Multidrug resistance-associated protein 5 is a protein that in humans is encoded by the ABCC5 gene.[1][2][3]
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 functions in the cellular export of its substrate, cyclic nucleotides. This export contributes to the degradation of phosphodiesterases and possibly an elimination pathway for cyclic nucleotides. Studies show that this protein provides resistance to thiopurine anticancer drugs, 6-mercatopurine and thioguanine, and the anti-HIV drug 9-(2-phosphonylmethoxyethyl)adenine. This protein may be involved in resistance to thiopurines in acute lymphoblastic leukemia and antiretroviral nucleoside analogs in HIV-infected patients. Alternative splicing of this gene has been detected; however, the complete sequence and translation initiation site is unclear.[3]
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Interactive pathway map [link]
Click on genes, proteins and metabolites below to link to respective articles. [4]
See also [link]
References [link]
- ^ Allikmets R, Gerrard B, Hutchinson A, Dean M (Feb 1997). "Characterization of the human ABC superfamily: isolation and mapping of 21 new genes using the expressed sequence tags database". Hum Mol Genet 5 (10): 1649–55. DOI:10.1093/hmg/5.10.1649. PMID 8894702.
- ^ Belinsky MG, Bain LJ, Balsara BB, Testa JR, Kruh GD (Dec 1998). "Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins". J Natl Cancer Inst 90 (22): 1735–41. DOI:10.1093/jnci/90.22.1735. PMID 9827529.
- ^ a b "Entrez Gene: ABCC5 ATP-binding cassette, sub-family C (CFTR/MRP), member 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10057.
- ^ The interactive pathway map can be edited at WikiPathways: "Fluoropyrimidine_Activity_WP1601". https://www.wikipathways.org/index.php/Pathway:WP1601.
Further reading [link]
- Kool M, de Haas M, Scheffer GL et al. (1997). "Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines". Cancer Res. 57 (16): 3537–47. PMID 9270026.
- Suzuki T, Nishio K, Sasaki H et al. (1997). "cDNA cloning of a short type of multidrug resistance protein homologue, SMRP, from a human lung cancer cell line". Biochem. Biophys. Res. Commun. 238 (3): 790–4. DOI:10.1006/bbrc.1997.7346. PMID 9325169.
- Cole SP (1999). "Re: Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins". J. Natl. Cancer Inst. 91 (10): 888–9. DOI:10.1093/jnci/91.10.888. PMID 10340910.
- McAleer MA, Breen MA, White NL, Matthews N (1999). "pABC11 (also known as MOAT-C and MRP5), a member of the ABC family of proteins, has anion transporter activity but does not confer multidrug resistance when overexpressed in human embryonic kidney 293 cells". J. Biol. Chem. 274 (33): 23541–8. DOI:10.1074/jbc.274.33.23541. PMID 10438534.
- Suzuki T, Sasaki H, Kuh HJ et al. (2000). "Detailed structural analysis on both human MRP5 and mouse mrp5 transcripts". Gene 242 (1–2): 167–73. DOI:10.1016/S0378-1119(99)00529-6. PMID 10721709.
- Oguri T, Isobe T, Suzuki T et al. (2000). "Increased expression of the MRP5 gene is associated with exposure to platinum drugs in lung cancer". Int. J. Cancer 86 (1): 95–100. DOI:10.1002/(SICI)1097-0215(20000401)86:1<95::AID-IJC15>3.0.CO;2-G. PMID 10728601.
- Dias Neto E, Correa RG, Verjovski-Almeida S et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. DOI:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16267.
- Wijnholds J, Mol CA, van Deemter L et al. (2000). "Multidrug-resistance protein 5 is a multispecific organic anion transporter able to transport nucleotide analogs". Proc. Natl. Acad. Sci. U.S.A. 97 (13): 7476–81. DOI:10.1073/pnas.120159197. PMC 16570. PMID 10840050. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16570.
- Jedlitschky G, Burchell B, Keppler D (2000). "The multidrug resistance protein 5 functions as an ATP-dependent export pump for cyclic nucleotides". J. Biol. Chem. 275 (39): 30069–74. DOI:10.1074/jbc.M005463200. PMID 10893247.
- Alcorn J, Lu X, Moscow JA, McNamara PJ (2002). "Transporter gene expression in lactating and nonlactating human mammary epithelial cells using real-time reverse transcription-polymerase chain reaction". J. Pharmacol. Exp. Ther. 303 (2): 487–96. DOI:10.1124/jpet.102.038315. PMID 12388627.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Wielinga PR, van der Heijden I, Reid G et al. (2003). "Characterization of the MRP4- and MRP5-mediated transport of cyclic nucleotides from intact cells". J. Biol. Chem. 278 (20): 17664–71. DOI:10.1074/jbc.M212723200. PMID 12637526.
- Pascolo L, Fernetti C, Pirulli D et al. (2003). "Effects of maturation on RNA transcription and protein expression of four MRP genes in human placenta and in BeWo cells". Biochem. Biophys. Res. Commun. 303 (1): 259–65. DOI:10.1016/S0006-291X(03)00327-9. PMID 12646196.
- Reid G, Wielinga P, Zelcer N et al. (2003). "Characterization of the transport of nucleoside analog drugs by the human multidrug resistance proteins MRP4 and MRP5". Mol. Pharmacol. 63 (5): 1094–103. DOI:10.1124/mol.63.5.1094. PMID 12695538.
- Dazert P, Meissner K, Vogelgesang S et al. (2003). "Expression and Localization of the Multidrug Resistance Protein 5 (MRP5/ABCC5), a Cellular Export Pump for Cyclic Nucleotides, in Human Heart". Am. J. Pathol. 163 (4): 1567–77. DOI:10.1016/S0002-9440(10)63513-4. PMC 1868287. PMID 14507663. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1868287.
- Brandenberger R, Wei H, Zhang S et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. DOI:10.1038/nbt971. PMID 15146197.
- Jedlitschky G, Tirschmann K, Lubenow LE et al. (2004). "The nucleotide transporter MRP4 (ABCC4) is highly expressed in human platelets and present in dense granules, indicating a role in mediator storage". Blood 104 (12): 3603–10. DOI:10.1182/blood-2003-12-4330. PMID 15297306.
- Meyer Zu Schwabedissen HE (2005). "Expression, Localization, and Function of MRP5 (ABCC5), a Transporter for Cyclic Nucleotides, in Human Placenta and Cultured Human Trophoblasts : Effects of Gestational Age and Cellular Differentiation". Am. J. Pathol. 166 (1): 39–48. DOI:10.1016/S0002-9440(10)62230-4. PMC 1602292. PMID 15631998. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1602292.
External links [link]
- ABCC5+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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Human Genome Organisation
The Human Genome Organisation (HUGO) is an organization involved in the Human Genome Project, a project about mapping the human genome. HUGO was established in 1989 as an international organization, primarily to foster collaboration between genome scientists around the world. The HUGO Gene Nomenclature Committee (HGNC), sometimes referred to as "HUGO", is one of HUGO's most active committees and aims to assign a unique gene name and symbol to each human gene.
History
HUGO was established in late April 1988 at the first meeting dedicated to genome mapping at Cold Spring Harbor. The idea of starting the organization stemmed from a South African biologist by the name of Sydney Brenner, who is known for his significant contributions to work on the genetic code and other areas of molecular biology, as well as winning the Nobel prize in Physiology of Medicine in 2002. A Founding Council was elected at the meeting that total 42 scientists from 17 different countries. HUGO is grounded in Geneva Switzerland, and later went on to elect an additional 178 members, bringing the total up to 220.
