The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Abstract
The redox state of the endoplasmic reticulum (ER) was measured with the peptide N -Acetyl-Asn-Tyr-Thr-Cys-NH 2 . The peptide diffused across cellular membranes; some became glycosylated and thus trapped within the secretory pathway, and its cysteine residue underwent reversible thiol-disulfide exchanges with the surrounding redox buffer. Glycosylated peptides from cells were disulfide-linked to glutathione, indicating that glutathione is the major redox buffer in the secretory pathway. The redox state of the secretory pathway was more oxidative than that of the cytosol; the ratio of reduced glutathione to the disulfide form (GSH/GSSG) within the secretory pathway ranged from 1:1 to 3:1, whereas the overall cellular GSH/GSSG ratio ranged from 30:1 to 100:1. Cytosolic glutathione was also transported into the lumen of microsomes in a cell-free system. Although how the ER maintains an oxidative environment is not known, these results suggest that the demonstrated preferential transport of GSSG compared to GSH into the ER lumen may contribute to this redox compartmentation.
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“The GSH/GSSG ratio is a good marker of oxidative stress of an organism (Hwang et al. 1992).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Hwang et al. 1992
In the citing paper
“In the cells, the GSH/GSS ratio is greater than 30, and in the serum is about 10 times lower (Hwang et al. 1992).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Hwang et al. 1992
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
[70] Determination of glutathione and glutathione disulfide in biological samples
Anderson, M. E. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(85)13073-9 · Cited by 2,755
The Glutathione Status of Cells
Kosower, N. S., & Kosower, E. M. (1978) · International review of cytology · doi:10.1016/s0074-7696(08)60166-7 · Cited by 1,211
ROLE OF REVERSIBLE OXIDATION-REDUCTION OF ENZYME THIOLS-DISULFIDES IN METABOLIC REGULATION
Ziegler, D. M. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.001513 · Cited by 838
Evidence That the Leucine Zipper Is a Coiled Coil
O’Shea, E. K., Rutkowski, R., & Kim, P. S. (1989) · Science · doi:10.1126/science.2911757 · Cited by 837
Molecular and Cellular Aspects of Thiol–Disulfide Exchange
Gilbert, H. (1990) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123096.ch2 · Cited by 770
[6] Preparation of microsomal membranes for cotranslational protein translocation
Walter, P., & Blobel, G. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(83)96010-x · Cited by 656
The rate of bulk flow from the endoplasmic reticulum to the cell surface
Wieland, F., Gleason, M. L., Serafini, T. A., & Rothman, J. E. (1987) · Cell · doi:10.1016/0092-8674(87)90224-8 · Cited by 534
Lyles, M. M., & Gilbert, H. (1991) · Biochemistry · doi:10.1021/bi00217a004 · Cited by 420
Wetlaufer, D. B., & Saxena, V. (1970) · Biochemistry · doi:10.1021/bi00827a028 · Cited by 397
Research works printed but not linked: 1
- Cotgreave, I. A., Sulfur- Containing Drugs and Related Organic Compounds. Chemistry, Biochemistry, and Toxicology. Analytical, Biochemical, and Toxicological Aspects of Sulphur Xenobiochemistry 2: 101 (1989).
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Free radicals, metals and antioxidants in oxidative stress-induced cancer
Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680
Reactive Oxygen Species in Inflammation and Tissue Injury
Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
Reactive oxygen species in cell signaling
Thannickal, V. J., & Fanburg, B. L. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.6.l1005 · Cited by 2,950
Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638
Metadata
- Authors
- Hwang, C., Sinskey, A. J., & Lodish, H. F.
- Affiliations
- Whitehead Institute for Biomedical Research (US)
- Venue
- Science
- Published
- 1992-09-11
- Volume
- 257
- Issue
- 5076
- Pages
- 1496-1502
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2050994990
- Cited by
- 1,968
- References
- 36
- Citations by year
- 2026: 37 · 2025: 43 · 2024: 56 · 2023: 61 · 2022: 64 · 2021: 67 · 2020: 61 · 2019: 71 · 2018: 75 · 2017: 65 · 2016: 53 · 2015: 78 · 2014: 80 · 2013: 68 · 2012: 84
- FWCI
- 17.30
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione, endoplasmic reticulum, redox state, secretory pathway, disulfide exchange, GSH/GSSG ratio, redox buffer, thiol-disulfide exchange, glycosylation
- MeSH terms
- Amino Acid Sequence, Animals, Chromatography, High Pressure Liquid, Chromatography, Thin Layer, Dogs, Endoplasmic Reticulum, Glutathione, Kinetics, Microsomes, Models, Biological, Molecular Sequence Data, Oligopeptides, Oxidation-Reduction, Pancreas, Glutathione Disulfide
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