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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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
Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer
Lyles, M. M., & Gilbert, H. (1991) · Biochemistry · doi:10.1021/bi00217a004 · Cited by 420
Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme
Wetlaufer, D. B., & Saxena, V. (1970) · Biochemistry · doi:10.1021/bi00827a028 · Cited by 397

Show all 36 references

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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Zhang, J., Ji, X., Ren, H., Zhou, J., Chen, Z., Dong, X., & Zhao, W. (2018) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2018.01.016 · Cited by 75
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Foreman, R., Fiebig, A., & Crosson, S. (2012) · Journal of Bacteriology · doi:10.1128/jb.00182-12 · Cited by 75
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm
Jonda, S., Huber‐Wunderlich, M., Glockshuber, R., & Mössner, E. (1999) · The EMBO Journal · doi:10.1093/emboj/18.12.3271 · Cited by 75
The Alternative Pathway of Glutathione Degradation Is Mediated by a Novel Protein Complex Involving Three New Genes in Saccharomyces cerevisiae
Ganguli, D., Kumar, C., & Bachhawat, A. K. (2006) · Genetics · doi:10.1534/genetics.106.066944 · Cited by 75
Isoform Cloning, Actin Binding, and Chromosomal Localization of Human Erythroid Dematin, a Member of the Villin Superfamily
Azim, A. C., Knoll, J. H. M., Beggs, A. H., & Chishti, A. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17407 · Cited by 75
Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90).
Margolese, L., Waneck, G. L., Suzuki, C. K., Degen, E., Flavell, R. A., & Williams, D. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46798-6 · Cited by 75
Signal transduction in photoreceptor histidine kinases
Möglich, A. (2019) · Protein Science · doi:10.1002/pro.3705 · Cited by 74
Bioreducible Liposomes for Gene Delivery: From the Formulation to the Mechanism of Action
Candiani, G., Pezzoli, D., Ciani, L., Chiesa, R., & Ristori, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013430 · Cited by 77
HYDROGEN PEROXIDE INDUCES APOPTOSIS IN HUMAN HEPATOMA CELLS AND ALTERS CELL REDOX STATUS
Li, J., Huang, C., Zheng, R., Cui, K., & Li, J. (2000) · Cell Biology International · doi:10.1006/cbir.1999.0438 · Cited by 74
Chaperones and folding of MHC class I molecules in the endoplasmic reticulum
Paulsson, K. M., & Wang, P. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(03)00048-x · Cited by 74
Posttranscriptional regulation of macrophage tissue factor expression by antioxidants
Brisseau, G. F., Dackiw, A., Cheung, P., Christie, N. A., & Od, R. (1995) · Blood · doi:10.1182/blood.v85.4.1025.bloodjournal8541025 · Cited by 74
FMN reduces Amyloid-β toxicity in yeast by regulating redox status and cellular metabolism
Chen, X., Ji, B., Hao, X., Li, X., Eisele, F., Nyström, T., & Petranović, D. (2020) · Nature Communications · doi:10.1038/s41467-020-14525-4 · Cited by 77
Oxidative Stress Responses and NRF2 in Human Leukaemia
Abdul-Aziz, A. M., MacEwan, D. J., Bowles, K. M., & Rushworth, S. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/454659 · Cited by 73
Engineering of a Recombinant Vitamin K-dependent γ-Carboxylation System with Enhanced γ-Carboxyglutamic Acid Forming Capacity
Wajih, N., Sane, D. C., Hutson, S. M., & Wallin, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413982200 · Cited by 73
An Analysis of the Solution Structure and Signaling Mechanism of LovK, a Sensor Histidine Kinase Integrating Light and Redox Signals
Purcell, E. B., McDonald, C. A., Palfey, B. A., & Crosson, S. (2010) · Biochemistry · doi:10.1021/bi1006404 · Cited by 73
A Novel Group of Glutaredoxins in thecis-Golgi Critical for Oxidative Stress Resistance
Mesecke, N., Spang, A., Deponte, M., & Herrmann, J. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0896 · Cited by 72
An endoplasmic reticulum-selective ratiometric fluorescent probe for imaging a copper pool
Park, S. Y., Kim, W., Park, S.-H., Han, J., Lee, J., Kang, C., & Lee, M. H. (2017) · Chemical Communications · doi:10.1039/c7cc01430a · Cited by 73
Rapid degradation of an unassembled immunoglobulin light chain is mediated by a serine protease and occurs in a pre-Golgi compartment.
Gardner, A. M., Aviel, S., & Argon, Y. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74477-9 · Cited by 73
Balancing oxidative protein folding: The influences of reducing pathways on disulfide bond formation
Kojer, K., & Riemer, J. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.02.004 · Cited by 79
Redox Regulation of the Influenza Hemagglutinin Maturation Process: A New Cell-Mediated Strategy for Anti-Influenza Therapy
Sgarbanti, R., Nencioni, L., Amatore, D., Coluccio, P., Fraternale, A., Sale, P., Mammola, C. L., Carpino, G., Gaudio, E., Magnani, M., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3512 · Cited by 72
Oxidative Stress of Vertebrates and Invertebrates
Felton, G. W. (1995) · Springer eBooks · doi:10.1007/978-1-4615-9689-9_10 · Cited by 72
Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes.
Marquardt, T., Hebert, D. N., & Helenius, A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36561-5 · Cited by 72

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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