14 results match your criteria surface trx-1

  • Page 1 of 1

Detection of thioredoxin-1 using ultra-sensitive ELISA with enzyme-encapsulated human serum albumin nanoparticle.

Nano Converg 2019 Dec 9;6(1):37. Epub 2019 Dec 9.

Department of Chemical & Biomolecular Engineering, Sogang University, Mapo-Gu, Seoul, 04170, South Korea.

Many methods for early diagnosis of the disease use biomarker tests, which measure indicators of biological state in body fluids or blood. However, a limitation of these methods is their low sensitivity to biomarkers. In this study, human serum albumin (HSA) based nanoparticles capable of encapsulating excess horseradish peroxidase (HRP) are synthesized and applied to the development of enzyme-linked immunosorbent assay (ELISA) kit with ultra-high sensitivity. Read More

View Article and Full-Text PDF
December 2019

Impact of key residues within chloroplast thioredoxin- on recognition for reduction and oxidation of target proteins.

J Biol Chem 2019 11 9;294(46):17437-17450. Epub 2019 Oct 9.

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan

Thioredoxin (Trx) is a redox-responsive protein that modulates the activities of its target proteins mostly by reducing their disulfide bonds. In chloroplasts, five Trx isoforms (Trx-, Trx-, Trx-, Trx-, and Trx-) regulate various photosynthesis-related enzymes with distinct target selectivity. To elucidate the determinants of the target selectivity of each Trx isoform, here we investigated the residues responsible for target recognition by Trx-, the most well-studied chloroplast-resident Trx. Read More

View Article and Full-Text PDF
November 2019

Deletion of a conserved transcript PG_RS02100 expressed during logarithmic growth in Porphyromonas gingivalis results in hyperpigmentation and increased tolerance to oxidative stress.

PLoS One 2018 12;13(11):e0207295. Epub 2018 Nov 12.

Department of Oral Biology, University of Florida, Gainesville, Florida, United States of America.

The oral obligate anaerobe Porphyromonas gingivalis possesses a small conserved transcript PG_RS02100 of unknown function we previously identified using small RNA-seq analysis as expressed during logarithmic growth. In this study, we sought to determine if PG_RS02100 plays a role in P. gingivalis growth or stress response. Read More

View Article and Full-Text PDF

A thioredoxin-mimetic peptide exerts potent anti-inflammatory, antioxidant, and atheroprotective effects in ApoE2.Ki mice fed high fat diet.

Cardiovasc Res 2019 02;115(2):292-301

Sorbonne Université, Institut de Biologie Paris Seine (IBPS), CNRS, INSERM ERL U-1164, Biological Adaptation and Ageing (B2A), UMR-8256, F-75252, Paris, France.

Aims: Oxidative stress and inflammation play a pathogenic role in atherosclerosis. Thioredoxin-1 (Trx-1) is an anti-oxidative, anti-inflammatory protein with atheroprotective effects. However, in vivo cleavage of Trx-1 generates a truncated pro-inflammatory protein, Trx-80, which compromises the therapeutic use of Trx-1. Read More

View Article and Full-Text PDF
February 2019

Thioredoxin-1 Negatively Modulates ADAM17 Activity Through Direct Binding and Indirect Reductive Activity.

Antioxid Redox Signal 2018 09 27;29(8):717-734. Epub 2018 Feb 27.

1 Laboratório Nacional de Biociências , LNBio, CNPEM, Campinas, Brazil .

Aims: A disintegrin and metalloprotease 17 (ADAM17) modulates signaling events by releasing surface protein ectodomains such as TNFa and the EGFR-ligands. We have previously characterized cytoplasmic thioredoxin-1 (Trx-1) as a partner of ADAM17 cytoplasmic domain. Still, the mechanism of ADAM17 regulation by Trx-1 is unknown, and it has become of paramount importance to assess the degree of influence that Trx-1 has on metalloproteinase ADAM17. Read More

View Article and Full-Text PDF
September 2018

Human Plasma Thioredoxin-80 Increases With Age and in ApoE Mice Induces Inflammation, Angiogenesis, and Atherosclerosis.

Circulation 2017 Aug 4;136(5):464-475. Epub 2017 May 4.

From Biological Adaptation and Ageing (B2A), CNRS UMR-8256/INSERM ERL U-1164, Biological Institute Paris-Seine, Sorbonne University, Paris, France (D.C., A.A., D.F.D.M., M.M.H., F.C., V.D., K.E.H., M.R.); Lipoprotein Metabolism Section, Cardiovascular-Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD (B.V., A.T.R.): Institut des Maladies Métaboliques et Cardiovasculaires (12 MC), INSERM UMR 1048, Toulouse, France (A.N.-S.); and Centre de Recherche sur le Vieillissement, Service Gériatrique, Département de Médecine, Université de Sherbrooke, Quebec, Canada (A.L.P., T.F.).

Background: Thioredoxin (TRX)-1, a ubiquitous 12-kDa protein, exerts antioxidant and anti-inflammatory effects. In contrast, the truncated form, called TRX80, produced by macrophages induces upregulation of proinflammatory cytokines. TRX80 also promotes the differentiation of mouse peritoneal and human macrophages toward a proinflammatory M1 phenotype. Read More

View Article and Full-Text PDF

Thioredoxin as a putative biomarker and candidate target in age-related immune decline.

Biochem Soc Trans 2014 Aug;42(4):922-7

*School of Life and Health Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, U.K.

The oxidoreductase Trx-1 (thioredoxin 1) is highly conserved and found intra- and extra-cellularly in mammalian systems. There is increasing interest in its capacity to regulate immune function based on observations of altered distribution and expression during ageing and disease. We have investigated previously whether extracellular T-cell or peripheral blood mononuclear cell Trx-1 levels serve as a robust marker of ageing. Read More

View Article and Full-Text PDF

Healthy ageing and depletion of intracellular glutathione influences T cell membrane thioredoxin-1 levels and cytokine secretion.

Chem Cent J 2013 Sep 5;7(1):150. Epub 2013 Sep 5.

Life and Health Sciences, Aston University, Aston Triangle Birmingham B4 7ET, UK.

Background: During ageing an altered redox balance has been observed in both intracellular and extracellular compartments, primarily due to glutathione depletion and metabolic stress. Maintaining redox homeostasis is important for controlling proliferation and apoptosis in response to specific stimuli for a variety of cells. For T cells, the ability to generate specific response to antigen is dependent on the oxidation state of cell surface and cytoplasmic protein-thiols. Read More

View Article and Full-Text PDF
September 2013

Truncated thioredoxin (Trx-80) promotes pro-inflammatory macrophages of the M1 phenotype and enhances atherosclerosis.

J Cell Physiol 2013 Jul;228(7):1577-83

Unité de Recherche, UR-04, Vieillissement, Stress et Inflammation, Bât. A-6è étage-Case courrier 256, Université Pierre et Marie Curie, Paris Cedex, France.

Vascular cells are particularly susceptible to oxidative stress that is believed to play a key role in the pathogenesis of cardiovascular disorders. Thioredoxin-1 (Trx-1) is an oxidative stress-limiting protein with anti-inflammatory and anti-apoptotic properties. In contrast, its truncated form (Trx-80) exerts pro-inflammatory effects. Read More

View Article and Full-Text PDF

Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1.

J Biol Chem 2012 Dec 26;287(51):43071-82. Epub 2012 Oct 26.

Laboratório de Espectrometria de Massas, Laboratório Nacional de Biociências, LNBio, Centro Nacional de Pesquisa em Energia e Materiais, Campinas, Brasil.

ADAM17, which is also known as TNFα-converting enzyme, is the major sheddase for the EGF receptor ligands and is considered to be one of the main proteases responsible for the ectodomain shedding of surface proteins. How a membrane-anchored proteinase with an extracellular catalytic domain can be activated by inside-out regulation is not completely understood. We characterized thioredoxin-1 (Trx-1) as a partner of the ADAM17 cytoplasmic domain that could be involved in the regulation of ADAM17 activity. Read More

View Article and Full-Text PDF
December 2012

Thioredoxin-1 promotes anti-inflammatory macrophages of the M2 phenotype and antagonizes atherosclerosis.

Arterioscler Thromb Vasc Biol 2012 Jun 19;32(6):1445-52. Epub 2012 Apr 19.

Unité de Recherche, UR-04, Vieillissement, Stress et Inflammation, Université Pierre et Marie Curie, Paris, France.

Objective: Oxidative stress is believed to play a key role in cardiovascular disorders. Thioredoxin (Trx) is an oxidative stress-limiting protein with anti-inflammatory and antiapoptotic properties. Here, we analyzed whether Trx-1 might exert atheroprotective effects by promoting macrophage differentiation into the M2 anti-inflammatory phenotype. Read More

View Article and Full-Text PDF

Truncated and full-length thioredoxin-1 have opposing activating and inhibitory properties for human complement with relevance to endothelial surfaces.

J Immunol 2012 Apr 19;188(8):4103-12. Epub 2012 Mar 19.

Section of Medical Protein Chemistry, Department of Laboratory Medicine, Lund University, S-205 02 Malmö, Sweden.

Thioredoxin (Trx)-1 is a small, ubiquitously expressed redox-active protein with known important cytosolic functions. However, Trx1 is also upregulated in response to various stress stimuli, is found both at the cell surface and secreted into plasma, and has known anti-inflammatory and antiapoptotic properties. Previous animal studies have demonstrated that exogenous Trx1 delivery can have therapeutic effects in a number of disease models and have implicated an interaction of Trx1 with the complement system. Read More

View Article and Full-Text PDF

Increased thioredoxin-1 production in human naturally occurring regulatory T cells confers enhanced tolerance to oxidative stress.

Blood 2011 Jan 28;117(3):857-61. Epub 2010 Oct 28.

Department of Oncology and Pathology, Cancer Center Karolinska, Karolinska Institutet, Stockholm, Sweden.

Levels of regulatory T cells (Tregs) are increased in different cancer types as well as in inflammatory diseases, such as rheumatoid arthritis. Treg accumulation may result from aberrant proliferation and trafficking as well as greater resilience to oxidative stress compared with conventional T cells. This enhanced antioxidative capacity of Tregs possibly serves as feedback inhibition during inflammation and prevents uncontrolled immune reactions by favoring survival of suppressor rather than effector cells. Read More

View Article and Full-Text PDF
January 2011

Naturally occurring free thiols within beta 2-glycoprotein I in vivo: nitrosylation, redox modification by endothelial cells, and regulation of oxidative stress-induced cell injury.

Blood 2010 Sep 15;116(11):1961-70. Epub 2010 Jun 15.

Department of Immunology, Allergy, and Infectious Diseases, University of New South Wales, Sydney, Australia.

β2-Glycoprotein I (β2GPI) is an evolutionary conserved, abundant circulating protein. Although its function remains uncertain, accumulated evidence points toward interactions with endothelial cells and components of the coagulation system, suggesting a regulatory role in vascular biology. Our group has shown that thioredoxin 1 (TRX-1) generates free thiols in β2GPI, a process that may have a regulatory role in platelet adhesion. Read More

View Article and Full-Text PDF
September 2010
  • Page 1 of 1