, Sang Su Park, Jiwon Yoo, Jaepyeong Jang, Jonghwa Jin, Mark J Osborn, Yeon Jin Jang, Thu Trang Thi Vu, Heung-Bum Oh, Han Choe
Human fibroblast growth factor 21 (hFGF21) has been characterized as an important regulator of glucose and lipid metabolism homeostasis. Here, to produce hFGF21 efficiently in Escherichia coli, the expression and solubility of hFGF21 were tested and optimised by fusing the protein with one of eight tags: hexahistidine (His6), thioredoxin (Trx), small ubiquitin-related modifier (Sumo), glutathione S-transferase (GST), maltose-binding protein (MBP), N-utilisation substance protein A (NusA), human protein disulphide isomerase (PDI), and the b'a' domain of PDI (PDIb'a')...
November 23, 2017: Scientific Reports
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