Literature DB >> 20682242

Redox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse.

José Rodrigo Godoy1, Maria Funke, Waltraud Ackermann, Petra Haunhorst, Sabrina Oesteritz, Francisco Capani, Hans-Peter Elsässer, Christopher Horst Lillig.   

Abstract

BACKGROUND: Oxidoreductases of the thioredoxin family of proteins have been thoroughly studied in numerous cellular and animal models mimicking human diseases. Despite of their well documented role in various disease conditions, no systematic information on the presence of these proteins is available.
METHODS: Here, we have systematically analyzed the presence of some of the major constituents of the glutaredoxin (Grx)-, peroxiredoxin (Prx)-, and thioredoxin (Trx)-systems, i.e. Grx1, Grx2, Grx3 (TXNL-2/PICOT), Grx5, nucleoredoxin (Nrx), Prx1, Prx2, Prx3, Prx4, Prx5, Prx6, Trx1, thioredoxin reductase 1 (TrxR1), Trx2, TrxR2, and γ-glutamyl cysteine synthetase (γ-GCS) in various tissues of the mouse using immunohistochemistry.
RESULTS: The identification of the Trx family proteins in the central nervous system, sensory organs, digestive system, lymphatic system, reproductive system, urinary system, respiratory system, endocrine system, skin, heart, and muscle revealed a number of significant differences between these proteins with respect to their distribution in these tissues.
CONCLUSION: Our results imply more specific functions and interactions between the proteins of this family than previously assumed. GENERAL SIGNIFICANCE: Crucial functions of Trx family proteins have been demonstrated in various disease conditions. A detailed overview on their distribution in various tissues will be helpful to fully comprehend their potential role and the interactions of these proteins in the most thoroughly studied model for human diseases-the laboratory mouse. This article is part of a Special Issue entitled Human and Murine Redox Protein Atlases.
Copyright © 2010 Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20682242     DOI: 10.1016/j.bbagen.2010.05.006

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  48 in total

1.  Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.

Authors:  Eva-Maria Hanschmann; Maria Elisabet Lönn; Lena Dorothee Schütte; Maria Funke; José R Godoy; Susanne Eitner; Christoph Hudemann; Christopher Horst Lillig
Journal:  J Biol Chem       Date:  2010-10-07       Impact factor: 5.157

2.  Peroxiredoxin 2 deficiency exacerbates atherosclerosis in apolipoprotein E-deficient mice.

Authors:  Jong-Gil Park; Ji-Young Yoo; Se-Jin Jeong; Jae-Hoon Choi; Mi-Ran Lee; Mi-Ni Lee; Jeong Hwa Lee; Hyoung Chin Kim; Hanjoong Jo; Dae-Yeul Yu; Sang Won Kang; Sue Goo Rhee; Mun-Han Lee; Goo Taeg Oh
Journal:  Circ Res       Date:  2011-08-11       Impact factor: 17.367

Review 3.  Redox biology of the intestine.

Authors:  Magdalena L Circu; Tak Yee Aw
Journal:  Free Radic Res       Date:  2011-09-05

Review 4.  Proteostasis and REDOX state in the heart.

Authors:  Elisabeth S Christians; Ivor J Benjamin
Journal:  Am J Physiol Heart Circ Physiol       Date:  2011-10-14       Impact factor: 4.733

5.  Aging impairs induction of redox factor-1 after heat stress: a potential mechanism for heat-induced liver injury.

Authors:  Leslee M Sholomskas; Kathryn L Roche; Steven A Bloomer
Journal:  Int J Physiol Pathophysiol Pharmacol       Date:  2015-03-20

Review 6.  Thiol-redox signaling, dopaminergic cell death, and Parkinson's disease.

Authors:  Aracely Garcia-Garcia; Laura Zavala-Flores; Humberto Rodriguez-Rocha; Rodrigo Franco
Journal:  Antioxid Redox Signal       Date:  2012-05-03       Impact factor: 8.401

Review 7.  The thioredoxin system in neonatal lung disease.

Authors:  Trent E Tipple
Journal:  Antioxid Redox Signal       Date:  2014-03-13       Impact factor: 8.401

8.  Proteomic analysis on the alteration of protein expression in the early-stage placental villous tissue of electromagnetic fields associated with cell phone exposure.

Authors:  Qiong Luo; Ying Jiang; Min Jin; Jian Xu; He-Feng Huang
Journal:  Reprod Sci       Date:  2013-02-18       Impact factor: 3.060

9.  How the location of superoxide generation influences the β-cell response to nitric oxide.

Authors:  Katarzyna A Broniowska; Bryndon J Oleson; Jennifer McGraw; Aaron Naatz; Clayton E Mathews; John A Corbett
Journal:  J Biol Chem       Date:  2015-02-03       Impact factor: 5.157

10.  Sex- and structure-specific differences in antioxidant responses to methylmercury during early development.

Authors:  Joanna A Ruszkiewicz; Aaron B Bowman; Marcelo Farina; João B T Rocha; Michael Aschner
Journal:  Neurotoxicology       Date:  2016-07-22       Impact factor: 4.294

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