Cited by 1,968Redox biology and oxidative stressSulfur Compounds in BiologyGlutathione Transferases and Polymorphisms

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Oxidized Redox State of Glutathione in the Endoplasmic Reticulum

Hwang, Christopher, Sinskey, Anthony J., Lodish, Harvey F.·1992·Science

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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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Authors: Hwang, C., Sinskey, A. J., & Lodish, H. F.
Affiliations: Whitehead Institute for Biomedical Research (US)
ORCID: Sinskey, Anthony J.
Lodish, Harvey F.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1992-09-11
Volume: 257
Issue: 5076
Pages: 1496-1502
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1523409
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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Oxidized Redox State of Glutathione in the Endoplasmic Reticulum

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