Literature DB >> 16607396

The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress.

Seema Chakravarthi1, Catherine E Jessop, Neil J Bulleid.   

Abstract

Glutathione is a ubiquitous molecule found in all parts of the cell where it fulfils a range of functions from detoxification to protection from oxidative damage. It provides the main redox buffer for cells and as such has been implicated in the formation of native disulphide bonds. However, the discovery of the enzyme Ero1 has called into question the exact role of glutathione in this process. In this review, we discuss the arguments for and against a role for glutathione in facilitating disulphide-bond formation and consider its role in protecting the cell from endoplasmic-reticulum-generated oxidative stress.

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Year:  2006        PMID： 16607396      PMCID： PMC1456887          DOI： 10.1038/sj.embor.7400645

Source DB:  PubMed          Journal:  EMBO Rep        ISSN： 1469-221X            Impact factor:   8.807


  32 in total

1.  Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes.

Authors:  Maddalena Fratelli; Hans Demol; Magda Puype; Simona Casagrande; Ivano Eberini; Mario Salmona; Valentina Bonetto; Manuela Mengozzi; Francis Duffieux; Emeric Miclet; Angela Bachi; Joel Vandekerckhove; Elisabetta Gianazza; Pietro Ghezzi
Journal:  Proc Natl Acad Sci U S A       Date:  2002-03-19       Impact factor: 11.205

2.  Oxidized redox state of glutathione in the endoplasmic reticulum.

Authors:  C Hwang; A J Sinskey; H F Lodish
Journal:  Science       Date:  1992-09-11       Impact factor: 47.728

Review 3.  Signaling the unfolded protein response from the endoplasmic reticulum.

Authors:  Kezhong Zhang; Randal J Kaufman
Journal:  J Biol Chem       Date:  2004-04-07       Impact factor: 5.157

4.  The endoplasmic reticulum membrane is permeable to small molecules.

Authors:  Sylvie Le Gall; Andrea Neuhof; Tom Rapoport
Journal:  Mol Biol Cell       Date:  2003-11-14       Impact factor: 4.138

5.  Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.

Authors:  Seema Chakravarthi; Neil J Bulleid
Journal:  J Biol Chem       Date:  2004-07-14       Impact factor: 5.157

6.  Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death.

Authors:  Cole M Haynes; Eric A Titus; Antony A Cooper
Journal:  Mol Cell       Date:  2004-09-10       Impact factor: 17.970

7.  Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase.

Authors:  J S Weissman; P S Kim
Journal:  Nature       Date:  1993-09-09       Impact factor: 49.962

8.  Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer.

Authors:  M M Lyles; H F Gilbert
Journal:  Biochemistry       Date:  1991-01-22       Impact factor: 3.162

9.  Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell.

Authors:  Einav Gross; David B Kastner; Chris A Kaiser; Deborah Fass
Journal:  Cell       Date:  2004-05-28       Impact factor: 41.582

10.  Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.

Authors:  Silvia Nerini Molteni; Anna Fassio; Maria Rosa Ciriolo; Giuseppe Filomeni; Elena Pasqualetto; Claudio Fagioli; Roberto Sitia
Journal:  J Biol Chem       Date:  2004-05-25       Impact factor: 5.157
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  138 in total

Review 1.  Molecular targeting of proteins by L-homocysteine: mechanistic implications for vascular disease.

Authors:  Alla V Glushchenko; Donald W Jacobsen
Journal:  Antioxid Redox Signal       Date:  2007-11       Impact factor: 8.401

Review 2.  The oxidative protein folding machinery in plant cells.

Authors:  Isabel Aller; Andreas J Meyer
Journal:  Protoplasma       Date:  2012-10-23       Impact factor: 3.356

3.  Photoinduced heterodisulfide metathesis for reagent-free synthesis of polymer nanoparticles.

Authors:  Longyu Li; Cunfeng Song; Matthew Jennings; S Thayumanavan
Journal:  Chem Commun (Camb)       Date:  2015-01-28       Impact factor: 6.222

Review 4.  Generating disulfides with the Quiescin-sulfhydryl oxidases.

Authors:  Erin J Heckler; Pumtiwitt C Rancy; Vamsi K Kodali; Colin Thorpe
Journal:  Biochim Biophys Acta       Date:  2007-10-12

5.  Reactivity-Based Probe of the Iron(II)-Dependent Interactome Identifies New Cellular Modulators of Ferroptosis.

Authors:  Ying-Chu Chen; Juan A Oses-Prieto; Lauren E Pope; Alma L Burlingame; Scott J Dixon; Adam R Renslo
Journal:  J Am Chem Soc       Date:  2020-10-30       Impact factor: 15.419

Review 6.  Redox Signaling by Reactive Electrophiles and Oxidants.

Authors:  Saba Parvez; Marcus J C Long; Jesse R Poganik; Yimon Aye
Journal:  Chem Rev       Date:  2018-08-27       Impact factor: 60.622

7.  Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine.

Authors:  April A Dukes; Victor S Van Laar; Michael Cascio; Teresa G Hastings
Journal:  J Neurochem       Date:  2008-07-01       Impact factor: 5.372

8.  Polyol accumulation in muscle and liver in a mouse model of type 2 diabetes.

Authors:  Emily J Gallagher; Derek LeRoith; Marilyn Stasinopoulos; Zara Zelenko; Joseph Shiloach
Journal:  J Diabetes Complications       Date:  2016-04-27       Impact factor: 2.852

9.  Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation.

Authors:  Brian M Dixon; Shi-Hua D Heath; Robert Kim; Jung H Suh; Tory M Hagen
Journal:  Antioxid Redox Signal       Date:  2008-05       Impact factor: 8.401

Review 10.  Signaling functions of reactive oxygen species.

Authors:  Henry Jay Forman; Matilde Maiorino; Fulvio Ursini
Journal:  Biochemistry       Date:  2010-02-09       Impact factor: 3.162
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