Glutathione disulfide explained

Glutathione disulfide (GSSG) is a disulfide derived from two glutathione molecules.[1]

In living cells, glutathione disulfide is reduced into two molecules of glutathione with reducing equivalents from the coenzyme NADPH. This reaction is catalyzed by the enzyme glutathione reductase.[2]

Antioxidant enzymes, such as glutathione peroxidases and peroxiredoxins, generate glutathione disulfide during the reduction of peroxides such as hydrogen peroxide (H2O2) and organic hydroperoxides (ROOH):[3]

2 GSH + ROOH → GSSG + ROH + H2O

Other enzymes, such as glutaredoxins, generate glutathione disulfide through thiol-disulfide exchange with protein disulfide bonds or other low molecular mass compounds, such as coenzyme A disulfide or dehydroascorbic acid.[4]

2 GSH + R-S-S-R → GSSG + 2 RSH

The GSH:GSSG ratio is therefore an important bioindicator of cellular health, with a higher ratio signifying less oxidative stress in the organism. A lower ratio may even be indicative of neurodegenerative diseases, such as Parkinson's disease (PD) and Alzheimer's disease.[5]

Neuromodulator

GSSG, along with glutathione and S-nitrosoglutathione (GSNO), have been found to bind to the glutamate recognition site of the NMDA and AMPA receptors (via their γ-glutamyl moieties), and may be endogenous neuromodulators.[6] [7] At millimolar concentrations, they may also modulate the redox state of the NMDA receptor complex.

See also

Notes and References

  1. Meister A, Anderson ME . Glutathione . Annual Review of Biochemistry . 52 . 711–60 . 1983 . 6137189 . 10.1146/annurev.bi.52.070183.003431 .
  2. Deneke SM, Fanburg BL . Regulation of cellular glutathione . The American Journal of Physiology . 257 . 4 Pt 1 . L163–73 . 1989 . 10.1152/ajplung.1989.257.4.L163 . 2572174 . 2017-03-20 . 2020-06-10 . https://web.archive.org/web/20200610200759/https://journals.physiology.org/doi/abs/10.1152/ajplung.1989.257.4.L163?view=reprint&pmid=2572174 . dead .
  3. Meister A . Glutathione metabolism and its selective modification . The Journal of Biological Chemistry . 263 . 33 . 17205–8 . 1988 . 10.1016/S0021-9258(19)77815-6 . 3053703 . free . 2017-03-20 . 2020-06-10 . https://web.archive.org/web/20200610200802/https://www.jbc.org/content/263/33/17205.long . dead .
  4. Holmgren A, Johansson C, Berndt C, Lönn ME, Hudemann C, Lillig CH . Thiol redox control via thioredoxin and glutaredoxin systems . Biochem. Soc. Trans. . 33 . Pt 6 . 1375–7 . December 2005 . 16246122 . 10.1042/BST20051375.
  5. Book: Joshua B. . Owen . D. Allan . Butterfield . Measurement of oxidized/reduced glutathione ratio . Peter . Bross . Niels . Gregersen . Protein Misfolding and Cellular Stress in Disease and Aging . 648 . 269–77 . 2010 . 20700719 . 10.1007/978-1-60761-756-3_18 . Methods in Molecular Biology . 978-1-60761-755-6 .
  6. Steullet P, Neijt HC, Cuénod M, Do KQ . Synaptic plasticity impairment and hypofunction of NMDA receptors induced by glutathione deficit: relevance to schizophrenia . Neuroscience . 137 . 3 . 807–19 . 2006 . 16330153 . 10.1016/j.neuroscience.2005.10.014 . 1417873 .
  7. Varga V, Jenei Z, Janáky R, Saransaari P, Oja SS . Glutathione is an endogenous ligand of rat brain N-methyl-D-aspartate (NMDA) and 2-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptors . Neurochemical Research . 22 . 9 . 1165–71 . 1997 . 9251108 . 10.1023/A:1027377605054 . 24024090 .

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