The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Quantifying the global cellular thiol–disulfide status
Open accessAbstract
It is widely accepted that the redox status of protein thiols is of central importance to protein structure and folding and that glutathione is an important low-molecular-mass redox regulator. However, the total cellular pools of thiols and disulfides and their relative abundance have never been determined. In this study, we have assembled a global picture of the cellular thiol–disulfide status in cultured mammalian cells. We have quantified the absolute levels of protein thiols, protein disulfides, and glutathionylated protein (PSSG) in all cellular protein, including membrane proteins. These data were combined with quantification of reduced and oxidized glutathione in the same cells. Of the total protein cysteines, 6% and 9.6% are engaged in disulfide bond formation in HEK and HeLa cells, respectively. Furthermore, the steady-state level of PSSG is <0.1% of the total protein cysteines in both cell types. However, when cells are exposed to a sublethal dose of the thiol-specific oxidant diamide, PSSG levels increase to >15% of all protein cysteine. Glutathione is typically characterized as the “cellular redox buffer”; nevertheless, our data show that protein thiols represent a larger active redox pool than glutathione. Accordingly, protein thiols are likely to be directly involved in the cellular defense against oxidative stress.
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An Introduction to Error Analysis
Taylor, J. R. (1982) · Medical Entomology and Zoology · Cited by 2,807
Introduction to Error Analysis
Praktikum, P.-C. (2009) · Cited by 1,295
CORRELATED MORPHOMETRIC AND BIOCHEMICAL STUDIES ON THE LIVER CELL
Weibel, E. R., Stäubli, W., Gnägi, H. R., & Hess, F. A. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.42.1.68 · Cited by 1,141
Imaging Dynamic Redox Changes in Mammalian Cells with Green Fluorescent Protein Indicators
Dooley, C. T., Dore, T. M., Hanson, G. T., Jackson, W. C., Remington, S. J., & Tsien, R. Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312847200 · Cited by 776
Fratelli, M., Demol, H., Puype, M., Casagrande, S., Eberini, I., Salmona, M., Bonetto, V., Mengozzi, M., Duffieux, F., Miclet, E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052592699 · Cited by 556
[2] Thiol/disulfide exchange equilibria and disulfidebond stability
Gilbert, H. F. (1995) · Methods in Enzymology · doi:10.1016/0076-6879(95)51107-5 · Cited by 545
Quantifying changes in the thiol redox proteome upon oxidative stress in vivo
Leichert, L. I., Gehrke, F., Gudiseva, H. V., Blackwell, T., Ilbert, M., Walker, A. K., Strahler, J. R., Andrews, P. C., & Jakob, U. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707723105 · Cited by 519
Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
Gallogly, M. M., & Mieyal, J. J. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2007.06.003 · Cited by 476
Protein Disulfide Bond Formation in the Cytoplasm during Oxidative Stress
Cumming, R. C., Andon, N. L., Haynes, P. A., Park, M., Fischer, W. H., & Schubert, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312267200 · Cited by 462
Protein Sulfhydryls and Their Role in the Antioxidant Function of Protein S-Thiolation
Thomas, J. A., Poland, B., & Honzatko, R. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1261 · Cited by 399
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Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
Glutathione Homeostasis and Functions: Potential Targets for Medical Interventions
Lushchak, V. I. (2012) · Journal of Amino Acids · doi:10.1155/2012/736837 · Cited by 1,266
Chemical Biology of H2S Signaling through Persulfidation
Filipovic, M. R., Zivanovic, J., Alvarez, B., & Banerjee, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00205 · Cited by 1,046
Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837
Reisz, J. A., Bansal, N., Qian, J., Zhao, W., & Furdui, C. M. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5489 · Cited by 833
Metadata
- Authors
- Hansen, R. E., Roth, D., & Winther, J. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-01-13
- Volume
- 106
- Issue
- 2
- Pages
- 422-427
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2010478212
- Cited by
- 424
- References
- 38
- FWCI
- 10.44
- Type
- journal article
- Language
- en
- Open access
- green
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