The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

ABCC2  -  ATP-binding cassette, sub-family C...

Homo sapiens

Synonyms: ABC30, ATP-binding cassette sub-family C member 2, CMOAT, CMOAT1, CMRP, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ABCC2


High impact information on ABCC2

  • The structures show that MRP1/MRP2 is a heterotetramer and, despite little sequence homology, each MRP subunit exhibits the same "Whirly" transcription-factor fold [5].
  • These findings indicate that radixin is required for secretion of conjugated bilirubin through its support of Mrp2 localization at BCMs [6].
  • Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes [6].
  • The complementary DNA for rat cmoat, a homolog of the human multidrug resistance gene (hMRP1), was isolated and shown to be expressed in the canalicular membrane of hepatocytes [7].
  • MOAT-D is also highly related to cMOAT (about 47% identity) [8].

Chemical compound and disease context of ABCC2


Biological context of ABCC2


Anatomical context of ABCC2


Associations of ABCC2 with chemical compounds


Physical interactions of ABCC2


Regulatory relationships of ABCC2

  • Stable expression of MRP2 in transfected human embryonic kidney (HEK-293) and Madin-Darby canine kidney (MDCK) cells was enhanced by inhibitors of histone deacetylase [25].
  • When intestinal Bcrp1 was inhibited by FTC in Mrp2-deficient rats, total plasma concentrations of quercetin and its methylated metabolite isorhamnetin after 30 min of perfusion were more than twice that of controls (12.3 +/- 1.5 versus 5.6 +/- 1.3 muM; p < 0.01), whereas uptake of free quercetin from the intestinal lumen was not affected [26].
  • Upregulation of the expression of endogenous Mdr1 P-glycoprotein enhances lipid translocation in MDCK cells transfected with human MRP2 [27].
  • MRP4 is a novel PAH transporter that has higher affinity for PAH and is expressed more highly in kidney than MRP2, and may therefore be more important in renal PAH excretion [28].

Other interactions of ABCC2

  • To obtain deeper insight into the intestinal and hepatic processes, the disposition of ezetimibe was studied in the presence of rifampin (INN, rifampicin), a modulator of P-gp, MRP2, and hepatic organic anion (uptake) transporting polypeptides (OATPs) (SLCOs) [29].
  • Expression levels of BCRP, MRP1, or MRP2 were not related with the length of PFS [30].
  • Collectively, these results suggest that bosentan inhibits BSEP in humans with a similar potency to rats, and that increased bile salt-independent flow in rats by bosentan is at least partly attributable to the activation of Mrp2 [31].
  • In contrast to MRP, which is widely expressed in tissues, including liver, and cMOAT, the expression of which is largely restricted to liver, the MOAT-B transcript is widely expressed, with particularly high levels in prostate, but is barely detectable in liver [32].
  • Taken together, our results suggest that enhanced expression of MRP2 and lower expression of AQP3 are responsible for lower arsenic accumulation in arsenic-resistant R15 cells [33].

Analytical, diagnostic and therapeutic context of ABCC2


  1. A family of drug transporters: the multidrug resistance-associated proteins. Borst, P., Evers, R., Kool, M., Wijnholds, J. J. Natl. Cancer Inst. (2000) [Pubmed]
  2. Consequences of bile duct obstruction on intestinal expression and function of multidrug resistance-associated protein 2. Dietrich, C.G., Geier, A., Salein, N., Lammert, F., Roeb, E., Oude Elferink, R.P., Matern, S., Gartung, C. Gastroenterology (2004) [Pubmed]
  3. Expression of the MRP2 gene-encoded conjugate export pump in human kidney proximal tubules and in renal cell carcinoma. Schaub, T.P., Kartenbeck, J., König, J., Spring, H., Dörsam, J., Staehler, G., Störkel, S., Thon, W.F., Keppler, D. J. Am. Soc. Nephrol. (1999) [Pubmed]
  4. Hepatic secretion of conjugated drugs and endogenous substances. Keppler, D., König, J. Semin. Liver Dis. (2000) [Pubmed]
  5. Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal RNA matchmaking mechanism. Schumacher, M.A., Karamooz, E., Zíková, A., Trantírek, L., Lukes, J. Cell (2006) [Pubmed]
  6. Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. Kikuchi, S., Hata, M., Fukumoto, K., Yamane, Y., Matsui, T., Tamura, A., Yonemura, S., Yamagishi, H., Keppler, D., Tsukita, S., Tsukita, S. Nat. Genet. (2002) [Pubmed]
  7. Congenital jaundice in rats with a mutation in a multidrug resistance-associated protein gene. Paulusma, C.C., Bosma, P.J., Zaman, G.J., Bakker, C.T., Otter, M., Scheffer, G.L., Scheper, R.J., Borst, P., Oude Elferink, R.P. Science (1996) [Pubmed]
  8. Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins. Belinsky, M.G., Bain, L.J., Balsara, B.B., Testa, J.R., Kruh, G.D. J. Natl. Cancer Inst. (1998) [Pubmed]
  9. Increased expression of an ATP-binding cassette superfamily transporter, multidrug resistance protein 2, in human colorectal carcinomas. Hinoshita, E., Uchiumi, T., Taguchi, K., Kinukawa, N., Tsuneyoshi, M., Maehara, Y., Sugimachi, K., Kuwano, M. Clin. Cancer Res. (2000) [Pubmed]
  10. MRP2 (ABCC2) transports taxanes and confers paclitaxel resistance and both processes are stimulated by probenecid. Huisman, M.T., Chhatta, A.A., van Tellingen, O., Beijnen, J.H., Schinkel, A.H. Int. J. Cancer (2005) [Pubmed]
  11. The role of multidrug resistance proteins MRP1, MRP2 and MRP3 in cellular folate homeostasis. Hooijberg, J.H., Peters, G.J., Assaraf, Y.G., Kathmann, I., Priest, D.G., Bunni, M.A., Veerman, A.J., Scheffer, G.L., Kaspers, G.J., Jansen, G. Biochem. Pharmacol. (2003) [Pubmed]
  12. Identification of a Novel 974C-->G Nonsense Mutation of the MRP2/ABCC2 Gene in a Patient with Dubin-Johnson Syndrome and Analysis of the Effects of Rifampicin and Ursodeoxycholic Acid on Serum Bilirubin and Bile Acids. Corpechot, C., Ping, C., Wendum, D., Matsuda, F., Barbu, V., Poupon, R. Am. J. Gastroenterol. (2006) [Pubmed]
  13. Reconstitution of transport-active multidrug resistance protein 2 (MRP2; ABCC2) in proteoliposomes. Hagmann, W., Schubert, J., König, J., Keppler, D. Biol. Chem. (2002) [Pubmed]
  14. Influence of ABCB1, ABCC1, ABCC2, and ABCG2 haplotypes on the cellular exposure of nelfinavir in vivo. Colombo, S., Soranzo, N., Rotger, M., Sprenger, R., Bleiber, G., Furrer, H., Buclin, T., Goldstein, D., Décosterd, L., Telenti, A. Pharmacogenet. Genomics (2005) [Pubmed]
  15. Expression and localization of the multidrug resistance proteins MRP2 and MRP3 in human gallbladder epithelia. Rost, D., König, J., Weiss, G., Klar, E., Stremmel, W., Keppler, D. Gastroenterology (2001) [Pubmed]
  16. Multidrug resistance protein MRP2 contributes to blood-brain barrier function and restricts antiepileptic drug activity. Potschka, H., Fedrowitz, M., Löscher, W. J. Pharmacol. Exp. Ther. (2003) [Pubmed]
  17. Purification of the human apical conjugate export pump MRP2 reconstitution and functional characterization as substrate-stimulated ATPase. Hagmann, W., Nies, A.T., König, J., Frey, M., Zentgraf, H., Keppler, D. Eur. J. Biochem. (1999) [Pubmed]
  18. Influence of drug transporter polymorphisms on pravastatin pharmacokinetics in humans. Kivist??, K.T., Niemi, M. Pharm. Res. (2007) [Pubmed]
  19. Structural requirements for the apical sorting of human multidrug resistance protein 2 (ABCC2). Nies, A.T., König, J., Cui, Y., Brom, M., Spring, H., Keppler, D. Eur. J. Biochem. (2002) [Pubmed]
  20. Simvastatin does not influence the intestinal P-glycoprotein and MPR2, and the disposition of talinolol after chronic medication in healthy subjects genotyped for the ABCB1, ABCC2 and SLCO1B1 polymorphisms. Bernsdorf, A., Giessmann, T., Modess, C., Wegner, D., Igelbrink, S., Hecker, U., Haenisch, S., Cascorbi, I., Terhaag, B., Siegmund, W. British journal of clinical pharmacology. (2006) [Pubmed]
  21. Association of genetic polymorphism in ABCC2 with hepatic multidrug resistance-associated protein 2 expression and pravastatin pharmacokinetics. Niemi, M., Arnold, K.A., Backman, J.T., Pasanen, M.K., Gödtel-Armbrust, U., Wojnowski, L., Zanger, U.M., Neuvonen, P.J., Eichelbaum, M., Kivistö, K.T., Lang, T. Pharmacogenet. Genomics (2006) [Pubmed]
  22. Influence of genetic polymorphisms on intestinal expression and rifampicin-type induction of ABCC2 and on bioavailability of talinolol. Haenisch, S., May, K., Wegner, D., Caliebe, A., Cascorbi, I., Siegmund, W. Pharmacogenet. Genomics (2008) [Pubmed]
  23. Effect of multidrug resistance-reversing agents on transporting activity of human canalicular multispecific organic anion transporter. Chen, Z.S., Kawabe, T., Ono, M., Aoki, S., Sumizawa, T., Furukawa, T., Uchiumi, T., Wada, M., Kuwano, M., Akiyama, S.I. Mol. Pharmacol. (1999) [Pubmed]
  24. Inhibitory effect of the reversal agents V-104, GF120918 and Pluronic L61 on MDR1 Pgp-, MRP1- and MRP2-mediated transport. Evers, R., Kool, M., Smith, A.J., van Deemter, L., de Haas, M., Borst, P. Br. J. Cancer (2000) [Pubmed]
  25. Drug resistance and ATP-dependent conjugate transport mediated by the apical multidrug resistance protein, MRP2, permanently expressed in human and canine cells. Cui, Y., König, J., Buchholz, J.K., Spring, H., Leier, I., Keppler, D. Mol. Pharmacol. (1999) [Pubmed]
  26. Breast cancer resistance protein (Bcrp1/Abcg2) limits net intestinal uptake of quercetin in rats by facilitating apical efflux of glucuronides. Sesink, A.L., Arts, I.C., de Boer, V.C., Breedveld, P., Schellens, J.H., Hollman, P.C., Russel, F.G. Mol. Pharmacol. (2005) [Pubmed]
  27. Upregulation of the expression of endogenous Mdr1 P-glycoprotein enhances lipid translocation in MDCK cells transfected with human MRP2. Raggers, R.J., Vogels, I., van Meer, G. Histochem. Cell Biol. (2002) [Pubmed]
  28. Contribution of multidrug resistance protein 2 (MRP2/ABCC2) to the renal excretion of p-aminohippurate (PAH) and identification of MRP4 (ABCC4) as a novel PAH transporter. Smeets, P.H., van Aubel, R.A., Wouterse, A.C., van den Heuvel, J.J., Russel, F.G. J. Am. Soc. Nephrol. (2004) [Pubmed]
  29. Disposition and sterol-lowering effect of ezetimibe are influenced by single-dose coadministration of rifampin, an inhibitor of multidrug transport proteins. Oswald, S., Giessmann, T., Luetjohann, D., Wegner, D., Rosskopf, D., Weitschies, W., Siegmund, W. Clin. Pharmacol. Ther. (2006) [Pubmed]
  30. RNA expression of breast cancer resistance protein, lung resistance-related protein, multidrug resistance-associated proteins 1 and 2, and multidrug resistance gene 1 in breast cancer: correlation with chemotherapeutic response. Burger, H., Foekens, J.A., Look, M.P., Meijer-van Gelder, M.E., Klijn, J.G., Wiemer, E.A., Stoter, G., Nooter, K. Clin. Cancer Res. (2003) [Pubmed]
  31. Effects of bosentan, an endothelin receptor antagonist, on bile salt export pump and multidrug resistance-associated protein 2. Mano, Y., Usui, T., Kamimura, H. Biopharmaceutics & drug disposition (2007) [Pubmed]
  32. Isolation of MOAT-B, a widely expressed multidrug resistance-associated protein/canalicular multispecific organic anion transporter-related transporter. Lee, K., Belinsky, M.G., Bell, D.W., Testa, J.R., Kruh, G.D. Cancer Res. (1998) [Pubmed]
  33. Enhanced expression of multidrug resistance-associated protein 2 and reduced expression of aquaglyceroporin 3 in an arsenic-resistant human cell line. Lee, T.C., Ho, I.C., Lu, W.J., Huang, J.D. J. Biol. Chem. (2006) [Pubmed]
WikiGenes - Universities