The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with πGST
Open accessAbstract
1-cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily, can protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols. However, purified native or recombinant enzyme in vitro generally lacks GSH peroxidase (GPx) activity because of oxidation of its single conserved cysteine. Reduction of the resultant oxidized cysteine is difficult because of its protected location within the homodimer formed by the oxidized protein monomers. Partial purification of 1-cysPrx from bovine lung revealed the presence of πGST in an active preparation, while purification to homogeneity yielded enzyme that inactivated with time. We show that heterodimerization of 1-cysPrx with GSH-saturated πGST results in glutathionylation of the oxidized cysteine in 1-cysPrx followed by subsequent spontaneous reduction of the mixed disulfide and restoration of enzymatic activity. Maximum activation of 1-cysPrx occurred with a 1:1 molar ratio of GSH-saturated πGST and a 2:1 molar ratio of GSH to 1-cysPrx. Liposome-mediated delivery of oxidized recombinant enzyme into NCI-H441 cells that lack 1-cysPrx but express πGST resulted in 1-cysPrx activation, whereas activation in MCF7 cells required co-delivery of πGST. Our data indicate a physiological mechanism for glutathionylation of the oxidized catalytic cysteine of 1-cysPrx by its heterodimerization with πGST followed by its GSH-mediated reduction and enzyme activation.
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Cites
Structure, mechanism and regulation of peroxiredoxins
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Self-citationCharacterization of a Mammalian Peroxiredoxin That Contains One Conserved Cysteine
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Metabolic Enzymes of Mycobacteria Linked to Antioxidant Defense by a Thioredoxin-Like Protein
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Phospholipid Hydroperoxides Are Substrates for Non-selenium Glutathione Peroxidase
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Oxidative Stress and Antioxidant Defense
Birben, E., Sahiner, U. M., Sackesen, C., Erzurum, S., & Kalayci, O. (2012) · World Allergy Organization Journal · doi:10.1097/wox.0b013e3182439613 · Cited by 4,935
Glutathione: new roles in redox signaling for an old antioxidant
Aquilano, K., Baldelli, S., & Ciriolo, M. R. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00196 · Cited by 865
Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784
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Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603
Molecular Mechanisms and Clinical Implications of Reversible Protein S -Glutathionylation
Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., & Shelton, M. D. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2089 · Cited by 523
Metadata
- Authors
- Manevich, Y., Feinstein, S. I., & Fisher, A. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-03-02
- Volume
- 101
- Issue
- 11
- Pages
- 3780-3785
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2143372650
- Cited by
- 349
- References
- 32
- FWCI
- 6.56
- Type
- journal article
- Language
- en
- Open access
- green
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- Manevich, Y., Feinstein, S. I., & Fisher, A. B. (2004). Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with πGST. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0400181101
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