Ammonia production and glutamine incorporation into glutathione in the functioning rat kidney
Abstract
Incorporation of glutamine's γ-glutamyl moiety into glutathione was studied in the isolated perfused rat kidney under two conditions: (1) a resting state and (2) during reabsorption of a filtered glycylglycine load (designed to stimulate glutathione breakdown). Glutamine uptake and ammonia production were monitored simultaneously with [14 C]glutamine (γ-glutamyl moiety) incorporation into glutathione.Renal glutathione content was highly dependent upon the presence of glutamine; in its absence, glutathione levels fell 40% in 30 min indicating synthesis does not keep pace with degradation. Presenting the kidney with a glycylglycine load doubled the rate of glutathione degradation. However, perfusing kidneys with physiological L-glutamine concentration (1 mM) maintained glutathione levels significantly above those in glutamine's absence in either condition 1 or 2. Evidence that glutamine functions as the γ-glutamyl donor in glutathione synthesis was established by the significant incorporation of [14 C]glutamine into glutathione during condition 1 and the accelerated incorporation rate during glycylglycine loading (condition 2). Stimulating glutathione breakdown (condition 2) resulted in a significant increase in renal glutamine uptake and ammonia production apparently via the γ-glutamyltransferase pathway since inhibiting this activity blocked the incremental rise in glutamine uptake during glycylglycine loading. These results are consistent with the interpretation that stimulating γ-glutamyl cycle activity with a γ-glutamyl acceptor (glycylglycine) accelerates γ-glutamyl donor uptake (glutamine) and ammonia production via the γ-glutamyltransferase pathway.
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Glutamine is the rate-limiting factor in glutathione synthesis.
“Glutamine is considered the rate-limiting factor in glutathione synthesis58,59.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [58]
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Wang, M., Wang, K., Liu, X., Shi, M., Zhang, H., Zhang, X., Wei, R., Li, N., Pan, W., & Tang, B. (2023) · Chemical Communications · doi:10.1039/d3cc00487b · Cited by 3 · see citing works
Akmansu, M. (2018) · Turkish Journal of Oncology · doi:10.5505/tjo.2018.1803 · Cited by 3 · see citing works
- Authors
- Welbourne, T. C.
- Corresponding author
- Welbourne, T. C.
- Venue
- Canadian Journal of Biochemistry
- Publisher
- Canadian Science Publishing
- Published
- 1979-03-01
- Volume
- 57
- Issue
- 3
- Pages
- 233-237
- ISSN
- 0008-4018 (ISSN-L)
- OpenAlex
- W2051191064
- Cited by
- 115
- References
- 0
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 5 · 2023: 5 · 2022: 10 · 2021: 5 · 2020: 7 · 2019: 5 · 2018: 3 · 2017: 2 · 2016: 2 · 2015: 5 · 2014: 2 · 2013: 4 · 2012: 3
- FWCI
- 0.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Canadian Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Health Sciences › Medicine › Nephrology › Renal function and acid-base balance
- Keywords
- glutathione synthesis, glutamine, ammonia synthesis, gamma-glutamyl transferase, glycylglycine, glutathione degradation, kidney, gamma-glutamyl cycle, glutathione turnover
- MeSH terms
- Ammonia, Animals, Glutamine, Glutathione, Glycylglycine, Kidney, Male, Rats
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