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Volumn 115, Issue 8, 2010, Pages 1632-1639

Identification of multidrug resistance protein 1 (MRP1/ABCC1) as a molecular gate for cellular export of cobalamin

Author keywords

[No Author keywords available]

Indexed keywords

COBALAMIN; MULTIDRUG RESISTANCE PROTEIN 1; ADENOSINE TRIPHOSPHATE; CYANOCOBALAMIN; MULTIDRUG RESISTANCE PROTEIN; MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN 1;

EID: 77949904065     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2009-07-232587     Document Type: Article
Times cited : (114)

References (51)
  • 1
    • 33749685522 scopus 로고    scopus 로고
    • Vitamin B12, folic acid, and the nervous system
    • Reynolds E. Vitamin B12, folic acid, and the nervous system. Lancet Neurol. 2006;5(11):949-960.
    • (2006) Lancet Neurol. , vol.5 , Issue.11 , pp. 949-960
    • Reynolds, E.1
  • 2
    • 33750001533 scopus 로고    scopus 로고
    • Mitochondrial function and toxicity: Role of B vitamins on the one-carbon transfer pathways
    • DOI 10.1016/j.cbi.2006.05.010, PII S0009279706001335
    • Depeint F, Bruce WR, Shangari N, Mehta R, O'Brien PJ. Mitochondrial function and toxicity: role of B vitamins on the one-carbon transfer pathways. Chem Biol Interact. 2006;163(1-2):113-132. (Pubitemid 44572216)
    • (2006) Chemico-Biological Interactions , vol.163 , Issue.1-2 , pp. 113-132
    • Depeint, F.1    Bruce, W.R.2    Shangari, N.3    Mehta, R.4    O'Brien, P.J.5
  • 3
    • 0021778323 scopus 로고
    • Vitamin B12-folate interrelationships
    • Shane B, Stokstad EL. Vitamin B12-folate interrelationships. Annu Rev Nutr. 1985;5:115-141.
    • (1985) Annu Rev Nutr. , vol.5 , pp. 115-141
    • Shane, B.1    Stokstad, E.L.2
  • 6
    • 0020673438 scopus 로고
    • Intrinsic factor-mediated absorption of cobalamin by guinea pig ileal cells
    • Kapadia CR, Serfilippi D, Voloshin K, Donaldson RM Jr. Intrinsic factor-mediated absorption of cobalamin by guinea pig ileal cells. J Clin Invest. 1983;71(3):440-448.
    • (1983) J Clin Invest. , vol.71 , Issue.3 , pp. 440-448
    • Kapadia, C.R.1    Serfilippi, D.2    Voloshin, K.3    Donaldson Jr., R.M.4
  • 7
    • 59149091781 scopus 로고    scopus 로고
    • Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism
    • Rutsch F, Gailus S, Miousse IR, et al. Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism. Nat Genet. 2009;41(2):234-239.
    • (2009) Nat Genet. , vol.41 , Issue.2 , pp. 234-239
    • Rutsch, F.1    Gailus, S.2    Miousse, I.R.3
  • 8
    • 59449100953 scopus 로고    scopus 로고
    • The protein and the gene encoding the receptor for the cellular uptake of transcobalamin-bound cobalamin
    • Quadros EV, Nakayama Y, Sequeira JM. The protein and the gene encoding the receptor for the cellular uptake of transcobalamin-bound cobalamin. Blood. 2009;113(1):186-192.
    • (2009) Blood , vol.113 , Issue.1 , pp. 186-192
    • Quadros, E.V.1    Nakayama, Y.2    Sequeira, J.M.3
  • 10
    • 0017747530 scopus 로고
    • Cellular fluxes of vitamin B12
    • Ostray F, Gams RA. Cellular fluxes of vitamin B12. Blood. 1977;50(5):877-888.
    • (1977) Blood , vol.50 , Issue.5 , pp. 877-888
    • Ostray, F.1    Gams, R.A.2
  • 11
    • 0024378767 scopus 로고
    • Cobalamin release from intrinsic factor and transfer to transcobalamin II within the rat enterocyte
    • Ramasamy M, Alpers DH, Tiruppathi C, Seetharam B. Cobalamin release from intrinsic factor and transfer to transcobalamin II within the rat enterocyte. Am J Physiol. 1989;257(5):G791-G797.
    • (1989) Am J Physiol. , vol.257 , Issue.5
    • Ramasamy, M.1    Alpers, D.H.2    Tiruppathi, C.3    Seetharam, B.4
  • 12
    • 28944442871 scopus 로고    scopus 로고
    • 12 uptake
    • DOI 10.1021/bi0513103
    • Borths EL, Poolman B, Hvorup RN, Locher KP, Rees DC. In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake. Biochemistry. 2005;44(49):16301-16309. (Pubitemid 41785829)
    • (2005) Biochemistry , vol.44 , Issue.49 , pp. 16301-16309
    • Borths, E.L.1    Poolman, B.2    Hvorup, R.N.3    Locher, K.P.4    Rees, D.C.5
  • 13
    • 0021893059 scopus 로고
    • Transport of vitamin B12 in Escherichia coli: Cloning of the btuCD region
    • DeVeaux LC, Kadner RJ. Transport of vitamin B12 in Escherichia coli: cloning of the btuCD region. J Bacteriol. 1985;162(3):888-896.
    • (1985) J Bacteriol. , vol.162 , Issue.3 , pp. 888-896
    • DeVeaux, L.C.1    Kadner, R.J.2
  • 14
    • 0017760782 scopus 로고
    • Genetic analysis of components involved in vitamin B12 uptake in Escherichia coli
    • Bassford PJ Jr, Kadner RJ. Genetic analysis of components involved in vitamin B12 uptake in Escherichia coli. J Bacteriol. 1977;132(3):796-805.
    • (1977) J Bacteriol. , vol.132 , Issue.3 , pp. 796-805
    • Bassford Jr., P.J.1    Kadner, R.J.2
  • 15
    • 0015108326 scopus 로고
    • Synthesis of cobalamin coenzymes by human cells in tissue culture
    • Mahoney MJ, Rosenberg LE. Synthesis of cobalamin coenzymes by human cells in tissue culture. J Lab Clin Med. 1971;78(2):302-308.
    • (1971) J Lab Clin Med. , vol.78 , Issue.2 , pp. 302-308
    • Mahoney, M.J.1    Rosenberg, L.E.2
  • 16
    • 0029073103 scopus 로고
    • Immunofunctional properties of a yolk sac epithelial cell line expressing two proteins gp280 and gp330 of the intermicrovillar area of proximal tubule cells: Inhibition of endocytosis by the specific antibodies
    • Le Panse S, Galceran M, Pontillon F, et al. Immunofunctional properties of a yolk sac epithelial cell line expressing two proteins gp280 and gp330 of the intermicrovillar area of proximal tubule cells: inhibition of endocytosis by the specific antibodies. Eur J Cell Biol. 1995;67(2):120-129.
    • (1995) Eur J Cell Biol. , vol.67 , Issue.2 , pp. 120-129
    • Le Panse, S.1    Galceran, M.2    Pontillon, F.3
  • 17
    • 0034697037 scopus 로고    scopus 로고
    • Conformational changes of transcobalamin induced by aquocobalamin binding. Mechanism of substitution of the cobalt-coordinated group in the bound ligand
    • DOI 10.1074/jbc.275.16.11791
    • Fedosov SN, Fedosova NU, Nexo E, Petersen TE. Conformational changes of transcobalamin induced by aquocobalamin binding. Mechanism of substitution of the cobalt-coordinated group in the bound ligand. J Biol Chem. 2000;275(16):11791-11798. (Pubitemid 30237745)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11791-11798
    • Fedosov, S.N.1    Fedosova, N.U.2    Nexo, E.3    Petersen, T.E.4
  • 18
    • 0031449603 scopus 로고    scopus 로고
    • Transport of glutathione prostaglandin a conjugates by the multidrug resistance protein 1
    • DOI 10.1016/S0014-5793(97)01442-7, PII S0014579397014427
    • Evers R, Cnubben NH, Wijnholds J, et al. Transport of glutathione prostaglandin A conjugates by the multidrug resistance protein 1. FEBS Lett. 1997;419(1):112-116. (Pubitemid 28011228)
    • (1997) FEBS Letters , vol.419 , Issue.1 , pp. 112-116
    • Evers, R.1    Cnubben, N.H.P.2    Wijnholds, J.3    Van Deemter, L.4    Van Bladeren, P.J.5    Borst, P.6
  • 19
    • 0028000734 scopus 로고
    • Immunochemical detection of the multidrug resistance-associated protein MRP in human multidrug-resistant tumor cells by monoclonal antibodies
    • Flens MJ, Izquierdo MA, Scheffer GL, et al. Immunochemical detection of the multidrug resistance-associated protein MRP in human multidrug-resistant tumor cells by monoclonal antibodies. Cancer Res. 1994;54(17):4557-4563.
    • (1994) Cancer Res. , vol.54 , Issue.17 , pp. 4557-4563
    • Flens, M.J.1    Izquierdo, M.A.2    Scheffer, G.L.3
  • 20
    • 20344401776 scopus 로고    scopus 로고
    • Glycosylation independent measurement of the cobalamin binding protein haptocorrin
    • DOI 10.1016/j.cccn.2005.01.013, PII S000989810500063X
    • Morkbak AL, Pedersen JF, Nexo E. Glycosylation independent measurement of the cobalamin binding protein haptocorrin. Clin Chim Acta. 356(1-2):184-190, 2005. (Pubitemid 40779901)
    • (2005) Clinica Chimica Acta , vol.356 , Issue.1-2 , pp. 184-190
    • Morkbak, A.L.1    Pedersen, J.F.2    Nexo, E.3
  • 22
    • 33750695953 scopus 로고    scopus 로고
    • A simple, convenient method to synthesize cobalamins: Synthesis of homocysteinylcobalamin, Nacetylcysteinylcobalamin, 2-N-acetylamino-2- carbomethoxyethanethiolatocobalamin, sulfitocobalamin and nitrocobalamin
    • Suarez-Moreira E, Hannibal L, Smith CA, et al. A simple, convenient method to synthesize cobalamins: synthesis of homocysteinylcobalamin, Nacetylcysteinylcobalamin, 2-N-acetylamino-2- carbomethoxyethanethiolatocobalamin, sulfitocobalamin and nitrocobalamin. Dalton Trans. 2006;44:5269-5277.
    • (2006) Dalton Trans. , vol.44 , pp. 5269-5277
    • Suarez-Moreira, E.1    Hannibal, L.2    Smith, C.A.3
  • 24
    • 27444444053 scopus 로고    scopus 로고
    • Automated assay for the determination of methylmalonic acid, total homocysteine, and related amino acids in human serum or plasma by means of methylchloroformate derivatization and gas chromatography-mass spectrometry
    • DOI 10.1373/clinchem.2005.053835
    • Windelberg A, Arseth O, Kvalheim G, Ueland PM. Automated assay for the determination of methylmalonic acid, total homocysteine, and related amino acids in human serum or plasma by means of methylchloroformate derivatization and gas chromatography-mass spectrometry. Clin Chem. 2005;51(11):2103-2109. (Pubitemid 41532626)
    • (2005) Clinical Chemistry , vol.51 , Issue.11 , pp. 2103-2109
    • Windelberg, A.1    Arseth, O.2    Kvalheim, G.3    Ueland, P.M.4
  • 25
    • 0037155814 scopus 로고    scopus 로고
    • Comparative analysis of cobalamin binding kinetics and ligand protection for intrinsic factor, transcobalamin, and haptocorrin
    • Fedosov SN, Berglund L, Fedosova NU, Nexo E, Petersen TE. Comparative analysis of cobalamin binding kinetics and ligand protection for intrinsic factor, transcobalamin, and haptocorrin. J Biol Chem. 2002;277(12):9989-9996.
    • (2002) J Biol Chem. , vol.277 , Issue.12 , pp. 9989-9996
    • Fedosov, S.N.1    Berglund, L.2    Fedosova, N.U.3    Nexo, E.4    Petersen, T.E.5
  • 26
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson AL, Chen J. ATP-binding cassette transporters in bacteria. Annu Rev Biochem. 2004;73:241-268.
    • (2004) Annu Rev Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 27
    • 34249740700 scopus 로고    scopus 로고
    • The role of transporters in cellular heme and porphyrin homeostasis
    • DOI 10.1016/j.pharmthera.2007.02.001, PII S016372580700023X
    • Krishnamurthy P, Xie T, Schuetz JD. The role of transporters in cellular heme and porphyrin homeostasis. Pharmacol Ther. 2007;114(3):345-358. (Pubitemid 46843250)
    • (2007) Pharmacology and Therapeutics , vol.114 , Issue.3 , pp. 345-358
    • Krishnamurthy, P.1    Xie, T.2    Schuetz, J.D.3
  • 28
    • 33846703691 scopus 로고    scopus 로고
    • Portrait of multifaceted transporter, the multidrug resistance-associated protein 1 (MRP1/ABCC1)
    • DOI 10.1007/s00424-006-0160-8, 20 years of ABC transporters
    • Bakos E, Homolya L. Portrait of multifaceted transporter, the multidrug resistance-associated protein 1 (MRP1/ABCC1). Pflugers Arch. 2007;453(5):621-641. (Pubitemid 46192535)
    • (2007) Pflugers Archiv European Journal of Physiology , vol.453 , Issue.5 , pp. 621-641
    • Bakos, E.1    Homolya, L.2
  • 29
    • 33846681607 scopus 로고    scopus 로고
    • Multidrug resistance-associated proteins 3, 4, and 5
    • Borst P, de Wolf C, van de Wetering K. Multidrug resistance-associated proteins 3, 4, and 5. Pflugers Arch. 2007;453(5):661-673.
    • (2007) Pflugers Arch. , vol.453 , Issue.5 , pp. 661-673
    • Borst, P.1    De Wolf, C.2    Van De Wetering, K.3
  • 30
    • 33745835398 scopus 로고    scopus 로고
    • Transmembrane transport of endo- And xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins
    • DOI 10.1152/physrev.00035.2005
    • Deeley RG, Westlake C, Cole SP. Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. Physiol Rev. 2006;86(3):849-899. (Pubitemid 44033384)
    • (2006) Physiological Reviews , vol.86 , Issue.3 , pp. 849-899
    • Deeley, R.G.1    Westlake, C.2    Cole, S.P.C.3
  • 31
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst P, Elferink RO. Mammalian ABC transporters in health and disease. Annu Rev Biochem. 2002;71:537-592.
    • (2002) Annu Rev Biochem. , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 32
    • 0345724724 scopus 로고    scopus 로고
    • The MRP family of drug efflux pumps
    • Kruh GD, Belinsky MG. The MRP family of drug efflux pumps. Oncogene. 2003;22(47):7537-7552.
    • (2003) Oncogene. , vol.22 , Issue.47 , pp. 7537-7552
    • Kruh, G.D.1    Belinsky, M.G.2
  • 33
    • 0030665969 scopus 로고    scopus 로고
    • Disruption of the murine MRP (multidrug resistance protein) gene leads to increased sensitivity to etoposide (VP-16) and increased levels of glutathione
    • Lorico A, Rappa G, Finch RA, et al. Disruption of the murine MRP (multidrug resistance protein) gene leads to increased sensitivity to etoposide (VP-16) and increased levels of glutathione. Cancer Res. 1997;57(23):5238-5242. (Pubitemid 27516355)
    • (1997) Cancer Research , vol.57 , Issue.23 , pp. 5238-5242
    • Lorico, A.1    Rappa, G.2    Finch, R.A.3    Yang, D.4    Flavell, R.A.5    Sartorelli, A.C.6
  • 34
    • 0035866385 scopus 로고    scopus 로고
    • The pharmacological phenotype of combined multidrug-resistance mdr1a/1b- And mrp1-deficient mice
    • Johnson DR, Finch RA, Lin ZP, Zeiss CJ, Sartorelli AC. The pharmacological phenotype of combined multidrug-resistance mdr1a/1b- and mrp1-deficient mice. Cancer Res. 2001;61(4):1469-1476.
    • (2001) Cancer Res. , vol.61 , Issue.4 , pp. 1469-1476
    • Johnson, D.R.1    Finch, R.A.2    Lin, Z.P.3    Zeiss, C.J.4    Sartorelli, A.C.5
  • 35
    • 55749101940 scopus 로고    scopus 로고
    • Decyanation of vitamin B12 by a trafficking chaperone
    • Kim J, Gherasim C, Banerjee R. Decyanation of vitamin B12 by a trafficking chaperone. Proc Natl Acad Sci U S A. 2008;105(38):14551-14554.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.38 , pp. 14551-14554
    • Kim, J.1    Gherasim, C.2    Banerjee, R.3
  • 36
    • 67649658036 scopus 로고    scopus 로고
    • Processing of alkylcobalamins in mammalian cells: A role for the MMACHC (cblC) gene product
    • Hannibal L, Kim J, Brasch NE, et al. Processing of alkylcobalamins in mammalian cells: a role for the MMACHC (cblC) gene product. Mol Genet Metab. 2009;97(4):260-266.
    • (2009) Mol Genet Metab. , vol.97 , Issue.4 , pp. 260-266
    • Hannibal, L.1    Kim, J.2    Brasch, N.E.3
  • 37
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • DOI 10.1074/jbc.M000713200
    • Abboud S, Haile DJ. A novel mammalian ironregulated iron-regulated protein involved in intracellular iron metabolism. J Biol Chem. 2000;275(26):19906-19912. (Pubitemid 30441595)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.26 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 38
    • 0038007980 scopus 로고    scopus 로고
    • 12 homeostasis
    • DOI 10.1093/ndt/gfg089
    • Birn H, Nexo E, Christensen EI, Nielsen R. Diversity in rat tissue accumulation of vitamin B12 supports a distinct role for the kidney in vitamin B12 homeostasis. Nephrol Dial Transplant. 2003;18(6):1095-1100. (Pubitemid 36722509)
    • (2003) Nephrology Dialysis Transplantation , vol.18 , Issue.6 , pp. 1095-1100
    • Birn, H.1    Nexo, E.2    Christensen, E.I.3    Nielsen, R.4
  • 39
    • 0021178552 scopus 로고
    • The regulatory roles of liver and kidney in cobalamin (vitamin B12) metabolism in the rat: The uptake and intracellular binding of cobalamin and the activity of the cobalamin-dependent enzymes in response to varying cobalamin supply
    • Scott JS, Treston AM, Bowman EP, Owens JA, Cooksley WG. The regulatory roles of liver and kidney in cobalamin (vitamin B12) metabolism in the rat: the uptake and intracellular binding of cobalamin and the activity of the cobalamin-dependent enzymes in response to varying cobalamin supply. Clin Sci (Lond). 1984;67(3):299-306.
    • (1984) Clin Sci (Lond) , vol.67 , Issue.3 , pp. 299-306
    • Scott, J.S.1    Treston, A.M.2    Bowman, E.P.3    Owens, J.A.4    Cooksley, W.G.5
  • 42
    • 8344273321 scopus 로고    scopus 로고
    • Cobalamin transport proteins and their cell-surface receptors
    • Seetharam B, Yammani RR. Cobalamin transport proteins and their cell-surface receptors. Expert Rev Mol Med. 2003;5(18):1-18.
    • (2003) Expert Rev Mol Med. , vol.5 , Issue.18 , pp. 1-18
    • Seetharam, B.1    Yammani, R.R.2
  • 44
    • 0025290614 scopus 로고
    • Glutathionyl-cobalamin as an intermediate in the formation of cobalamin coenzymes
    • Pezacka E, Green R, Jacobsen DW. Glutathionyl-cobalamin as an intermediate in the formation of cobalamin coenzymes. Biochem Biophys Res Commun. 1990;169(2):443-450.
    • (1990) Biochem Biophys Res Commun. , vol.169 , Issue.2 , pp. 443-450
    • Pezacka, E.1    Green, R.2    Jacobsen, D.W.3
  • 45
    • 57449097784 scopus 로고    scopus 로고
    • Accurate assessment and identification of naturally occurring cellular cobalamins
    • Hannibal L, Axhemi A, Glushchenko AV, et al. Accurate assessment and identification of naturally occurring cellular cobalamins. Clin Chem Lab Med. 2008;46(12):1739-1746.
    • (2008) Clin Chem Lab Med. , vol.46 , Issue.12 , pp. 1739-1746
    • Hannibal, L.1    Axhemi, A.2    Glushchenko, A.V.3
  • 46
    • 31844455959 scopus 로고    scopus 로고
    • Substrate recognition and transport by multidrug resistance protein 1 (ABCC1)
    • DOI 10.1016/j.febslet.2005.12.036, PII S001457930501505X, ABC Transporters
    • Deeley RG, Cole SP. Substrate recognition and transport by multidrug resistance protein 1 (ABCC1). FEBS Lett. 2006;580(4):1103-1111. (Pubitemid 43185290)
    • (2006) FEBS Letters , vol.580 , Issue.4 , pp. 1103-1111
    • Deeley, R.G.1    Cole, S.P.C.2
  • 48
    • 0030678131 scopus 로고    scopus 로고
    • Evidence that the multidrug resistance protein (MRP) functions as a co- Transporter of glutathione and natural product toxins
    • Rappa G, Lorico A, Flavell RA, Sartorelli AC. Evidence that the multidrug resistance protein (MRP) functions as a co-transporter of glutathione and natural product toxins. Cancer Res. 1997;57(23):5232-5237. (Pubitemid 27516354)
    • (1997) Cancer Research , vol.57 , Issue.23 , pp. 5232-5237
    • Rappa, G.1    Lorico, A.2    Flavell, R.A.3    Sartorelli, A.C.4
  • 49
    • 0033616684 scopus 로고    scopus 로고
    • Choroid plexus epithelial expression of MDR1 P glycoprotein and multidrug resistance-associated protein contribute to the blood-cerebrospinal-fluid drug-permeability barrier
    • Rao VV, Dahlheimer JL, Bardgett ME, et al. Choroid plexus epithelial expression of MDR1 P glycoprotein and multidrug resistance-associated protein contribute to the blood-cerebrospinal-fluid drug-permeability barrier. Proc Natl Acad Sci U S A. 1999;96(7):3900-3905.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.7 , pp. 3900-3905
    • Rao, V.V.1    Dahlheimer, J.L.2    Bardgett, M.E.3


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