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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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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