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Science 11 September 1992: Vol. 257. no. 5076, pp. 1496 - 1502 DOI: 10.1126/science.1523409
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Articles
Science, Vol 257, Issue 5076, 1496-1502
Copyright © 1992 by American Association for the Advancement of Science
Oxidized redox state of glutathione in the endoplasmic reticulum
C Hwang,
AJ Sinskey,
and
HF Lodish
Department of Biology, Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.
The redox state of the endoplasmic reticulum (ER) was measured with the peptide N-Acetyl-Asn-Tyr-Thr-Cys-NH2. 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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PNAS
99, 3505-3510
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- Evidence for an initiation site for hen lysozyme folding from the reduced form using its dissected peptide fragments.
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Protein Eng. Des. Sel.
14, 829-833
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- Rearrangement of Nicotinic Receptor {alpha} Subunits during Formation of the Ligand Binding Sites.
- M. Mitra, C. P. Wanamaker, and W. N. Green (2001)
J. Neurosci.
21, 3000-3008
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J. Cell Sci.
114, 1273-1282
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Am J Physiol Lung Cell Mol Physiol
279, L1005-L1028
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- Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum.
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Science
290, 1571-1574
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- Biogenesis of the Chloroplast-Encoded D1 Protein: Regulation of Translation Elongation, Insertion, and Assembly into Photosystem II.
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PLANT CELL
12, 1769-1782
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- Glutathione synthesis is essential for mouse development but not for cell growth in culture.
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PNAS
97, 5101-5106
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J. Nutr.
130, 1455S-1458
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- Hgt1p, a High Affinity Glutathione Transporter from the Yeast Saccharomyces cerevisiae.
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275, 13259-13265
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- Specific Chaperone-like Activity of Inhibitor of Caspase-activated DNase for Caspase-activated DNase.
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275, 8091-8096
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Plant Physiology
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- Yeast flavin-containing monooxygenase is induced by the unfolded protein response.
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PNAS
97, 121-126
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PNAS
96, 11723-11728
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