The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Ascorbate recycling in human erythrocytes: Role of GSH in reducing dehydroascorbate
Abstract
Human erythrocytes regenerate ascorbate from its oxidized product, dehydroascorbate. The extent to which such ascorbate recycling occurs by a GSH-dependent mechanism was investigated. In the presence of glucose, erythrocytes took up over 90% of extracellular [14C]dehydroascorbate and rapidly converted it to [14C]ascorbate, which was trapped within the cells. Dehydroascorbate uptake and reduction was not associated with generation of a monoascorbyl free radical intermediate. Uptake and reduction of dehydroascorbate by glucose-depleted erythrocytes coordinately decreased GSH and raised GSSG concentrations in erythrocytes. This effect was reversed by D-glucose, but not by L-lactate. Conversely, depletion of cellular GSH decreased the ability of cells to recycle dehydroascorbate to ascorbate, as reflected in the extent to which cells were able to reduce extracellular ferricyanide. Monoascorbyl free radical was formed during the reduction of extracellular ferricyanide, indicating that one electron transfer steps were involved in this process. In GSH-depleted cells, addition of L-lactate as an energy source for glycolysis-dependent NADH regeneration did cause a partial recovery of the ability of cells to reduce ferricyanide. However, in resealed erythrocyte ghosts containing either 4 mM GSH or 400 mu M NADH, only the GSH-containing ghosts supported regeneration of ascorbate from added dehydroascorbate. These results suggest that in human erythrocytes ascorbate regeneration from dehydroascorbate is largely GSH dependent, and that it occurs through either enzymatic or nonenzymatic reactions not involving the monoascorbyl free radical.
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“Inside the cell, DHA is rapidly reduced back to ascorbate at the expense of GSH and NADPH47,49.”
From Targeting cancer vulnerabilities with high-dose vitamin C (2019) · cites this paper as [49]
Citations
Cites
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Diamide, a new reagent for the intracellular oxidation of glutathione to the disulfide
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Mammalian facilitative hexose transporters mediate the transport of dehydroascorbic acid
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Chappell, L. C., Seed, P. T., Briley, A. L., Kelly, F. J., Lee, R., Hunt, B. J., Parmar, K., Bewley, S., Shennan, A. H., Steer, P. J., et al. (1999) · The Lancet · doi:10.1016/s0140-6736(99)80010-5 · Cited by 784
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Metadata
- Authors
- May, J. M., Qu, Z.-C., Whitesell, R. R., & Cobb, C. E.
- Affiliations
- Vanderbilt University (US)
- Corresponding author
- May, James M.
- ORCID
- May, James M.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 1996
- Volume
- 20
- Issue
- 4
- Pages
- 543-551
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2025497222
- Cited by
- 200
- References
- 27
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 1 · 2021: 7 · 2020: 4 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 6 · 2015: 4 · 2014: 5 · 2013: 8 · 2012: 5
- FWCI
- 10.16
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1s10rr004075-01)
- National Heart, Lung, and Blood Institute (HL34737)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-26657, P30DK026657)
- National Center for Research Resources (RR 04075)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Vitamin C and Antioxidants Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- ascorbate recycling, dehydroascorbic acid, glutathione, human erythrocytes, ascorbate regeneration, ferricyanide reduction, NADH regeneration, glucose, L-lactate, glutathione disulfide, erythrocyte ghosts, single electron transfer
- MeSH terms
- Ascorbic Acid, Dehydroascorbic Acid, Erythrocytes, Ferricyanides, Glutathione, Humans, Oxidation-Reduction
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