ABCC2

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ATP-binding cassette, sub-family C (CFTR/MRP), member 2
Identifiers
Symbols ABCC2 ; ABC30; CMOAT; DJS; KIAA1010; MRP2; cMRP
External IDs Template:OMIM5 Template:MGI HomoloGene68052
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

ATP-binding cassette, sub-family C (CFTR/MRP), member 2, also known as ABCC2, is a human gene.[1]

The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MRP subfamily, which is involved in multi-drug resistance. This protein is expressed in the canalicular (apical) part of the hepatocyte and functions in biliary transport. Substrates include anticancer drugs such as vinblastine; therefore, this protein appears to contribute to drug resistance in mammalian cells. Several different mutations in this gene have been observed in patients with Dubin-Johnson syndrome (DJS), an autosomal recessive disorder characterized by conjugated hyperbilirubinemia.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: ABCC2 ATP-binding cassette, sub-family C (CFTR/MRP), member 2".

Further reading

  • Keppler D, König J (2001). "Hepatic secretion of conjugated drugs and endogenous substances". Semin. Liver Dis. 20 (3): 265–72. PMID 11076395.
  • Gerk PM, Vore M (2002). "Regulation of expression of the multidrug resistance-associated protein 2 (MRP2) and its role in drug disposition". J. Pharmacol. Exp. Ther. 302 (2): 407–15. doi:10.1124/jpet.102.035014. PMID 12130697.
  • Mayer R, Kartenbeck J, Büchler M; et al. (1995). "Expression of the MRP gene-encoded conjugate export pump in liver and its selective absence from the canalicular membrane in transport-deficient mutant hepatocytes". J. Cell Biol. 131 (1): 137–50. PMID 7559771.
  • Büchler M, König J, Brom M; et al. (1996). "cDNA cloning of the hepatocyte canalicular isoform of the multidrug resistance protein, cMrp, reveals a novel conjugate export pump deficient in hyperbilirubinemic mutant rats". J. Biol. Chem. 271 (25): 15091–8. PMID 8662992.
  • Taniguchi K, Wada M, Kohno K; et al. (1996). "A human canalicular multispecific organic anion transporter (cMOAT) gene is overexpressed in cisplatin-resistant human cancer cell lines with decreased drug accumulation". Cancer Res. 56 (18): 4124–9. PMID 8797578.
  • Paulusma CC, Kool M, Bosma PJ; et al. (1997). "A mutation in the human canalicular multispecific organic anion transporter gene causes the Dubin-Johnson syndrome". Hepatology. 25 (6): 1539–42. doi:10.1002/hep.510250635. PMID 9185779.
  • van Kuijck MA, Kool M, Merkx GF; et al. (1997). "Assignment of the canalicular multispecific organic anion transporter gene (CMOAT) to human chromosome 10q24 and mouse chromosome 19D2 by fluorescent in situ hybridization". Cytogenet. Cell Genet. 77 (3–4): 285–7. PMID 9284939.
  • Wada M, Toh S, Taniguchi K; et al. (1998). "Mutations in the canilicular multispecific organic anion transporter (cMOAT) gene, a novel ABC transporter, in patients with hyperbilirubinemia II/Dubin-Johnson syndrome". Hum. Mol. Genet. 7 (2): 203–7. PMID 9425227.
  • Evers R, Kool M, van Deemter L; et al. (1998). "Drug export activity of the human canalicular multispecific organic anion transporter in polarized kidney MDCK cells expressing cMOAT (MRP2) cDNA". J. Clin. Invest. 101 (7): 1310–9. PMID 9525973.
  • Kajihara S, Hisatomi A, Mizuta T; et al. (1999). "A splice mutation in the human canalicular multispecific organic anion transporter gene causes Dubin-Johnson syndrome". Biochem. Biophys. Res. Commun. 253 (2): 454–7. doi:10.1006/bbrc.1998.9780. PMID 9878557.
  • Toh S, Wada M, Uchiumi T; et al. (1999). "Genomic structure of the canalicular multispecific organic anion-transporter gene (MRP2/cMOAT) and mutations in the ATP-binding-cassette region in Dubin-Johnson syndrome". Am. J. Hum. Genet. 64 (3): 739–46. PMID 10053008.
  • Schaub TP, Kartenbeck J, König J; et al. (1999). "Expression of the MRP2 gene-encoded conjugate export pump in human kidney proximal tubules and in renal cell carcinoma". J. Am. Soc. Nephrol. 10 (6): 1159–69. PMID 10361853.
  • Tsujii H, König J, Rost D; et al. (1999). "Exon-intron organization of the human multidrug-resistance protein 2 (MRP2) gene mutated in Dubin-Johnson syndrome". Gastroenterology. 117 (3): 653–60. PMID 10464142.
  • Kocher O, Comella N, Gilchrist A; et al. (1999). "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". Lab. Invest. 79 (9): 1161–70. PMID 10496535.
  • Tanaka T, Uchiumi T, Hinoshita E; et al. (1999). "The human multidrug resistance protein 2 gene: functional characterization of the 5'-flanking region and expression in hepatic cells". Hepatology. 30 (6): 1507–12. doi:10.1002/hep.510300617. PMID 10573531.
  • St-Pierre MV, Serrano MA, Macias RI; et al. (2000). "Expression of members of the multidrug resistance protein family in human term placenta". Am. J. Physiol. Regul. Integr. Comp. Physiol. 279 (4): R1495–503. PMID 11004020.
  • Keitel V, Kartenbeck J, Nies AT; et al. (2001). "Impaired protein maturation of the conjugate export pump multidrug resistance protein 2 as a consequence of a deletion mutation in Dubin-Johnson syndrome". Hepatology. 32 (6): 1317–28. doi:10.1053/jhep.2000.19791. PMID 11093739.
  • Ito S, Ieiri I, Tanabe M; et al. (2001). "Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects". Pharmacogenetics. 11 (2): 175–84. PMID 11266082.
  • Mor-Cohen R, Zivelin A, Rosenberg N; et al. (2001). "Identification and functional analysis of two novel mutations in the multidrug resistance protein 2 gene in Israeli patients with Dubin-Johnson syndrome". J. Biol. Chem. 276 (40): 36923–30. doi:10.1074/jbc.M105047200. PMID 11477083.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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