GlutaredoxinV1, Main, Exploration, bibRecord, 000686

A comparison of reversible versus irreversible protein glutathionylation.

Identifieur interne : 000686 ( Main/Exploration ); précédent : 000685; suivant : 000687

A comparison of reversible versus irreversible protein glutathionylation.

Auteurs : Danyelle M. Townsend [États-Unis] ; Volodymyr I. Lushchak [Ukraine] ; Arthur J L. Cooper [États-Unis]

Source :

Advances in cancer research [ 2162-5557 ] ; 2014.

RBID : pubmed:24974182

Descripteurs français

KwdFr :
- Alanine (analogues et dérivés), Alanine (composition chimique), Amino-butyrates (composition chimique), Cristallin (métabolisme), Disulfure de glutathion (MeSH), Enzymes (composition chimique), Espèces réactives de l'oxygène (MeSH), Glutarédoxines (composition chimique), Glutathion (composition chimique), Glutathion (physiologie), Glutathione transferase (composition chimique), Humains (MeSH), Peptides (composition chimique), Protéines (composition chimique), Régulation de l'expression des gènes tumoraux (MeSH), Transduction du signal (MeSH), Tumeurs (métabolisme).
MESH :
- analogues et dérivés : Alanine.
- composition chimique : Alanine, Amino-butyrates, Enzymes, Glutarédoxines, Glutathion, Glutathione transferase, Peptides, Protéines.
- métabolisme : Cristallin, Tumeurs.
- physiologie : Glutathion.
- Disulfure de glutathion, Espèces réactives de l'oxygène, Humains, Régulation de l'expression des gènes tumoraux, Transduction du signal.

English descriptors

KwdEn :
- Alanine (analogs & derivatives), Alanine (chemistry), Aminobutyrates (chemistry), Enzymes (chemistry), Gene Expression Regulation, Neoplastic (MeSH), Glutaredoxins (chemistry), Glutathione (chemistry), Glutathione (physiology), Glutathione Disulfide (MeSH), Glutathione Transferase (chemistry), Humans (MeSH), Lens, Crystalline (metabolism), Neoplasms (metabolism), Peptides (chemistry), Proteins (chemistry), Reactive Oxygen Species (MeSH), Signal Transduction (MeSH).
MESH :
- chemical , analogs & derivatives : Alanine.
- chemical , chemistry : Alanine, Aminobutyrates, Enzymes, Glutaredoxins, Glutathione, Glutathione Transferase, Peptides, Proteins.
- chemical , physiology : Glutathione.
- metabolism : Lens, Crystalline, Neoplasms.
- Gene Expression Regulation, Neoplastic, Glutathione Disulfide, Humans, Reactive Oxygen Species, Signal Transduction.

Abstract

Glutathionylation is generally a reversible posttranslational modification that occurs to cysteine residues that have been exposed to reactive oxygen species (P-SSG). This cyclical process can regulate various clusters of proteins, including those involved in critical cellular signaling functions. However, certain conditions can favor the formation of dehydroamino acids, such as 2,3-didehydroalanine (2,3-dehydroalanine, DHA) and 2,3-didehydrobutyrine (2,3-dehydrobutyrine), which can act as Michael acceptors. In turn, these can form Michael adducts with glutathione (GSH), resulting in the formation of a stable thioether conjugate, an irreversible process referred to as nonreducible glutathionylation. This is predicted to be prevalent in nature, particularly in more slowly turning over proteins. Such nonreducible glutathionylation can be distinguished from the more facile cycling signaling processes and is predicted to be of gerontological, toxicological, pharmacological, and oncological relevance. Here, we compare reversible and irreversible glutathionylation.

DOI: 10.1016/B978-0-12-420117-0.00005-0
PubMed: 24974182
PubMed Central: PMC4603650

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000616
to stream Main, to step Curation: 000616

Le document en format XML

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<term>Aminobutyrates (chemistry)</term>
<term>Enzymes (chemistry)</term>
<term>Gene Expression Regulation, Neoplastic (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutathione (chemistry)</term>
<term>Glutathione (physiology)</term>
<term>Glutathione Disulfide (MeSH)</term>
<term>Glutathione Transferase (chemistry)</term>
<term>Humans (MeSH)</term>
<term>Lens, Crystalline (metabolism)</term>
<term>Neoplasms (metabolism)</term>
<term>Peptides (chemistry)</term>
<term>Proteins (chemistry)</term>
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<term>Cristallin (métabolisme)</term>
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<term>Espèces réactives de l'oxygène (MeSH)</term>
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<term>Glutathion (physiologie)</term>
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<term>Peptides (composition chimique)</term>
<term>Protéines (composition chimique)</term>
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<front><div type="abstract" xml:lang="en">Glutathionylation is generally a reversible posttranslational modification that occurs to cysteine residues that have been exposed to reactive oxygen species (P-SSG). This cyclical process can regulate various clusters of proteins, including those involved in critical cellular signaling functions. However, certain conditions can favor the formation of dehydroamino acids, such as 2,3-didehydroalanine (2,3-dehydroalanine, DHA) and 2,3-didehydrobutyrine (2,3-dehydrobutyrine), which can act as Michael acceptors. In turn, these can form Michael adducts with glutathione (GSH), resulting in the formation of a stable thioether conjugate, an irreversible process referred to as nonreducible glutathionylation. This is predicted to be prevalent in nature, particularly in more slowly turning over proteins. Such nonreducible glutathionylation can be distinguished from the more facile cycling signaling processes and is predicted to be of gerontological, toxicological, pharmacological, and oncological relevance. Here, we compare reversible and irreversible glutathionylation.</div>
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<Abstract><AbstractText>Glutathionylation is generally a reversible posttranslational modification that occurs to cysteine residues that have been exposed to reactive oxygen species (P-SSG). This cyclical process can regulate various clusters of proteins, including those involved in critical cellular signaling functions. However, certain conditions can favor the formation of dehydroamino acids, such as 2,3-didehydroalanine (2,3-dehydroalanine, DHA) and 2,3-didehydrobutyrine (2,3-dehydrobutyrine), which can act as Michael acceptors. In turn, these can form Michael adducts with glutathione (GSH), resulting in the formation of a stable thioether conjugate, an irreversible process referred to as nonreducible glutathionylation. This is predicted to be prevalent in nature, particularly in more slowly turning over proteins. Such nonreducible glutathionylation can be distinguished from the more facile cycling signaling processes and is predicted to be of gerontological, toxicological, pharmacological, and oncological relevance. Here, we compare reversible and irreversible glutathionylation.</AbstractText>
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<ReferenceList><Reference><Citation>Chem Res Toxicol. 2009 Jun;22(6):1050-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19480392</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2008 Oct 21;47(42):11144-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18816065</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biopolymers. 1999 Apr;49(4):329-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10079771</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1979 Nov;76(11):5606-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">42902</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biochem. 2005 Apr;272(1-2):133-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16010980</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 Jul 20;282(29):21169-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17513866</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Invest. 2011 Dec;29(10):655-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22085269</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1983 Apr 29;220(4596):472-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6836290</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Expert Opin Drug Metab Toxicol. 2011 Jul;7(7):891-910</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21557709</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Amino Acids. 2012;2012:736837</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22500213</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Pharmacol Exp Ther. 2008 Dec;327(3):770-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18791061</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1975 Feb 25;250(4):1422-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1112810</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Aspects Med. 2010 Apr;31(2):145-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20206201</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Xenobiotica. 2012 Dec;42(12):1170-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22725664</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Semin Cell Dev Biol. 2011 May;22(3):278-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21310260</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Vis. 2008;14:862-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18490958</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Org Biomol Chem. 2005 Sep 21;3(18):3357-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16132097</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2012 Jan 27;287(5):3454-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22094463</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Sci. 2004 May;95(5):454-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15132775</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2013 Mar 8;432(2):291-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23396059</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2012 Apr 1;443(1):213-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22188542</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Drug Saf. 2008;31(2):127-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18217789</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Pharmacol. 2007 May 1;73(9):1257-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17098212</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1963 Nov;50:931-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14082360</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Biol Interact. 1990;73(1):77-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2154337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Interv. 2007 Dec;7(6):313-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18199853</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Exp Eye Res. 2004 Oct;79(4):499-512</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15381034</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Drug Metab Dispos. 2008 Aug;36(8):1546-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18474673</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>MBio. 2013;4(1):e00033-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23386433</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Aug 28;284(35):23364-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19561357</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2013;527:113-28</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23830628</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2005 Jul-Aug;7(7-8):930-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15998248</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biosci Bioeng. 2009 May;107(5):475-87</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19393544</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Metallomics. 2011 Nov;3(11):1119-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21804974</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2012 Oct 19;338(6105):387-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22983711</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2001 Aug 31;293(5535):1666-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11533492</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acc Chem Res. 2011 Sep 20;44(9):730-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21563755</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Chromatogr B Biomed Sci Appl. 1999 Jun 25;730(1):25-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10437668</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Drug Metab Rev. 2011 May;43(2):179-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21351850</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Philos Trans R Soc Lond B Biol Sci. 2005 Dec 29;360(1464):2355-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16321806</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2012 Mar 15;16(6):471-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22136616</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1950 Jun;184(2):633-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15428447</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 1983;52:711-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6137189</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Amino Acids. 2011 Jun;41(1):7-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20306345</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1980 Jun 10;255(11):5281-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7372636</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Free Radic Biol Med. 1999 Nov;27(9-10):916-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10569624</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 1966 Aug 20;88(16):3851-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5916376</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1981 Sep 10;256(17):9167-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7021557</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1983 May 25;258(10):6030-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6343368</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2013 Sep 13;288(37):26497-504</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23861399</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Jan 2;284(1):436-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18990698</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Free Radic Biol Med. 2013 Jan;54:51-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23108103</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Res Toxicol. 2012 Dec 17;25(12):2670-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23106594</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Phys Chem B. 2008 Oct 16;112(41):13091-100</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18811194</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Aquat Toxicol. 2008 Apr 28;87(2):108-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18304661</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Natl Cancer Inst. 1947 Aug;8(1):35-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20259027</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Comp Biochem Physiol C Toxicol Pharmacol. 2011 Mar;153(2):175-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20959147</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Mol Med. 2009 Sep;15(9):391-404</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19726230</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2004 May 1;379(Pt 3):595-600</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14763903</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2012 Sep 18;109(38):15115-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22949699</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 1973 Nov 1;39(1):301-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4770799</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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A comparison of reversible versus irreversible protein glutathionylation.

A comparison of reversible versus irreversible protein glutathionylation.

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