Is the glutathione conjugate of trans-4-hydroxy-2-nonenal transported by the multispecific organic anion transporting-ATPase of human erythrocytes?
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Trans-4-hydroxy-2-nonenal (4-HNE), a cytotoxic end product of lipid peroxidation, is present in normal human blood plasma at concentrations of 0.1-1.0 microM. It can be, however, further metabolized within a cell, and one of the main products is 4-HNE glutathione conjugate (HNE-SG). In human erythrocyte membrane the system for active extrusion of glutathione (GSH) conjugates of various endo- and xenobiotics has been described; it exhibits either a low (Km at submillimolar concentration range) or a high (Km at low micromolar range) affinity for the transported substrates, such as for example S-(2,4-dinitrophenyl)glutathione (Dnp-SG). In the present study it has been shown that the high affinity transport system for Dnp-SG is competitively inhibited by HNE-SG with Ki of 0.2 microM, while 4-HNE inhibits non-competitively the activity of the transport system for Dnp-SG with Ki of 220microM. These observations point to the possibility that HNE-SG shares the same transport system with GSH conjugates of other endo- and xenobiotics in erythrocytes. This may be of importance for overall detoxification of the organism under oxidative stress.
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4-HNE can reach levels as high as 1 μM in normal human plasma; concentrations as high as 100 μM have been observed near the site of lipid peroxidation.
“4-HNE can reach levels as high as 1 µM in normal human plasma [72]; however, concentrations as high as 100 µM have been observed near the site of lipid peroxidation [57].”
From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [72]
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A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
Bligh, E. G., & Dyer, W. J. (1959) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o59-099 · Cited by 54,751 · see citing works
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Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease?
Hindle, A., Singh, S. P., Pradeepkiran, J. A., Bose, C., Vijayan, M., Kshirsagar, S., Sawant, N. A., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116098 · Cited by 14 · see citing works
- Authors
- Dygas, A., Makowski, P., & Pikuła, S.
- Affiliations
- Instytut Biologii Doświadczalnej im. Marcelego Nenckiego (PL)
- ORCID
- Pikuła, S
- Venue
- Acta Biochimica Polonica
- Publisher
- Frontiers Media SA
- Published
- 1998-03-31
- Volume
- 45
- Issue
- 1
- Pages
- 59-65
- ISSN
- 0001-527X (ISSN-L)
- 1734-154X
- OpenAlex
- W2092562525
- Cited by
- 5
- References
- 1
- Citations by year
- 2022: 1 · 2019: 1 · 2017: 1
- FWCI
- 0.15
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-sa
- Locations
- Acta Biochimica Polonica (publishedVersion, cc-by-sa)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- human erythrocytes, glutathione conjugate transport, lipid peroxidation, competitive inhibition, non-competitive inhibition, oxidative stress detoxification, erythrocyte membrane
- MeSH terms
- Adenosine Triphosphatases, Aldehydes, Catalysis, Erythrocytes, Glutathione, Humans, Substrate Specificity, Lipid Peroxidation, Ion Transport
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