The DOI matches its OpenAlex record; 29 of the 29 references it cites were found in a registry or an index.
Canalicular multispecific organic anion transporter/multidrug resistance protein 2 mediates low-affinity transport of reduced glutathione
Open accessAbstract
The canalicular multispecific organic anion transporter (cMOAT), a member of the ATP-binding cassette transporter family, mediates the transport of a broad range of non-bile salt organic anions from liver into bile. cMOAT-deficient Wistar rats (TR-) are mutated in the gene encoding cMOAT, leading to defective hepatobiliary transport of a whole range of substrates, including bilirubin glucuronide. These mutants also have impaired hepatobiliary excretion of GSH and, as a result, the bile flow in these animals is reduced. In the present work we demonstrate a role for cMOAT in the excretion of GSH both in vivo and in vitro. Biliary GSH excretion in rats heterozygous for the cMOAT mutation (TR/tr) was decreased to 63% of controls (TR/TR) (114+/-24 versus 181+/-20 nmol/min per kg body weight). Madin-Darby canine kidney (MDCK) II cells stably expressing the human cMOAT protein displayed >10-fold increase in apical GSH excretion compared with wild-type MDCKII cells (141+/-6.1 pmol/min per mg of protein versus 13.2+/-1.3 pmol/min per mg of protein in wild-type MDCKII cells). Similarly, MDCKII cells expressing the human multidrug resistance protein 1 showed a 4-fold increase in GSH excretion across the basolateral membrane. In several independent cMOAT-transfectants, the level of GSH excretion correlated with the expression level of the protein. Furthermore, we have shown, in cMOAT-transfected cells, that GSH is a low-affinity substrate for the transporter and that its excretion is reduced upon ATP depletion. In membrane vesicles isolated from cMOAT-expressing MDCKII cells, ATP-dependent S-(2,4-dinitrophenyl)glutathione uptake is competitively inhibited by high concentrations of GSH (Ki approximately 20 mM). We concluded that cMOAT mediates low-affinity transport of GSH. However, since hepatocellular GSH concentrations are high (5-10 mM), cMOAT might serve an important physiological function in maintenance of bile flow in addition to hepatic GSH turnover.
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Cites
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Self-citationCongenital Jaundice in Rats with a Mutation in a Multidrug Resistance-Associated Protein Gene
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Self-citationZaman, G. J., Lankelma, J., van Tellingen, O., Beijnen, J., Dekker, H., Paulusma, C., Oude Elferink, R. P., Baas, F., & Borst, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7690 · Cited by 498
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Reactions of arsenic(III) and arsenic(V) species with glutathione
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Cited by
Bile salt transporters: molecular characterization, function, and regulation
Trauner, M., & Boyer, J. L. (2003) · Physiological Reviews · doi:10.1152/physrev.00027.2002 · Cited by 999
Deeley, R. G., Westlake, C., & Cole, S. P. C. (2006) · Physiological Reviews · doi:10.1152/physrev.00035.2005 · Cited by 761
The multidrug resistance protein family
Borst, P., Evers, R., Kool, M., & Wijnholds, J. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(99)00167-4 · Cited by 648
Self-citationThe apical conjugate efflux pump ABCC2 (MRP2)
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Nies, A. T., Jedlitschky, G., König, J., Herold-Mende, C., Steiner, H. H., Schmitt, H.-P., & Keppler, D. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.07.051 · Cited by 379
Metadata
- Authors
- Paulusma, C. C., van Geer, M. A., Evers, R., Heijn, M., Ottenhoff, R., Borst, P., & Elferink, R. P. J. O.
- Venue
- Biochemical Journal
- Publisher
- Portland Press
- Published
- 1999-02-22
- Volume
- 338
- Issue
- 2
- Pages
- 393-393
- ISSN
- 0264-6021 (ISSN-L)
- OpenAlex
- W1968425502
- Cited by
- 252
- References
- 29
- FWCI
- 9.65
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Paulusma, C. C., van Geer, M. A., Evers, R., Heijn, M., Ottenhoff, R., Borst, P., & Elferink, R. P. J. O. (1999). Canalicular multispecific organic anion transporter/multidrug resistance protein 2 mediates low-affinity transport of reduced glutathione. Biochemical Journal. https://doi.org/10.1042/0264-6021%3A3380393
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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