Display options
Cite
Ismair MG, Stanca C, Ha HR, et al. Interactions of glycyrrhizin with organic anion transporting polypeptides of rat and human liver. Hepatol Res. 2003;26(4):343-347doi: 10.1016/s1386-6346(03)00154-2.
Ismair, M. G., Stanca, C., Ha, H. R., Renner, E. L., Meier, P. J., & Kullak-Ublick, G. A. (2003). Interactions of glycyrrhizin with organic anion transporting polypeptides of rat and human liver. Hepatology research : the official journal of the Japan Society of Hepatology, 26(4), 343-347. https://doi.org/10.1016/s1386-6346(03)00154-2
Ismair, Manfred G., et al. "Interactions of glycyrrhizin with organic anion transporting polypeptides of rat and human liver." Hepatology research : the official journal of the Japan Society of Hepatology vol. 26,4 (2003): 343-347. doi: https://doi.org/10.1016/s1386-6346(03)00154-2
Ismair MG, Stanca C, Ha HR, Renner EL, Meier PJ, Kullak-Ublick GA. Interactions of glycyrrhizin with organic anion transporting polypeptides of rat and human liver. Hepatol Res. 2003 Aug;26(4):343-347. doi: 10.1016/s1386-6346(03)00154-2. PMID: 12963436.
Copy Download .nbib Format: NLM
Share it on

Hepatol Res. 2003 Aug;26(4):343-347. doi: 10.1016/s1386-6346(03)00154-2.

Interactions of glycyrrhizin with organic anion transporting polypeptides of rat and human liver.

Hepatology research : the official journal of the Japan Society of Hepatology

Manfred G. Ismair, Carmen Stanca, Huy R. Ha, Eberhard L. Renner, Peter J. Meier, Gerd A. Kullak-Ublick

Affiliations

  1. Division of Clinical Pharmacology and Toxicology, Department of Internal Medicine, University Hospital, CH-8091, Zurich, Switzerland

PMID: 12963436 DOI: 10.1016/s1386-6346(03)00154-2

Abstract

Glycyrrhizin (GL) is used in Japan for the treatment of chronic hepatitis C. Following intravenous administration, GL is eliminated mainly by excretion into bile. Hepatocyte uptake of GL is a carrier-mediated process with characteristics resembling the organic anion transporting polypeptides (OATPs, solute carrier gene family SLC21A). We, therefore, studied whether GL is a potential transport substrate of the OATPs of rat and human liver. Because transport of GL could not be measured directly, GL-mediated cis-inhibition of [3H]estrone-3-sulfate or [35S]bromosulfophthalein uptake was analyzed kinetically in Xenopus laevis oocytes injected with cRNA coding for OATPs. GL inhibited [3H]estrone-3-sulfate uptake by 75-100% in oocytes expressing rat Oatp4, human OATP-C or human OATP8, members of the OATP1B subfamily that are expressed predominantly in hepatocytes. Dixon plots indicated a non-competitive type of inhibition, with Ki values of 6.1, 15.9 and 12.5 μmol/l, respectively. In contrast, GL inhibition of rat Oatp1, Oatp2 and Oatp3 and human OATP-A and OATP-B was only between 0 and 53%. In conclusion, GL is an inhibitor and, therefore, potentially a transport substrate of the liver-specific OATPs in rat and man. The rate at which GL is taken up into the liver may depend upon the function and expression levels of these hepatocellular OATPs.

Publication Types