The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Inactivation of Enzymes of the Glutathione Antioxidant System by Treatment of Cultured Human Keratinocytes with Peroxides
Open accessAbstract
Either metal ions, H2O2, t-butyl hydroperoxide (tBHP), or cumene hydroperoxide (CHP) was added to the medium of cultured human keratinocytes, and the activities of key peroxide-metabolizing enzymes were examined in a sonicated cell supernatant from the treated cells. 200 microM Fe++ +200 microM Fe was without effect on any enzyme activity. 700 microM CHP or tBHP decreased glutathione (GSH) peroxidase activity by 90% after 5 h and by 100% at 20 h, even if the CHP or tBHP was removed from the media after 90 min. H2O2 at 700 microM caused a brief 17% decrease in activity, which was followed by complete recovery. GSH peroxidase was found to be rapidly inactivated in vitro by CHP, but the enzyme was also inactivated at 37 degrees C even in the absence of CHP. GSH prevented both types of inactivation. Consistent with this in vitro data, in vivo depletion of the GSH pool with buthionine sulfoximine led to lower levels of GSH peroxidase and increased sensitivity to peroxide-induced inactivation. Neither GSH reductase nor GSH S-transferase were inactivated by any treatment although CHP did cause a small increase in the activity of the latter, which was not due to induction. The activity of glucose-6-phosphate dehydrogenase was decreased 50% following treatment for 5 h with 700 microM CHP or tBHP, whereas H2O2 treatment caused a brief 15% decline, followed by recovery. The effects of peroxides were not altered by changing the concentration of Ca++ in the media. Catalase was unaffected by concentrations of peroxide up to 700 microM. Inhibition of catalase with aminotriazole slightly enhanced the toxicity of 700 microns H2O2. In summary, organic hydroperoxides at relatively low concentrations inactive key enzymes of the glutathione pathway, but hydrogen peroxide does not.
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“Interestingly, the cellular pool of GSH is also necessary to prevent oxidative inactivation of GPx-1 by excess oxidants (433).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [433]
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Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280
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SCHAFER, M., & WERNER, S. (2008) · Pharmacological Research · doi:10.1016/j.phrs.2008.06.004 · Cited by 902
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Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
Metadata
- Authors
- Vessey, D. A., & Lee, K.-H.
- Affiliations
- San Francisco VA Medical Center (US)
- Venue
- Journal of Investigative Dermatology
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 100
- Issue
- 6
- Pages
- 829-833
- ISSN
- 0022-202X (ISSN-L)
- OpenAlex
- W2009191072
- Cited by
- 45
- References
- 29
- Citations by year
- 2025: 1 · 2021: 1 · 2020: 1 · 2017: 1 · 2014: 2 · 2013: 3 · 2012: 2
- FWCI
- 0.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Investigative Dermatology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR39448, P01AR039448)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- glutathione peroxidase, enzyme inactivation, cumene hydroperoxide, tert-butyl hydroperoxide, hydrogen peroxide, keratinocytes, glutathione pathway, GSH reductase, glucose-6-phosphate dehydrogenase, catalase, buthionine sulfoximine, oxidative stress, 3-amino-1,2,4-triazole, metal ions
- MeSH terms
- Antimetabolites, Benzene Derivatives, Calcium, Catalase, Cells, Cultured, Culture Media, Enzyme Activation, Ferric Compounds, Ferrous Compounds, Glucosephosphate Dehydrogenase, Glutathione, Glutathione Reductase, Humans, Hydrogen Peroxide, Methionine Sulfoximine, Peroxides, Time Factors, Keratinocytes, Oxidants, Buthionine Sulfoximine, tert-Butylhydroperoxide
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