Table of Contents Author Guidelines Submit a Manuscript
Evidence-Based Complementary and Alternative Medicine
Volume 2017 (2017), Article ID 1640187, 7 pages
https://doi.org/10.1155/2017/1640187
Research Article

Upregulation of PDZK1 by Calculus Bovis Sativus May Play an Important Role in Restoring Biliary Transport Function in Intrahepatic Cholestasis

1Department of Pharmacy, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China
2Department of Pharmacy, Puai Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China

Correspondence should be addressed to Cheng-Liang Zhang and Dong Liu

Received 12 August 2016; Revised 2 November 2016; Accepted 7 December 2016; Published 4 January 2017

Academic Editor: Yuewen Gong

Copyright © 2017 Dong Xiang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. Z. Chen, Y. Zhu, Y. Zhao et al., “Serum metabolomic profiling in a rat model reveals protective function of paeoniflorin against ANIT induced cholestasis,” Phytotherapy Research, vol. 30, no. 4, pp. 654–662, 2016. View at Publisher · View at Google Scholar · View at Scopus
  2. Q. Meng, X.-L. Chen, C.-Y. Wang et al., “Alisol B 23-acetate protects against ANIT-induced hepatotoxity and cholestasis, due to FXR-mediated regulation of transporters and enzymes involved in bile acid homeostasis,” Toxicology and Applied Pharmacology, vol. 283, no. 3, pp. 178–186, 2015. View at Publisher · View at Google Scholar · View at Scopus
  3. W. L. Van Der Woerd, S. W. C. Van Mil, J. M. Stapelbroek, L. W. J. Klomp, S. F. J. Van De Graaf, and R. H. J. Houwen, “Familial cholestasis: progressive familial intrahepatic cholestasis, benign recurrent intrahepatic cholestasis and intrahepatic cholestasis of pregnancy,” Best Practice and Research: Clinical Gastroenterology, vol. 24, no. 5, pp. 541–553, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. C. Clerici, D. Castellani, S. Asciutti et al., “3α-6α-Dihydroxy-7α-fluoro-5β-cholanoate (UPF-680), physicochemical and physiological properties of a new fluorinated bile acid that prevents 17α-ethynyl-estradiol-induced cholestasis in rats,” Toxicology and Applied Pharmacology, vol. 214, no. 2, pp. 199–208, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. A. Honda, T. Ikegami, M. Nakamuta et al., “Anticholestatic effects of bezafibrate in patients with primary biliary cirrhosis treated with ursodeoxycholic acid,” Hepatology, vol. 57, no. 5, pp. 1931–1941, 2013. View at Publisher · View at Google Scholar · View at Scopus
  6. K. Shimada, Y. Azuma, M. Kawase, T. Takahashi, S. W. Schaffer, and K. Takahashi, “Taurine as a marker for the identification of natural Calculus Bovis and its substitutes,” Advances in Experimental Medicine and Biology, vol. 776, pp. 141–149, 2013. View at Publisher · View at Google Scholar · View at Scopus
  7. S.-K. Yan, Y.-W. Wu, R.-H. Liu, and W.-D. Zhang, “Comparative study on major bioactive components in natural, artificial and in-vitro cultured Calculus Bovis,” Chemical and Pharmaceutical Bulletin, vol. 55, no. 1, pp. 128–132, 2007. View at Publisher · View at Google Scholar · View at Scopus
  8. C. Feng, X. Li, C. Zhang et al., “Development of a rapid and simple LC-MS/MS method for identification and quality control of natural Calculus bovis and Calculus bovis sativus,” Analytical Methods, vol. 7, no. 18, pp. 7606–7617, 2015. View at Publisher · View at Google Scholar · View at Scopus
  9. D. Liu, T. Wu, C.-L. Zhang et al., “Beneficial effect of calculus Bovis Sativus on 17α-ethynylestradiol-induced cholestasis in the rat,” Life Sciences, vol. 113, no. 1-2, pp. 22–30, 2014. View at Publisher · View at Google Scholar · View at Scopus
  10. Y. Kato, C. Watanabe, and A. Tsuji, “Regulation of drug transporters by PDZ adaptor proteins and nuclear receptors,” European Journal of Pharmaceutical Sciences, vol. 27, no. 5, pp. 487–500, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. Y. Emi, S. Nomura, H. Yokota, and M. Sakaguchi, “ATP-binding cassette transporter isoform C2 localizes to the apical plasma membrane via interactions with scaffolding protein,” Journal of Biochemistry, vol. 149, no. 2, pp. 177–189, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. T. Shimizu, T. Sugiura, T. Wakayama et al., “PDZK1 regulates breast cancer resistance protein in small intestine,” Drug Metabolism and Disposition, vol. 39, no. 11, pp. 2148–2154, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. O. Kocher, N. Comella, A. Gilchrist et al., “PDZK1, a novel PDZ domain-containing protein up-regulated in carcinomas and mapped to chromosome 1q21, interacts with cMOAT (MRP2), the multidrug resistance-associated protein,” Laboratory Investigation, vol. 79, no. 9, pp. 1161–1170, 1999. View at Google Scholar · View at Scopus
  14. T. Wu, X.-P. Li, Y.-J. Xu, G. Du, and D. Liu, “Ursodeoxycholic acid pretreatment reduces oral bioavailability of the multiple drug resistance-associated protein 2 substrate baicalin in rats,” Planta Medica, vol. 79, no. 17, pp. 1615–1619, 2013. View at Publisher · View at Google Scholar · View at Scopus
  15. G. An and M. E. Morris, “HPLC analysis of mitoxantrone in mouse plasma and tissues: Application in a Pharmacokinetic Study,” Journal of Pharmaceutical and Biomedical Analysis, vol. 51, no. 3, pp. 750–753, 2010. View at Publisher · View at Google Scholar · View at Scopus
  16. X. Yang and M. E. Morris, “Pharmacokinetics and biliary excretion of mitoxantrone in rats,” Journal of Pharmaceutical Sciences, vol. 99, no. 5, pp. 2502–2510, 2010. View at Publisher · View at Google Scholar · View at Scopus
  17. T. Akao, Y. Sakashita, M. Hanada, H. Goto, Y. Shimada, and K. Terasawa, “Enteric excretion of baicalein, a flavone of Scutellariae Radix, via glucuronidation in rat: involvement of multidrug resistance-associated protein 2,” Pharmaceutical Research, vol. 21, no. 11, pp. 2120–2126, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Noguchi, K. Katayama, J. Mitsuhashi, and Y. Sugimoto, “Functions of the breast cancer resistance protein (BCRP/ABCG2) in chemotherapy,” Advanced Drug Delivery Reviews, vol. 61, no. 1, pp. 26–33, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Clapéron, M. Mergey, and L. Fouassier, “Roles of the scaffolding proteins NHERF in liver biology,” Clinics and research in hepatology and gastroenterology, vol. 35, no. 3, pp. 176–181, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. H. Cai, Y. Guang, L. Liu, P. Yao, and F. Qiu, “The protective effects of in vitro cultivated calculus bovis on the cerebral and myocardial cells in hypoxic mice,” Journal of Huazhong University of Science and Technology—Medical Science, vol. 27, no. 6, pp. 635–638, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. K. Jemnitz, K. Heredi-Szabo, J. Janossy, E. Ioja, L. Vereczkey, and P. Krajcsi, “ABCC2/Abcc2: a multispecific transporter with dominant excretory functions,” Drug Metabolism Reviews, vol. 42, no. 3, pp. 402–436, 2010. View at Publisher · View at Google Scholar · View at Scopus
  22. Z. Ni, Z. Bikadi, M. F. Rosenberg, and Q. Mao, “Structure and function of the human breast cancer resistance protein (BCRP/ABCG2),” Current Drug Metabolism, vol. 11, no. 7, pp. 603–617, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. J. Y. L. Chiang, “Bile acid metabolism and signaling,” Comprehensive Physiology, vol. 3, no. 3, pp. 1191–1212, 2013. View at Publisher · View at Google Scholar · View at Scopus
  24. A. G. Blazquez, O. Briz, E. Gonzalez-Sanchez, M. J. Perez, C. I. Ghanem, and J. J. G. Marin, “The effect of acetaminophen on the expression of BCRP in trophoblast cells impairs the placental barrier to bile acids during maternal cholestasis,” Toxicology and Applied Pharmacology, vol. 277, no. 1, pp. 77–85, 2014. View at Publisher · View at Google Scholar · View at Scopus
  25. M. L. Ruiz, S. S. M. Villanueva, M. G. Luquita, S.-I. Ikushiro, A. D. Mottino, and V. A. Catania, “Beneficial effect of spironolactone administration on ethynylestradiol-induced cholestasis in the rat: involvement of up-regulation of multidrug resistance-associated protein 2,” Drug Metabolism and Disposition, vol. 35, no. 11, pp. 2060–2066, 2007. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Liu, H. Lu, Y.-F. Lu et al., “Potency of individual bile acids to regulate bile acid synthesis and transport genes in primary human hepatocyte cultures,” Toxicological Sciences, vol. 141, no. 2, pp. 538–546, 2014. View at Publisher · View at Google Scholar · View at Scopus
  27. F. Azzaroli, M. E. Raspanti, P. Simoni et al., “High doses of ursodeoxycholic acid up-regulate the expression of placental breast cancer resistance protein in patients affected by intrahepatic cholestasis of pregnancy,” PLoS ONE, vol. 8, no. 5, Article ID e64101, 2013. View at Publisher · View at Google Scholar · View at Scopus
  28. P. M. Gerk, W. Li, V. Megaraj, and M. Vore, “Human multidrug resistance protein 2 transports the therapeutic bile salt tauroursodeoxycholate,” Journal of Pharmacology and Experimental Therapeutics, vol. 320, no. 2, pp. 893–899, 2007. View at Publisher · View at Google Scholar · View at Scopus