메뉴 건너뛰기




Volumn 24, Issue 7, 2007, Pages 1227-1251

Polyspecific organic cation transporters: Structure, function, physiological roles, and biopharmaceutical implications

Author keywords

Drug transporters; MATE1; OCT1; OCT2; OCT3; OCT6; OCTN1; OCTN2; Organic cation transport; Polyspecific transporters

Indexed keywords

ACEBUTOLOL; AMANTADINE; ATROPINE; BECLOMETASONE; BUDESONIDE; CEFEPIME; CEFOSELIS; CEFSULODIN; CIMETIDINE; CITALOPRAM; CLONIDINE; DIPHENHYDRAMINE; DISOPYRAMIDE; FAMOTIDINE; KETAMINE; LEVOFLOXACIN; LIDOCAINE; MEMANTINE; MEPYRAMINE; MIDAZOLAM; OFLOXACIN; ORGANIC CATION TRANSPORTER; PHENCYCLIDINE; PIPERPHENAMINE; PRAZOSIN; PROCAINAMIDE; QUINIDINE; RANITIDINE; UNINDEXED DRUG; VERAPAMIL;

EID: 34249943356     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-007-9254-z     Document Type: Review
Times cited : (875)

References (234)
  • 1
    • 0037457802 scopus 로고    scopus 로고
    • Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: An overview
    • A. H. Schinkel and J. W. Jonker. Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: an overview. Adv. Drug Deliv. Rev. 55:3-29 (2003).
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 3-29
    • Schinkel, A.H.1    Jonker, J.W.2
  • 2
    • 1242272750 scopus 로고    scopus 로고
    • The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
    • H. Daniel and G. Kottra. The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology. Pflugers Arch. 447:610-618 (2004).
    • (2004) Pflugers Arch. , vol.447 , pp. 610-618
    • Daniel, H.1    Kottra, G.2
  • 3
    • 1242272736 scopus 로고    scopus 로고
    • Organic anion transporting polypeptides of the OATP/ SLC21 family: Phylogenetic classification as OATP/ SLCO superfamily, new nomenclature and molecular/functional properties
    • B. Hagenbuch and P. J. Meier. Organic anion transporting polypeptides of the OATP/ SLC21 family: phylogenetic classification as OATP/ SLCO superfamily, new nomenclature and molecular/functional properties. Pflugers Arch. 447:653-665 (2004).
    • (2004) Pflugers Arch. , vol.447 , pp. 653-665
    • Hagenbuch, B.1    Meier, P.J.2
  • 5
    • 1242295185 scopus 로고    scopus 로고
    • The SLC22 drug transporter family
    • H. Koepsell and H. Endou. The SLC22 drug transporter family. Pflugers Arch. 447:666-676 (2004).
    • (2004) Pflugers Arch. , vol.447 , pp. 666-676
    • Koepsell, H.1    Endou, H.2
  • 7
    • 29144523534 scopus 로고    scopus 로고
    • A human transporter protein that mediates the final excretion step for toxic organic cations
    • M. Otsuka, T. Matsumoto, R. Morimoto, S. Arioka, H. Omote, and Y. Moriyama. A human transporter protein that mediates the final excretion step for toxic organic cations. Proc. Natl. Acad. Sci. U.S.A. 102:17923-17928 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17923-17928
    • Otsuka, M.1    Matsumoto, T.2    Morimoto, R.3    Arioka, S.4    Omote, H.5    Moriyama, Y.6
  • 8
    • 0031893146 scopus 로고    scopus 로고
    • Organic cation transporters in intestine, kidney, liver, and brain
    • H. Koepsell. Organic cation transporters in intestine, kidney, liver, and brain. Annu. Rev. Physiol. 60:243-266 (1998).
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 243-266
    • Koepsell, H.1
  • 9
    • 3042569768 scopus 로고    scopus 로고
    • Polyspecific organic cation transporters: Their functions and interactions with drugs
    • H. Koepsell. Polyspecific organic cation transporters: their functions and interactions with drugs. TIPS 25:375-381 (2004).
    • (2004) TIPS , vol.25 , pp. 375-381
    • Koepsell, H.1
  • 10
    • 3042542425 scopus 로고    scopus 로고
    • Molecular and cellular physiology of renal organic cation and anion transport
    • S. H. Wright and W. H. Dantzler. Molecular and cellular physiology of renal organic cation and anion transport. Physiol. Rev. 84:987-1049 (2004).
    • (2004) Physiol. Rev. , vol.84 , pp. 987-1049
    • Wright, S.H.1    Dantzler, W.H.2
  • 11
    • 0035066252 scopus 로고    scopus 로고
    • Transporters involved in the elimination of drugs in the kidney: Organic anion transporters and organic cation transporters
    • M. J. Dresser, M. K. Leabman, and K. M. Giacomini. Transporters involved in the elimination of drugs in the kidney: organic anion transporters and organic cation transporters. J. Pharm. Sci. 90:397-421 (2001).
    • (2001) J. Pharm. Sci. , vol.90 , pp. 397-421
    • Dresser, M.J.1    Leabman, M.K.2    Giacomini, K.M.3
  • 13
    • 0028063302 scopus 로고
    • Drug excretion mediated by a new prototype of polyspecific transporter
    • D. Gründemann, V. Gorboulev, S. Gambaryan, M. Veyhl, and H. Koepsell. Drug excretion mediated by a new prototype of polyspecific transporter. Nature 372:549-552 (1994).
    • (1994) Nature , vol.372 , pp. 549-552
    • Gründemann, D.1    Gorboulev, V.2    Gambaryan, S.3    Veyhl, M.4    Koepsell, H.5
  • 17
    • 0032900120 scopus 로고    scopus 로고
    • Cloning and functional expression of a mouse liver organic cation transporter
    • R. M. Green, K. Lo, C. Sterritt, and D. R. Beier. Cloning and functional expression of a mouse liver organic cation transporter. Hepatology 29:1556-1562 (1999).
    • (1999) Hepatology , vol.29 , pp. 1556-1562
    • Green, R.M.1    Lo, K.2    Sterritt, C.3    Beier, D.R.4
  • 18
    • 0030590117 scopus 로고    scopus 로고
    • CDNA cloning and functional expression of a novel rat kidney organic cation transporter, OCT2
    • M. Okuda, H. Saito, Y. Urakami, M. Takano, and K. Inui. cDNA cloning and functional expression of a novel rat kidney organic cation transporter, OCT2. Biochem. Biophys. Res. Commun. 224:500-507 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 500-507
    • Okuda, M.1    Saito, H.2    Urakami, Y.3    Takano, M.4    Inui, K.5
  • 19
    • 0032807543 scopus 로고    scopus 로고
    • Cloning of the mouse organic cation transporter 2 gene, Slc22a2, from an enhancer-trap transgene integration locus
    • K. A. Mooslehner and N. D. Allen. Cloning of the mouse organic cation transporter 2 gene, Slc22a2, from an enhancer-trap transgene integration locus. Mamm. Genome 10:218-224 (1999).
    • (1999) Mamm. Genome , vol.10 , pp. 218-224
    • Mooslehner, K.A.1    Allen, N.D.2
  • 21
    • 0032150876 scopus 로고    scopus 로고
    • Molecular identification of the corticosterone-sensitive extraneuronal catecholamine transporter
    • D. Gründemann, B. Schechinger, G. A. Rappold, and E. Schömig. Molecular identification of the corticosterone-sensitive extraneuronal catecholamine transporter. Nat. Neurosci. 1:349-351 (1998).
    • (1998) Nat. Neurosci. , vol.1 , pp. 349-351
    • Gründemann, D.1    Schechinger, B.2    Rappold, G.A.3    Schömig, E.4
  • 22
    • 0032569029 scopus 로고    scopus 로고
    • Cloning and functional characterization of a potential-sensitive, polyspecific organic cation transporter (OCT3) most abundantly expressed in placenta
    • R. Kekuda, P. D. Prasad, X. Wu, H. Wang, Y.-J. Fei, F. H. Leibach, and V. Ganapathy. Cloning and functional characterization of a potential-sensitive, polyspecific organic cation transporter (OCT3) most abundantly expressed in placenta. J. Biol. Chem. 273:15971-15979 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15971-15979
    • Kekuda, R.1    Prasad, P.D.2    Wu, X.3    Wang, H.4    Fei, Y.-J.5    Leibach, F.H.6    Ganapathy, V.7
  • 24
    • 0030985189 scopus 로고    scopus 로고
    • Cloning and functional characterization of a rat renal organic cation transporter isoform (rOCT1A)
    • L. Zhang, M. J. Dresser, J. K. Chun, P. C. Babbitt, and K. M. Giacomini. Cloning and functional characterization of a rat renal organic cation transporter isoform (rOCT1A). J. Biol. Chem. 272:16548-16554 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 16548-16554
    • Zhang, L.1    Dresser, M.J.2    Chun, J.K.3    Babbitt, P.C.4    Giacomini, K.M.5
  • 25
    • 0036294807 scopus 로고    scopus 로고
    • CDNA cloning, functional characterization, and tissue distribution of an alternatively spliced variant of organic cation transporter hOCT2 predominantly expressed in the human kidney
    • Y. Urakami, M. Akazawa, H. Saito, M. Okuda, and K.-I. Inui. cDNA cloning, functional characterization, and tissue distribution of an alternatively spliced variant of organic cation transporter hOCT2 predominantly expressed in the human kidney. J. Am. Soc. Nephrol. 13:1703-1710 (2002).
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 1703-1710
    • Urakami, Y.1    Akazawa, M.2    Saito, H.3    Okuda, M.4    Inui, K.-I.5
  • 26
    • 0031410948 scopus 로고    scopus 로고
    • The two human organic cation transporter genes SLC22A1 and SLC22A2 are located on chromosome 6q26
    • M. R. Koehler, B. Wissinger, V. Gorboulev, H. Koepsell, and M. Schmid. The two human organic cation transporter genes SLC22A1 and SLC22A2 are located on chromosome 6q26. Cytogenet. Cell Genet. 79:198-200 (1997).
    • (1997) Cytogenet. Cell Genet. , vol.79 , pp. 198-200
    • Koehler, M.R.1    Wissinger, B.2    Gorboulev, V.3    Koepsell, H.4    Schmid, M.5
  • 27
    • 18844465361 scopus 로고    scopus 로고
    • Gene structures of the human non-neuronal monoamine transporters EMT and OCT2
    • D. Gründemann and E. Schömig. Gene structures of the human non-neuronal monoamine transporters EMT and OCT2. Hum. Genet. 106:627-635 (2000).
    • (2000) Hum. Genet. , vol.106 , pp. 627-635
    • Gründemann, D.1    Schömig, E.2
  • 28
    • 0342699762 scopus 로고    scopus 로고
    • Molecular cloning, functional characterization and genomic organization of four alternatively spliced isoforms of the human organic cation transporter 1 (hOCT1/SLC22A1)
    • M. Hayer, H. Bönisch, and M. Bruss. Molecular cloning, functional characterization and genomic organization of four alternatively spliced isoforms of the human organic cation transporter 1 (hOCT1/SLC22A1). Ann. Hum. Genet. 63:473-482 (1999).
    • (1999) Ann. Hum. Genet. , vol.63 , pp. 473-482
    • Hayer, M.1    Bönisch, H.2    Brüss, M.3
  • 29
    • 0033555592 scopus 로고    scopus 로고
    • Cloning of the mouse and human solute carrier 22a3 (Slc22a3/SLC22A3) identifies a conserved cluster of three organic cation transporters on mouse chromosome 17 and human 6q26-q27
    • S. Verhaagh, N. Schweifer, D. P. Barlow, and R. Zwart. Cloning of the mouse and human solute carrier 22a3 (Slc22a3/SLC22A3) identifies a conserved cluster of three organic cation transporters on mouse chromosome 17 and human 6q26-q27. Genomics 55:209-218 (1999).
    • (1999) Genomics , vol.55 , pp. 209-218
    • Verhaagh, S.1    Schweifer, N.2    Barlow, D.P.3    Zwart, R.4
  • 30
    • 0034212998 scopus 로고    scopus 로고
    • Structural and functional characteristics and tissue distribution pattern of rat OCTN1, an organic cation transporter, cloned from placenta
    • X. Wu, R. L. George, W. Huang, H. Wang, S. J. Conway, F. H. Leibach, and V. Ganapathy. Structural and functional characteristics and tissue distribution pattern of rat OCTN1, an organic cation transporter, cloned from placenta. Biochim. Biophys. Acta 1466:315-327 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1466 , pp. 315-327
    • Wu, X.1    George, R.L.2    Huang, W.3    Wang, H.4    Conway, S.J.5    Leibach, F.H.6    Ganapathy, V.7
  • 31
    • 0031434178 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human pH-dependent organic cation transporter, OCTN1
    • I. Tamai, H. Yabuuchi, J. Nezu, Y. Sai, A. Oku, M. Shimane, and A. Tsuji. Cloning and characterization of a novel human pH-dependent organic cation transporter, OCTN1. FEBS Lett. 419:107-111 (1997).
    • (1997) FEBS Lett. , vol.419 , pp. 107-111
    • Tamai, I.1    Yabuuchi, H.2    Nezu, J.3    Sai, Y.4    Oku, A.5    Shimane, M.6    Tsuji, A.7
  • 32
    • 0034704135 scopus 로고    scopus 로고
    • Molecular and functional characterization of organic cation/carnitine transporter family in mice
    • I. Tamai, R. Ohashi, J. Nezu, Y. Sai, D. Kobayashi, A. Oku, M. Shimane, and A. Tsuji. Molecular and functional characterization of organic cation/carnitine transporter family in mice. J. Biol. Chem. 275:40064-40072 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 40064-40072
    • Tamai, I.1    Ohashi, R.2    Nezu, J.3    Sai, Y.4    Kobayashi, D.5    Oku, A.6    Shimane, M.7    Tsuji, A.8
  • 33
    • 0032577202 scopus 로고    scopus 로고
    • CDNA sequence, transport function, and genomic organization of human OCTN2, a new member of the organic cation transporter family
    • X. Wu, P. D. Prasad, F. H. Leibach, and V. Ganapathy. cDNA sequence, transport function, and genomic organization of human OCTN2, a new member of the organic cation transporter family. Biochem. Biophys. Res. Commun. 246:589-595 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 589-595
    • Wu, X.1    Prasad, P.D.2    Leibach, F.H.3    Ganapathy, V.4
  • 38
    • 0036792072 scopus 로고    scopus 로고
    • Identification of OCT6 as a novel organic cation transporter preferentially expressed in hematopoietic cells and leukemias
    • S. Gong, X. Lu, Y. Xu, C. F. Swiderski, C. T. Jordan, and J. A. Moscow. Identification of OCT6 as a novel organic cation transporter preferentially expressed in hematopoietic cells and leukemias. Exp. Hematol. 30:1162-1169 (2002).
    • (2002) Exp. Hematol. , vol.30 , pp. 1162-1169
    • Gong, S.1    Lu, X.2    Xu, Y.3    Swiderski, C.F.4    Jordan, C.T.5    Moscow, J.A.6
  • 39
    • 33749327002 scopus 로고    scopus 로고
    • Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations
    • M. Hiasa, T. Matsumoto, T. Komatsu, and Y. Moriyama. Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations. Am. J. Physiol. Cell Physiol. 291:478-486 (2006).
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291 , pp. 678-686
    • Hiasa, M.1    Matsumoto, T.2    Komatsu, T.3    Moriyama, Y.4
  • 40
    • 33746508758 scopus 로고    scopus 로고
    • +/organic cation antiporter MATE1
    • T. Terada, S. Masuda, J.-i. Asaka, M. Tsuda, T. Katsura, and K.-i. Inui. Molecular cloning, functional characterization and tissue distribution of rat H+/organic cation antiporter MATE1. Pharm. Res. 23:1696-1701 (2006).
    • (2006) Pharm. Res. , vol.23 , pp. 1696-1701
    • Terada, T.1    Masuda, S.2    Asaka, J.-I.3    Tsuda, M.4    Katsura, T.5    Inui, K.-I.6
  • 41
    • 33751106714 scopus 로고    scopus 로고
    • + antiporter in the kidney
    • K. Y. Ohta, K. Inoue, Y. Hayashi, and H. Yuasa. Molecular identification and functional characterization of rat MATE1 as an organic cation/H+ antiporter in the kidney. Drug Metab. Dispos. 34:1868-1874 (2006).
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 1868-1874
    • Ohta, K.Y.1    Inoue, K.2    Hayashi, Y.3    Yuasa, H.4
  • 42
  • 43
    • 0035882382 scopus 로고    scopus 로고
    • Maintenance of serotonin in the intestinal mucosa and ganglia of mice that lack the high-affinity serotonin transporter: Abnormal intestinal motility and the expression of cation transporters
    • J. J. Chen, Z. Li, H. Pan, D. L. Murphy, H. Tamir, H. Koepsell, and M. D. Gershon. Maintenance of serotonin in the intestinal mucosa and ganglia of mice that lack the high-affinity serotonin transporter: abnormal intestinal motility and the expression of cation transporters. J. Neurosci. 21:6348-6361 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 6348-6361
    • Chen, J.J.1    Li, Z.2    Pan, H.3    Murphy, D.L.4    Tamir, H.5    Koepsell, H.6    Gershon, M.D.7
  • 46
    • 0142212154 scopus 로고    scopus 로고
    • Constitutive expression of various xenobiotic and endobiotic transporter mRNAs in the choroid plexus of rats
    • S. Choudhuri, N. J. Cherrington, N. Li, and C. D. Klaassen. Constitutive expression of various xenobiotic and endobiotic transporter mRNAs in the choroid plexus of rats. Drug Metab. Dispos. 31:1337-1345 (2003).
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1337-1345
    • Choudhuri, S.1    Cherrington, N.J.2    Li, N.3    Klaassen, C.D.4
  • 48
    • 0036146331 scopus 로고    scopus 로고
    • Tissue distribution and renal developmental changes in rat organic cation transporter mRNA levels
    • A. L. Slitt, N. J. Cherrington, D. P. Hartley, T. M. Leazer, and C. D. Klaassen. Tissue distribution and renal developmental changes in rat organic cation transporter mRNA levels. Drug Metab. Dispos. 30:212-219 (2002).
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 212-219
    • Slitt, A.L.1    Cherrington, N.J.2    Hartley, D.P.3    Leazer, T.M.4    Klaassen, C.D.5
  • 49
    • 33344454764 scopus 로고    scopus 로고
    • Tissue distribution and ontogeny of organic cation transporters in mice
    • Y. Alnouti, J. S. Petrick, and C. D. Klaassen. Tissue distribution and ontogeny of organic cation transporters in mice. Drug Metab. Dispos. 34:477-482 (2006).
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 477-482
    • Alnouti, Y.1    Petrick, J.S.2    Klaassen, C.D.3
  • 50
    • 27744454598 scopus 로고    scopus 로고
    • Drug specificity and intestinal membrane localization of human organic cation transporters (OCT)
    • J. Müller, K. S. Lips, L. Metzner, R. H. H. Neubert, H. Koepsell, and M. Brandsch. Drug specificity and intestinal membrane localization of human organic cation transporters (OCT). Biochem. Pharmacol. 70:1851-1860 (2005).
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1851-1860
    • Müller, J.1    Lips, K.S.2    Metzner, L.3    Neubert, R.H.H.4    Koepsell, H.5    Brandsch, M.6
  • 51
    • 0036827601 scopus 로고    scopus 로고
    • Transporter gene expression in lactating and nonlactating human mammary epithelial cells using real-time reverse transcription-polymerase chain reaction
    • J. Alcorn, X. Lu, J. A. Moscow, and P. J. McNamara. Transporter gene expression in lactating and nonlactating human mammary epithelial cells using real-time reverse transcription-polymerase chain reaction. J. Pharmacol. Exp. Ther. 303:487-496 (2002).
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 487-496
    • Alcorn, J.1    Lu, X.2    Moscow, J.A.3    McNamara, P.J.4
  • 52
    • 0036022593 scopus 로고    scopus 로고
    • Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3
    • M. Hayer-Zillgen, M. Brüss, and H. Bönisch. Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3. Br. J. Pharmacol. 136:829-836 (2002).
    • (2002) Br. J. Pharmacol. , vol.136 , pp. 829-836
    • Hayer-Zillgen, M.1    Brüss, M.2    Bönisch, H.3
  • 54
    • 33747178997 scopus 로고    scopus 로고
    • Expression of transporters potentially involved in the targeting of cytostatic bile acid derivatives to colon cancer and polyps
    • M. R. Ballestero, M. J. Monte, O. Briz, F. Jimenez, F. Gonzalez-San Martin, and J. J. G. Marin. Expression of transporters potentially involved in the targeting of cytostatic bile acid derivatives to colon cancer and polyps. Biochem. Pharmacol. 72:729-738 (2006).
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 729-738
    • Ballestero, M.R.1    Monte, M.J.2    Briz, O.3    Jimenez, F.4    Gonzalez-San Martin, F.5    Marin, J.J.G.6
  • 57
    • 0035193166 scopus 로고    scopus 로고
    • Interactions between cimetidine, nitrofurantoin, and probenecid active transport into rat milk
    • P. M. Gerk, C. Y. Oo, E. W. Paxton, J. A. Moscow, and P. J. McNamara. Interactions between cimetidine, nitrofurantoin, and probenecid active transport into rat milk. J. Pharmacol. Exp. Ther. 296:175-180 (2001).
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 175-180
    • Gerk, P.M.1    Oo, C.Y.2    Paxton, E.W.3    Moscow, J.A.4    McNamara, P.J.5
  • 64
    • 0035834634 scopus 로고    scopus 로고
    • Ventricular choline transport: A role for organic cation transporter 2 expressed in choroid plexus
    • D. H. Sweet, D. S. Miller, and J. B. Pritchard. Ventricular choline transport: a role for organic cation transporter 2 expressed in choroid plexus. J. Biol. Chem. 276:41611-41619 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 41611-41619
    • Sweet, D.H.1    Miller, D.S.2    Pritchard, J.B.3
  • 66
    • 33747090656 scopus 로고    scopus 로고
    • Variability in mRNA expression of ABC- and SLC-transporters in human intestinal cells: Comparison between human segments and Caco-2 cells
    • A. Seithel, J. Karlsson, C. Hilgendorf, A. Björquist, and A. L. Ungell. Variability in mRNA expression of ABC- and SLC-transporters in human intestinal cells: comparison between human segments and Caco-2 cells. Eur. J. Pharm. Sci. 28:291-299 (2006).
    • (2006) Eur. J. Pharm. Sci. , vol.28 , pp. 291-299
    • Seithel, A.1    Karlsson, J.2    Hilgendorf, C.3    Björquist, A.4    Ungell, A.-L.5
  • 67
    • 0037101913 scopus 로고    scopus 로고
    • Organic cation transporter mRNA and function in the rat superior cervical ganglion
    • D. Kristufek, W. Rudorfer, C. Pifl, and S. Huck. Organic cation transporter mRNA and function in the rat superior cervical ganglion. J. Physiol. 543:117-134 (2002).
    • (2002) J. Physiol. , vol.543 , pp. 117-134
    • Kristufek, D.1    Rudorfer, W.2    Pifl, C.3    Huck, S.4
  • 68
    • 0344406174 scopus 로고    scopus 로고
    • 1-Methyl-4-phenylpyridinium accumulates in cerebellar granule neurons via organic cation transporter 3
    • T. Shang, A. V. Uihlein, J. Van Asten, B. Kalyanaraman, and C. J. Hillard. 1-Methyl-4-phenylpyridinium accumulates in cerebellar granule neurons via organic cation transporter 3. J. Neurochem. 85:358-367 (2003).
    • (2003) J. Neurochem. , vol.85 , pp. 358-367
    • Shang, T.1    Uihlein, A.V.2    Van Asten, J.3    Kalyanaraman, B.4    Hillard, C.J.5
  • 69
    • 0037269107 scopus 로고    scopus 로고
    • Expression and functional characterization of the extraneuronal monoamine transporter in normal human astrocytes
    • M. Inazu, H. Takeda, and T. Matsumiya. Expression and functional characterization of the extraneuronal monoamine transporter in normal human astrocytes. J. Neurochem. 84:43-52 (2003).
    • (2003) J. Neurochem. , vol.84 , pp. 43-52
    • Inazu, M.1    Takeda, H.2    Matsumiya, T.3
  • 70
  • 72
    • 0032484146 scopus 로고    scopus 로고
    • 2) and evidence for the expression of the transporter in the brain
    • X. Wu, R. Kekuda, W. Huang, Y.-J. Fei, F. H. Leibach, J. Chen, S. J. Conway, and V. Ganapathy. Identity of the organic cation transporter OCT3 as the extraneuronal monoamine transporter (uptake2) and evidence for the expression of the transporter in the brain. J. Biol. Chem. 273:32776-32786 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 32776-32786
    • Wu, X.1    Kekuda, R.2    Huang, W.3    Fei, Y.-J.4    Leibach, F.H.5    Chen, J.6    Conway, S.J.7    Ganapathy, V.8
  • 73
    • 33748264554 scopus 로고    scopus 로고
    • Corticosterone-sensitive monoamine transport in the rat dorsomedial hypothalamus: Potential role for organic cation transporter 3 in stress-induced modulation of monoaminergic neurotransmission
    • P. J. Gasser, C. A. Lowry, and M. Orchinik. Corticosterone-sensitive monoamine transport in the rat dorsomedial hypothalamus: potential role for organic cation transporter 3 in stress-induced modulation of monoaminergic neurotransmission. J. Neurosci. 26:8758-8766 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 8758-8766
    • Gasser, P.J.1    Lowry, C.A.2    Orchinik, M.3
  • 74
    • 1642357402 scopus 로고    scopus 로고
    • Organic cation transporter 3 (Slc22a3) is implicated in salt-intake regulation
    • V. Vialou, A. Amphoux, R. Zwart, B. Giros, and S. Gautron. Organic cation transporter 3 (Slc22a3) is implicated in salt-intake regulation. J. Neurosci. 24:2846-2851 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 2846-2851
    • Vialou, V.1    Amphoux, A.2    Zwart, R.3    Giros, B.4    Gautron, S.5
  • 77
    • 33744801418 scopus 로고    scopus 로고
    • Novel localization of OCTN1, an organic cation/carnitine transporter, to mammalian mitochondria
    • A.-M. Lamhonwah and I. Tein. Novel localization of OCTN1, an organic cation/carnitine transporter, to mammalian mitochondria. Biochem. Biophys. Res. Commun. 345:1315-1325 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 1315-1325
    • Lamhonwah, A.-M.1    Tein, I.2
  • 78
    • 27144467098 scopus 로고    scopus 로고
    • Epitope shared by functional variant of organic cation/carnitine transporter, OCTN1, Campylobacter jejuni and Mycobacterium paratuberculosis may underlie susceptibility to Crohn's disease at 5q31
    • A.-M. Lamhonwah, C. Ackerley, R. Onizuka, A. Tilups, D. Lamhonwah, C. Chung, K. S. Tao, R. Tellier, and I. Tein. Epitope shared by functional variant of organic cation/carnitine transporter, OCTN1, Campylobacter jejuni and Mycobacterium paratuberculosis may underlie susceptibility to Crohn's disease at 5q31. Biochem. Biophys. Res. Commun. 337:1165-1175 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1165-1175
    • Lamhonwah, A.-M.1    Ackerley, C.2    Onizuka, R.3    Tilups, A.4    Lamhonwah, D.5    Chung, C.6    Tao, K.S.7    Tellier, R.8    Tein, I.9
  • 80
    • 0032493741 scopus 로고    scopus 로고
    • Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2
    • I. Tamai, R. Ohashi, J. Nezu, H. Yabuuchi, A. Oku, M. Shimane, Y. Sai, and A. Tsuji. Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2. J. Biol. Chem. 273:20378-20382 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 20378-20382
    • Tamai, I.1    Ohashi, R.2    Nezu, J.3    Yabuuchi, H.4    Oku, A.5    Shimane, M.6    Sai, Y.7    Tsuji, A.8
  • 82
    • 33645280080 scopus 로고    scopus 로고
    • Functional expression of the organic cation/carnitine transporter 2 in rat astrocytes
    • M. Inazu, H. Takeda, K. Maehara, K. Miyashita, A. Tomoda, and T. Matsumiya. Functional expression of the organic cation/carnitine transporter 2 in rat astrocytes. J. Neurochem. 97:424-434 (2006).
    • (2006) J. Neurochem. , vol.97 , pp. 424-434
    • Inazu, M.1    Takeda, H.2    Maehara, K.3    Miyashita, K.4    Tomoda, A.5    Matsumiya, T.6
  • 83
    • 0035815991 scopus 로고    scopus 로고
    • +-coupled transport of L-carnitine via high-affinity carnitine transporter OCTN2 and its subcellular localization in kidney
    • I. Tamai, K. China, Y. Sai, D. Kobayashi, J.-i. Nezu, E. Kawahara, and A. Tsuji. Na+-coupled transport of L-carnitine via high-affinity carnitine transporter OCTN2 and its subcellular localization in kidney. Biochim. Biophys. Acta 1512:273-284 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 273-284
    • Tamai, I.1    China, K.2    Sai, Y.3    Kobayashi, D.4    Nezu, J.-I.5    Kawahara, E.6    Tsuji, A.7
  • 84
    • 33744796298 scopus 로고    scopus 로고
    • Expression and distribution of OCTN2 in mouse epididymis and its association with obstructive azoospermia in juvenile visceral steatosis mice
    • K. Yakushiji, S. Kai, M. Yamauchi, M. Kuwajima, Y. Osada, and K. Toshimori. Expression and distribution of OCTN2 in mouse epididymis and its association with obstructive azoospermia in juvenile visceral steatosis mice. Int. J. Urol. 13:420-426 (2006).
    • (2006) Int. J. Urol. , vol.13 , pp. 420-426
    • Yakushiji, K.1    Kai, S.2    Yamauchi, M.3    Kuwajima, M.4    Osada, Y.5    Toshimori, K.6
  • 85
    • 12944271972 scopus 로고    scopus 로고
    • +-independent L-carnitine transporter in enterocytes basolateral membrane
    • J. M. Durán, M. J. Peral, M. L. Calonge, and A. A. Ilundáin. OCTN3: A Na+-independent L-carnitine transporter in enterocytes basolateral membrane. J. Cell. Physiol. 202:929-935 (2005).
    • (2005) J. Cell. Physiol. , vol.202 , pp. 929-935
    • Durán, J.M.1    Peral, M.J.2    Calonge, M.L.3    Ilundáin, A.A.4
  • 86
    • 0037474487 scopus 로고    scopus 로고
    • A third human carnitine/organic cation transporter (OCTN3) as a candidate for the 5q31 Crohn's disease locus (IBD5)
    • A.-M. Lamhonwah, J. Skaug, S. W. Scherer, and I. Tein. A third human carnitine/organic cation transporter (OCTN3) as a candidate for the 5q31 Crohn's disease locus (IBD5). Biochem. Biophys. Res. Commun. 301:98-101 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 98-101
    • Lamhonwah, A.-M.1    Skaug, J.2    Scherer, S.W.3    Tein, I.4
  • 88
    • 21644488840 scopus 로고    scopus 로고
    • Alkali cation binding and permeation in the rat organic cation transporter rOCT2
    • B. M. Schmitt and H. Koepsell. Alkali cation binding and permeation in the rat organic cation transporter rOCT2. J. Biol. Chem. 280:24481-24490 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 24481-24490
    • Schmitt, B.M.1    Koepsell, H.2
  • 89
    • 0032966119 scopus 로고    scopus 로고
    • Molecular mechanisms of organic cation transport in OCT2-expressing Xenopus oocytes
    • M. Okuda, Y. Urakami, H. Saito, and K.-i. Inui. Molecular mechanisms of organic cation transport in OCT2-expressing Xenopus oocytes. Biochim. Biophys. Acta 1417:224-231 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1417 , pp. 224-231
    • Okuda, M.1    Urakami, Y.2    Saito, H.3    Inui, K.-I.4
  • 93
    • 0034010850 scopus 로고    scopus 로고
    • Kinetic and selectivity differences between rodent, rabbit, and human organic cation transporters (OCT1)
    • M. J. Dresser, A. T. Gray, and K. M. Giacomini. Kinetic and selectivity differences between rodent, rabbit, and human organic cation transporters (OCT1). J. Pharmacol. Exp. Ther. 292:1146-1152 (2000).
    • (2000) J. Pharmacol. Exp. Ther. , vol.292 , pp. 1146-1152
    • Dresser, M.J.1    Gray, A.T.2    Giacomini, K.M.3
  • 94
    • 24644492295 scopus 로고    scopus 로고
    • Purification and functional reconstitution of the rat organic cation transporter OCT1
    • T. Keller, M. Elfeber, V. Gorboulev, H. Reiländer, and H. Koepsell. Purification and functional reconstitution of the rat organic cation transporter OCT1. Biochemistry 44:12253-12263 (2005).
    • (2005) Biochemistry , vol.44 , pp. 12253-12263
    • Keller, T.1    Elfeber, M.2    Gorboulev, V.3    Reiländer, H.4    Koepsell, H.5
  • 95
    • 0036198625 scopus 로고    scopus 로고
    • Human organic anion transporters and human organic cation transporters mediate renal transport of prostaglandins
    • H. Kimura, M. Takeda, S. Narikawa, A. Enomoto, K. Ichida, and H. Endou. Human organic anion transporters and human organic cation transporters mediate renal transport of prostaglandins. J. Pharmacol. Exp. Ther. 301:293-298 (2002).
    • (2002) J. Pharmacol. Exp. Ther. , vol.301 , pp. 293-298
    • Kimura, H.1    Takeda, M.2    Narikawa, S.3    Enomoto, A.4    Ichida, K.5    Endou, H.6
  • 97
    • 0142179119 scopus 로고    scopus 로고
    • Different affinities of inhibitors to the outwardly and inwardly directed substrate binding site of organic cation transporter 2
    • C. Volk, V. Gorboulev, T. Budiman, G. Nagel, and H. Koepsell. Different affinities of inhibitors to the outwardly and inwardly directed substrate binding site of organic cation transporter 2. Mol. Pharmacol. 64:1037-1047 (2003).
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1037-1047
    • Volk, C.1    Gorboulev, V.2    Budiman, T.3    Nagel, G.4    Koepsell, H.5
  • 98
    • 0034703068 scopus 로고    scopus 로고
    • Mechanism of electrogenic cation transport by the cloned organic cation transporter 2 from rat
    • T. Budiman, E. Bamberg, H. Koepsell, and G. Nagel. Mechanism of electrogenic cation transport by the cloned organic cation transporter 2 from rat. J. Biol. Chem. 275:29413-29420 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29413-29420
    • Budiman, T.1    Bamberg, E.2    Koepsell, H.3    Nagel, G.4
  • 99
    • 0032696186 scopus 로고    scopus 로고
    • +-dependent carnitine transport by organic cation transporter (OCTN2): Its pharmacological and toxicological relevance
    • R. Ohashi, I. Tamai, H. Yabuuchi, J. -i Nezu, A. Oku, Y. Sai, M. Shimane, and A. Tsuji. Na(+)-dependent carnitine transport by organic cation transporter (OCTN2): its pharmacological and toxicological relevance. J. Pharmacol. Exp. Ther. 291:778-784 (1999).
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , pp. 778-784
    • Ohashi, R.1    Tamai, I.2    Yabuuchi, H.3    Nezu, J.-I.4    Oku, A.5    Sai, Y.6    Shimane, M.7    Tsuji, A.8
  • 100
    • 0032767691 scopus 로고    scopus 로고
    • Functional characteristics and tissue distribution pattern of organic cation transporter 2 (OCTN2), an organic cation/carnitine transporter
    • X. Wu, W. Huang, P. D. Prasad, P. Seth, D. P. Rajan, F. H. Leibach, J. Chen, S. J. Conway, and V. Ganapathy. Functional characteristics and tissue distribution pattern of organic cation transporter 2 (OCTN2), an organic cation/carnitine transporter. J. Pharmacol. Exp. Ther. 290:1482-1492 (1999).
    • (1999) J. Pharmacol. Exp. Ther. , vol.290 , pp. 1482-1492
    • Wu, X.1    Huang, W.2    Prasad, P.D.3    Seth, P.4    Rajan, D.P.5    Leibach, F.H.6    Chen, J.7    Conway, S.J.8    Ganapathy, V.9
  • 102
    • 0032935034 scopus 로고    scopus 로고
    • Novel membrane transporter OCTN1 mediates multispecific, bidirectional, and pH-dependent transport of organic cations
    • H. Yabuuchi, I. Tamai, J. Nezu, K. Sakamoto, A. Oku, M. Shimane, Y. Sai, and A. Tsuji. Novel membrane transporter OCTN1 mediates multispecific, bidirectional, and pH-dependent transport of organic cations. J. Pharmacol. Exp. Ther. 289:768-773 (1999).
    • (1999) J. Pharmacol. Exp. Ther. , vol.289 , pp. 768-773
    • Yabuuchi, H.1    Tamai, I.2    Nezu, J.3    Sakamoto, K.4    Oku, A.5    Shimane, M.6    Sai, Y.7    Tsuji, A.8
  • 103
    • 15744362693 scopus 로고    scopus 로고
    • Molecular determinants of substrate/inhibitor binding to the human and rabbit renal organic cation transporters hOCT2 and rbOCT2
    • W. M. Suhre, S. Ekins, C. Chang, P. W. Swaan, and S. H. Wright. Molecular determinants of substrate/inhibitor binding to the human and rabbit renal organic cation transporters hOCT2 and rbOCT2. Mol. Pharmacol. 67:1067-1077 (2005).
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1067-1077
    • Suhre, W.M.1    Ekins, S.2    Chang, C.3    Swaan, P.W.4    Wright, S.H.5
  • 107
    • 0031846917 scopus 로고    scopus 로고
    • Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa)
    • L. Zhang, M. E. Schaner, and K. M. Giacomini. Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa). J. Pharmacol. Exp. Ther. 286:354-361 (1998).
    • (1998) J. Pharmacol. Exp. Ther. , vol.286 , pp. 354-361
    • Zhang, L.1    Schaner, M.E.2    Giacomini, K.M.3
  • 109
    • 25644452793 scopus 로고    scopus 로고
    • A species difference in the transport activities of H2 receptor antagonists by rat and human renal organic anion and cation transporters
    • H. Tahara, H. Kusuhara, H. Endou, H. Koepsell, T. Imaoka, E. Fuse, and Y. Sugiyama. A species difference in the transport activities of H2 receptor antagonists by rat and human renal organic anion and cation transporters. J. Pharmacol. Exp. Ther. 315:337-345 (2005).
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 337-345
    • Tahara, H.1    Kusuhara, H.2    Endou, H.3    Koepsell, H.4    Imaoka, T.5    Fuse, E.6    Sugiyama, Y.7
  • 113
    • 0034052434 scopus 로고    scopus 로고
    • Interactions of HIV protease inhibitors with a human organic cation transporter in a mammalian expression system
    • L. Zhang, W. Gorset, C. B. Washington, T. F. Blaschke, D. L. Kroetz, and K. M. Giacomini. Interactions of HIV protease inhibitors with a human organic cation transporter in a mammalian expression system. Drug Metab. Dispos. 28:329-334 (2000).
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 329-334
    • Zhang, L.1    Gorset, W.2    Washington, C.B.3    Blaschke, T.F.4    Kroetz, D.L.5    Giacomini, K.M.6
  • 115
    • 0842289357 scopus 로고    scopus 로고
    • Transporter-mediated renal handling of nafamostat mesilate
    • Q. Li, Y. Sai, Y. Kato, H. Muraoka, I. Tamai, and A. Tsuji. Transporter-mediated renal handling of nafamostat mesilate. J. Pharm. Sci. 93:262-272 (2004).
    • (2004) J. Pharm. Sci. , vol.93 , pp. 262-272
    • Li, Q.1    Sai, Y.2    Kato, Y.3    Muraoka, H.4    Tamai, I.5    Tsuji, A.6
  • 116
    • 0037309520 scopus 로고    scopus 로고
    • Agmatine is efficiently transported by non-neuronal monoamine transporters extraneuronal monoamine transporter (EMT) and organic cation transporter 2 (OCT2)
    • D. Gründemann, C. Hahne, R. Berkels, and E. Schömig. Agmatine is efficiently transported by non-neuronal monoamine transporters extraneuronal monoamine transporter (EMT) and organic cation transporter 2 (OCT2). J. Pharmacol. Exp. Ther. 304:810-817 (2003).
    • (2003) J. Pharmacol. Exp. Ther. , vol.304 , pp. 810-817
    • Gründemann, D.1    Hahne, C.2    Berkels, R.3    Schömig, E.4
  • 117
    • 0036721409 scopus 로고    scopus 로고
    • Studies on functional sites of organic cation/carnitine transporter OCTN2 (SLC22A5) using a Ser467Cys mutant protein
    • R. Ohashi, I. Tamai, A. Inano, M. Katsura, Y. Sai, J.-I. Nezu, and A. Tsuji. Studies on functional sites of organic cation/carnitine transporter OCTN2 (SLC22A5) using a Ser467Cys mutant protein. J. Pharmacol. Exp. Ther. 302:1286-1294 (2002).
    • (2002) J. Pharmacol. Exp. Ther. , vol.302 , pp. 1286-1294
    • Ohashi, R.1    Tamai, I.2    Inano, A.3    Katsura, M.4    Sai, Y.5    Nezu, J.-I.6    Tsuji, A.7
  • 118
    • 0036689433 scopus 로고    scopus 로고
    • Interactions of n-tetraalkylammonium compounds and biguanides with a human renal organic cation transporter (hOCT2)
    • M. J. Dresser, G. Xiao, M. K. Leabman, A. T. Gray, and K. M. Giacomini. Interactions of n-tetraalkylammonium compounds and biguanides with a human renal organic cation transporter (hOCT2). Pharm. Res. 19:1244-1247 (2002).
    • (2002) Pharm. Res. , vol.19 , pp. 1244-1247
    • Dresser, M.J.1    Xiao, G.2    Leabman, M.K.3    Gray, A.T.4    Giacomini, K.M.5
  • 122
    • 16544379186 scopus 로고    scopus 로고
    • Functional regions of organic cation/carnitine transporter OCTN2 (SLC22A5): Roles in carnitine recognition
    • A. Inano, Y. Sai, Y. Kato, I. Tamai, M. Ishiguro, and A. Tsuji. Functional regions of organic cation/carnitine transporter OCTN2 (SLC22A5): roles in carnitine recognition. Drug Metab. Pharmacokinet. 19:180-189 (2004).
    • (2004) Drug Metab. Pharmacokinet. , vol.19 , pp. 180-189
    • Inano, A.1    Sai, Y.2    Kato, Y.3    Tamai, I.4    Ishiguro, M.5    Tsuji, A.6
  • 123
    • 0033585084 scopus 로고    scopus 로고
    • Mutations in novel organic cation transporter (OCTN2), an organic cation/carnitine transporter, with differential effects on the organic cation transport function and the carnitine transport function
    • P. Seth, X. Wu, W. Huang, F. H. Leibach, and V. Ganapathy. Mutations in novel organic cation transporter (OCTN2), an organic cation/carnitine transporter, with differential effects on the organic cation transport function and the carnitine transport function. J. Biol. Chem. 274:33388-33392 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 33388-33392
    • Seth, P.1    Wu, X.2    Huang, W.3    Leibach, F.H.4    Ganapathy, V.5
  • 124
    • 0001762461 scopus 로고    scopus 로고
    • Characterization of L-carnitine transport into rat skeletal muscle plasma membrane vesicles
    • S. Berardi, B. Stieger, B. Hagenbuch, E. Carafoli, and S. Krähenbühl. Characterization of L-carnitine transport into rat skeletal muscle plasma membrane vesicles. Eur. J. Biochem. 267:1985-1994 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1985-1994
    • Berardi, S.1    Stieger, B.2    Hagenbuch, B.3    Carafoli, E.4    Krähenbühl, S.5
  • 125
    • 0029030612 scopus 로고
    • Characterization of L-carnitine transport by rat kidney brush-border-membrane vesicles
    • B. Stieger, B. O'Neill, and S. Krähenbühl. Characterization of L-carnitine transport by rat kidney brush-border-membrane vesicles. Biochem. J. 309:643-647 (1995).
    • (1995) Biochem. J. , vol.309 , pp. 643-647
    • Stieger, B.1    O'Neill, B.2    Krähenbühl, S.3
  • 126
    • 0021743458 scopus 로고
    • Sodium gradient-stimulated transport of L-carnitine into renal brush border membrane vesicles: Kinetics, specificity, and regulation by dietary carnitine
    • C. J. Rebouche and D. L. Mack. Sodium gradient-stimulated transport of L-carnitine into renal brush border membrane vesicles: kinetics, specificity, and regulation by dietary carnitine. Arch. Biochem. Biophys. 235:393-402 (1984).
    • (1984) Arch. Biochem. Biophys. , vol.235 , pp. 393-402
    • Rebouche, C.J.1    MacK, D.L.2
  • 131
    • 0035206702 scopus 로고    scopus 로고
    • Regulation of human extraneuronal monoamine transporter (hEMT) expressed in HEK293 cells by intracellular second messenger systems
    • F. Martel, E. Keating, C. Calhau, D. Gründemann, E. Schömig, and I. Azevedo. Regulation of human extraneuronal monoamine transporter (hEMT) expressed in HEK293 cells by intracellular second messenger systems. Naunyn Schmiedeberg's Arch. Pharmacol. 364:487-495 (2001).
    • (2001) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.364 , pp. 487-495
    • Martel, F.1    Keating, E.2    Calhau, C.3    Gründemann, D.4    Schömig, E.5    Azevedo, I.6
  • 132
    • 0035823636 scopus 로고    scopus 로고
    • Properties and regulation of organic cation transport in freshly isolated human proximal tubules
    • G. Pietig, T. Mehrens, J. R. Hirsch, I. Çetinkaya, H. Piechota, and E. Schlatter. Properties and regulation of organic cation transport in freshly isolated human proximal tubules. J. Biol. Chem. 276:33741-33746 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 33741-33746
    • Pietig, G.1    Mehrens, T.2    Hirsch, J.R.3    Çetinkaya, I.4    Piechota, H.5    Schlatter, E.6
  • 133
    • 6344251595 scopus 로고    scopus 로고
    • Screening of the interaction between xenobiotic transporters and PDZ proteins
    • Y. Kato, K. Yoshida, C. Watanabe, Y. Sai, and A. Tsuji. Screening of the interaction between xenobiotic transporters and PDZ proteins. Pharm. Res. 21:1886-1894 (2004).
    • (2004) Pharm. Res. , vol.21 , pp. 1886-1894
    • Kato, Y.1    Yoshida, K.2    Watanabe, C.3    Sai, Y.4    Tsuji, A.5
  • 134
    • 14944364233 scopus 로고    scopus 로고
    • PDZK1 directly regulates the function of organic cation/carnitine transporter OCTN2
    • Y. Kato, Y. Sai, K. Yoshida, C. Watanabe, T. Hirata, and A. Tsuji. PDZK1 directly regulates the function of organic cation/carnitine transporter OCTN2. Mol. Pharmacol. 67:734-743 (2005).
    • (2005) Mol. Pharmacol. , vol.67 , pp. 734-743
    • Kato, Y.1    Sai, Y.2    Yoshida, K.3    Watanabe, C.4    Hirata, T.5    Tsuji, A.6
  • 136
    • 0015419633 scopus 로고
    • Sex differences in organic ion transport by rat kidney
    • H. M. Bowman and J. B. Hook. Sex differences in organic ion transport by rat kidney. Proc. Soc. Exp. Biol. Med. 141:258-262 (1972).
    • (1972) Proc. Soc. Exp. Biol. Med. , vol.141 , pp. 258-262
    • Bowman, H.M.1    Hook, J.B.2
  • 138
    • 0034640217 scopus 로고    scopus 로고
    • Hormonal regulation of organic cation transporter OCT2 expression in rat kidney
    • Y. Urakami, M. Okuda, H. Saito, and K.-i. Inui. Hormonal regulation of organic cation transporter OCT2 expression in rat kidney. FEBS Lett. 473:173-176 (2000).
    • (2000) FEBS Lett. , vol.473 , pp. 173-176
    • Urakami, Y.1    Okuda, M.2    Saito, H.3    Inui, K.-I.4
  • 139
    • 0034816905 scopus 로고    scopus 로고
    • Functional characteristics and steroid hormone-mediated regulation of an organic cation transporter in madin-darby canine kidney cells
    • Y. Shu, C. L. Bello, L. M. Mangravite, B. Feng, and K. M. Giacomini. Functional characteristics and steroid hormone-mediated regulation of an organic cation transporter in madin-darby canine kidney cells. J. Pharmacol. Exp. Ther. 299:392-398 (2001).
    • (2001) J. Pharmacol. Exp. Ther. , vol.299 , pp. 392-398
    • Shu, Y.1    Bello, C.L.2    Mangravite, L.M.3    Feng, B.4    Giacomini, K.M.5
  • 140
    • 33646405992 scopus 로고    scopus 로고
    • Androgen receptor is responsible for rat organic cation transporter 2 gene regulation but not for rOCT1 and rOCT3
    • J.-i. Asaka, T. Terada, M. Okuda, T. Katsura, and K.-i. Inui. Androgen receptor is responsible for rat organic cation transporter 2 gene regulation but not for rOCT1 and rOCT3. Pharm. Res. 1-8 (2006).
    • (2006) Pharm. Res. , pp. 1-8
    • Asaka, J.-I.1    Terada, T.2    Okuda, M.3    Katsura, T.4    Inui, K.-I.5
  • 141
    • 31144465910 scopus 로고    scopus 로고
    • Sex differences in the mRNA, protein, and functional expression of organic anion transporter (Oat) 1, Oat3, and organic cation transporter (Oct) 2 in rabbit renal proximal tubules
    • C. E. Groves, W. B. Suhre, N. J. Cherrington, and S. H. Wright. Sex differences in the mRNA, protein, and functional expression of organic anion transporter (Oat) 1, Oat3, and organic cation transporter (Oct) 2 in rabbit renal proximal tubules. J. Pharmacol. Exp. Ther. 316:743-752 (2006).
    • (2006) J. Pharmacol. Exp. Ther. , vol.316 , pp. 743-752
    • Groves, C.E.1    Suhre, W.B.2    Cherrington, N.J.3    Wright, S.H.4
  • 142
    • 33645870991 scopus 로고    scopus 로고
    • The human organic cation transporter-1 gene is transactivated by hepatocyte nuclear factor-4α
    • M. Saborowski, G. A. Kullak-Ublick, and J. J. Eloranta. The human organic cation transporter-1 gene is transactivated by hepatocyte nuclear factor-4a. J. Pharmacol. Exp. Ther. 317:778-785 (2006).
    • (2006) J. Pharmacol. Exp. Ther. , vol.317 , pp. 778-785
    • Saborowski, M.1    Kullak-Ublick, G.A.2    Eloranta, J.J.3
  • 144
    • 0035991421 scopus 로고    scopus 로고
    • Down-regulation of rat organic cation transporter rOCT2 by 5/6 nephrectomy
    • L. Ji, S. Masuda, H. Saito, and K.-I. Inui. Down-regulation of rat organic cation transporter rOCT2 by 5/6 nephrectomy. Kidney Int. 62:514-524 (2002).
    • (2002) Kidney Int. , vol.62 , pp. 514-524
    • Ji, L.1    Masuda, S.2    Saito, H.3    Inui, K.-I.4
  • 146
  • 147
    • 0036251872 scopus 로고    scopus 로고
    • Functional impairment of renal organic cation transport in experimental diabetes
    • B. Grover, C. Auberger, R. Sarangarajan, and W. Cacini. Functional impairment of renal organic cation transport in experimental diabetes. Pharmacol. Toxicol. 90:181-186 (2002).
    • (2002) Pharmacol. Toxicol. , vol.90 , pp. 181-186
    • Grover, B.1    Auberger, C.2    Sarangarajan, R.3    Cacini, W.4
  • 148
    • 0042261645 scopus 로고    scopus 로고
    • Decreased activity of basolateral organic ion transports in hyperuricemic rat kidney: Roles of organic ion transporters, rOAT1, rOAT3 and rOCT2
    • Y. Habu, I. Yano, A. Takeuchi, H. Saito, M. Okuda, A. Fukatsu, and K.-i. Inui. Decreased activity of basolateral organic ion transports in hyperuricemic rat kidney: roles of organic ion transporters, rOAT1, rOAT3 and rOCT2. Biochem. Pharmacol. 66:1107-1114 (2003).
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1107-1114
    • Habu, Y.1    Yano, I.2    Takeuchi, A.3    Saito, H.4    Okuda, M.5    Fukatsu, A.6    Inui, K.-I.7
  • 149
    • 2342452711 scopus 로고    scopus 로고
    • Down-regulation of the organic cation transporter 1 of rat liver in obstructive cholestasis
    • G. U. Denk, C. J. Soroka, A. Mennone, H. Koepsell, U. Beuers, and J. L. Boyer. Down-regulation of the organic cation transporter 1 of rat liver in obstructive cholestasis. Hepatology 39:1382-1389 (2004).
    • (2004) Hepatology , vol.39 , pp. 1382-1389
    • Denk, G.U.1    Soroka, C.J.2    Mennone, A.3    Koepsell, H.4    Beuers, U.5    Boyer, J.L.6
  • 150
    • 3042599451 scopus 로고    scopus 로고
    • Lipopolysaccharide-mediated regulation of hepatic transporter mRNA levels in rats
    • N. J. Cherrington, A. L. Slitt, N. Li, and C. D. Klaassen. Lipopolysaccharide-mediated regulation of hepatic transporter mRNA levels in rats. Drug Metab. Dispos. 32:734-741 (2004).
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 734-741
    • Cherrington, N.J.1    Slitt, A.L.2    Li, N.3    Klaassen, C.D.4
  • 152
    • 23744497058 scopus 로고    scopus 로고
    • Regulation of testis-specific carnitine transporter (octn3) gene by proximal cis-acting elements Sp1 in mice
    • T. Maeda, M. Hirayama, D. Kobayashi, and I. Tamai. Regulation of testis-specific carnitine transporter (octn3) gene by proximal cis-acting elements Sp1 in mice. Biochem. Pharmacol. 70:858-868 (2005).
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 858-868
    • Maeda, T.1    Hirayama, M.2    Kobayashi, D.3    Tamai, I.4
  • 154
    • 0034935038 scopus 로고    scopus 로고
    • Reduced hepatic uptake and intestinal excretion of organic cations in mice with a targeted disruption of the organic cation transporter 1 (oct1[Slc22a1]) gene
    • J. W. Jonker, E. Wagenaar, C. A. A. M. Mol, M. Buitelaar, H. Koepsell, J. W. Smit, and A. H. Schinkel. Reduced hepatic uptake and intestinal excretion of organic cations in mice with a targeted disruption of the organic cation transporter 1 (oct1[Slc22a1]) gene. Mol. Cell. Biol. 21:5471-5477 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5471-5477
    • Jonker, J.W.1    Wagenaar, E.2    Mol, C.A.A.M.3    Buitelaar, M.4    Koepsell, H.5    Smit, J.W.6    Schinkel, A.H.7
  • 155
    • 0034975789 scopus 로고    scopus 로고
    • Impaired activity of the extraneuronal monoamine transporter system known as uptake-2 in Orct3/Slc22a3-deficient mice
    • R. Zwart, S. Verhaagh, M. Buitelaar, C. Popp-Snijders, and D. P. Barlow. Impaired activity of the extraneuronal monoamine transporter system known as uptake-2 in Orct3/Slc22a3-deficient mice. Mol. Cell Biol. 21:4188-4196 (2001).
    • (2001) Mol. Cell Biol. , vol.21 , pp. 4188-4196
    • Zwart, R.1    Verhaagh, S.2    Buitelaar, M.3    Popp-Snijders, C.4    Barlow, D.P.5
  • 156
    • 0142123151 scopus 로고    scopus 로고
    • Deficiency in the organic cation transporters 1 and 2 (oct1/oct2 [slc22a1/slc22a2]) in mice abolishes renal secretion of organic cations
    • J. W. Jonker, E. Wagenaar, S. van Eijl, and A. H. Schinkel. Deficiency in the organic cation transporters 1 and 2 (oct1/oct2 [slc22a1/slc22a2]) in mice abolishes renal secretion of organic cations. Mol. Cell Biol. 23:7902-7908 (2003).
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7902-7908
    • Jonker, J.W.1    Wagenaar, E.2    Van Eijl, S.3    Schinkel, A.H.4
  • 159
    • 0032573562 scopus 로고    scopus 로고
    • A missense mutation of mouse OCTN2, a sodium-dependent carnitine cotransporter, in the juvenile visceral steatosis mouse
    • K.-m. Lu, H. Nishimori, Y. Nakamura, K. Shima, and M. Kuwajima. A missense mutation of mouse OCTN2, a sodium-dependent carnitine cotransporter, in the juvenile visceral steatosis mouse. Biochem. Biophys. Res. Commun. 252:590-594 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 590-594
    • Lu, K.-M.1    Nishimori, H.2    Nakamura, Y.3    Shima, K.4    Kuwajima, K.5
  • 160
    • 0032525016 scopus 로고    scopus 로고
    • Gene-dose effect on carnitine transport activity in embryonic fibroblasts of JVS mice as a model of human carnitine transporter deficiency
    • N. Hashimoto, F. Suzuki, I. Tamai, H. Nikaido, M. Kuwajima, J.-I. Hayakawa, and A. Tsuji. Gene-dose effect on carnitine transport activity in embryonic fibroblasts of JVS mice as a model of human carnitine transporter deficiency. Biochem. Pharmac. 55:1729-1732 (1998).
    • (1998) Biochem. Pharmac. , vol.55 , pp. 1729-1732
    • Hashimoto, N.1    Suzuki, F.2    Tamai, I.3    Nikaido, H.4    Kuwajima, M.5    Hayakawa, J.-I.6    Tsuji, A.7
  • 161
    • 0001560310 scopus 로고
    • Inheritance of juvenile visceral steatosis found in C3H-H-2° mice
    • J. Hayakawa, T. Koizumi, and H. Nikaido. Inheritance of juvenile visceral steatosis found in C3H-H-2o mice. Mouse Genome 86:261 (1990).
    • (1990) Mouse Genome , vol.86 , pp. 261
    • Hayakawa, J.1    Koizumi, T.2    Nikaido, H.3
  • 162
    • 0023837255 scopus 로고
    • Infantile disease with microvesicular fatty infiltration of viscera spontaneously occurring in the C3H-H-2° strain of mouse with similarities to Reye's syndrome
    • T. Koizumi, H. Nikaido, J. Hayakawa, A. Nonomura, and T. Yoneda. Infantile disease with microvesicular fatty infiltration of viscera spontaneously occurring in the C3H-H-2° strain of mouse with similarities to Reye's syndrome. Lab. Anim. 22:83-87 (1988).
    • (1988) Lab. Anim. , vol.22 , pp. 83-87
    • Koizumi, T.1    Nikaido, H.2    Hayakawa, J.3    Nonomura, A.4    Yoneda, T.5
  • 165
    • 0032997519 scopus 로고    scopus 로고
    • Dysfunctions of the epididymis as a result of primary carnitine deficiency in juvenile visceral steatosis mice
    • K. Toshimori, M. Kuwajima, K. Yoshinaga, T. Wakayama, and K. Shima. Dysfunctions of the epididymis as a result of primary carnitine deficiency in juvenile visceral steatosis mice. FEBS Lett. 446:323-326 (1999).
    • (1999) FEBS Lett. , vol.446 , pp. 323-326
    • Toshimori, K.1    Kuwajima, M.2    Yoshinaga, K.3    Wakayama, T.4    Shima, K.5
  • 171
    • 33645220096 scopus 로고    scopus 로고
    • Transport of drugs in the kidney by the human organic cation transporter, OCT2 and its genetic variants
    • T. Fujita, T. J. Urban, M. K. Leabman, K. Fujita, and K. M. Giacomini. Transport of drugs in the kidney by the human organic cation transporter, OCT2 and its genetic variants. J. Pharm. Sci. 95:25-36 (2006).
    • (2006) J. Pharm. Sci. , vol.95 , pp. 25-36
    • Fujita, T.1    Urban, T.J.2    Leabman, M.K.3    Fujita, K.4    Giacomini, K.M.5
  • 172
    • 85017087382 scopus 로고    scopus 로고
    • Decreased function of genetic variants, Pro283Leu and Arg287Gly, in human organic cation transporter hOCT1
    • A. Takeuchi, H. Motohashi, M. Okuda, and K.-i. Inui. Decreased function of genetic variants, Pro283Leu and Arg287Gly, in human organic cation transporter hOCT1. Drug Metab. Pharmacokin. 18:409-412 (2003).
    • (2003) Drug Metab. Pharmacokin. , vol.18 , pp. 409-412
    • Takeuchi, A.1    Motohashi, H.2    Okuda, M.3    Inui, K.-I.4
  • 174
    • 0032746479 scopus 로고    scopus 로고
    • Genetic epidemiology of the carnitine transporter OCTN2 gene in a Japanese population and phenotypic characterization in Japanese pedigrees with primary systemic carnitine deficiency
    • A. Koizumi, J.-i. Nozaki, T. Ohura, T. Kayo, Y. Wada, J.-i. Nezu, R. Ohashi, I. Tamai, Y. Shoji, G. Takada, S. Kibira, T. Matsuishi, and A. Tsuji. Genetic epidemiology of the carnitine transporter OCTN2 gene in a Japanese population and phenotypic characterization in Japanese pedigrees with primary systemic carnitine deficiency. Hum. Mol. Genet. 8:2247-2254 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2247-2254
    • Koizumi, A.1    Nozaki, J.-I.2    Ohura, T.3    Kayo, T.4    Wada, Y.5    Nezu, J.-I.6    Ohashi, R.7    Tamai, I.8    Shoji, Y.9    Takada, G.10    Kibira, S.11    Matsuishi, T.12    Tsuji, A.13
  • 175
    • 0032997735 scopus 로고    scopus 로고
    • Mutations of OCTN2, an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency
    • N. L. S. Tang, V. Ganapathy, X. Wu, J. Hui, P. Seth, P. M. P. Yuen, T. F. Fok, and N. M. Hjelm. Mutations of OCTN2, an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency. Hum. Mol. Genet. 8:655-660 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 655-660
    • Tang, N.L.S.1    Ganapathy, V.2    Wu, X.3    Hui, J.4    Seth, P.5    Yuen, P.M.P.6    Fok, T.F.7    Hjelm, N.M.8
  • 176
    • 0033515017 scopus 로고    scopus 로고
    • Mutations in the organic cation/carnitine transporter OCTN2 in primary carnitine deficiency
    • Y. Wang, J. Ye, V. Ganapathy, and N. Longo. Mutations in the organic cation/carnitine transporter OCTN2 in primary carnitine deficiency. Proc. Natl. Acad. Sci. U.S.A. 96:2356-2360 (1999).
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2356-2360
    • Wang, Y.1    Ye, J.2    Ganapathy, V.3    Longo, N.4
  • 179
    • 33745448916 scopus 로고    scopus 로고
    • OCTNs: Will the real IBD5 gene please stand up?
    • M. S. Silverberg. OCTNs: Will the real IBD5 gene please stand up? World J. Gastroenterol. 12:3678-3681 (2006).
    • (2006) World J. Gastroenterol. , vol.12 , pp. 3678-3681
    • Silverberg, M.S.1
  • 183
    • 25444496731 scopus 로고    scopus 로고
    • Functional role of the 503F variant of the organic cation transporter OCTN1 in Crohn's disease
    • D. Taubert, G. Grimberg, N. Jung, A. Rubbert, and E. Schömig. Functional role of the 503F variant of the organic cation transporter OCTN1 in Crohn's disease. Gut 54:1505-1506 (2005).
    • (2005) Gut , vol.54 , pp. 1505-1506
    • Taubert, D.1    Grimberg, G.2    Jung, N.3    Rubbert, A.4    Schömig, E.5
  • 185
    • 28544444993 scopus 로고    scopus 로고
    • Current status of genetics research in inflammatory bowel disease
    • S. Vermeire and P. Rutgeerts. Current status of genetics research in inflammatory bowel disease. Genes Immun. 6:637-645 (2005).
    • (2005) Genes Immun. , vol.6 , pp. 637-645
    • Vermeire, S.1    Rutgeerts, P.2
  • 189
    • 17644411713 scopus 로고    scopus 로고
    • Amino acids critical for substrate affinity of rat organic cation transporter 1 line the substrate binding region in a model derived from the tertiary structure of lactose permease
    • C. Popp, V. Gorboulev, T. D. Müller, D. Gorbunov, N. Shatskaya, and H. Koepsell. Amino acids critical for substrate affinity of rat organic cation transporter 1 line the substrate binding region in a model derived from the tertiary structure of lactose permease. Mol. Pharmacol. 67:1600-1611 (2005).
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1600-1611
    • Popp, C.1    Gorboulev, V.2    Müller, T.D.3    Gorbunov, D.4    Shatskaya, N.5    Koepsell, H.6
  • 190
    • 17844385032 scopus 로고    scopus 로고
    • Subtype-specific affinity for corticosterone of rat organic cation transporters rOCT1 and rOCT2 depends on three amino acids within the substrate binding region
    • V. Gorboulev, N. Shatskaya, C. Volk, and H. Koepsell. Subtype-specific affinity for corticosterone of rat organic cation transporters rOCT1 and rOCT2 depends on three amino acids within the substrate binding region. Mol. Pharmacol. 67:1612-1619 (2005).
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1612-1619
    • Gorboulev, V.1    Shatskaya, N.2    Volk, C.3    Koepsell, H.4
  • 191
    • 0032723798 scopus 로고    scopus 로고
    • Selectivity of the polyspecific cation transporter rOCT1 is changed by mutation of aspartate 475 to glutamate
    • V. Gorboulev, C. Volk, P. Arndt, A. Akhoundova, and H. Koepsell. Selectivity of the polyspecific cation transporter rOCT1 is changed by mutation of aspartate 475 to glutamate. Mol. Pharmacol. 56:1254-1261 (1999).
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1254-1261
    • Gorboulev, V.1    Volk, C.2    Arndt, P.3    Akhoundova, A.4    Koepsell, H.5
  • 192
    • 27144555426 scopus 로고    scopus 로고
    • A conserved glutamate residue in transmembrane helix 10 influences substrate specificity of rabbit OCT2 (SLC22A2)
    • X. Zhang, N. V. Shirahatti, D. Mahadevan, and S. H. Wright. A conserved glutamate residue in transmembrane helix 10 influences substrate specificity of rabbit OCT2 (SLC22A2). J. Biol. Chem. 280:34813-34822 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 34813-34822
    • Zhang, X.1    Shirahatti, N.V.2    Mahadevan, D.3    Wright, S.H.4
  • 193
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • J. Abramson, I. Smirnova, V. Kasho, G. Verner, H. R. Kaback, and S. Iwata. Structure and mechanism of the lactose permease of Escherichia coli. Science 301:610-615 (2003).
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 194
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Y. Huang, M. J. Lemieux, J. Song, M. Auer, and D.-N. Wang. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301:616-620 (2003).
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.-N.5
  • 195
    • 33845922107 scopus 로고    scopus 로고
    • Cysteine accessibility in the hydrophilic cleft of the human organic cation transporter 2
    • R. M. Pelis, X. Zhang, Y. Danqprapai, and S. H. Wright. Cysteine accessibility in the hydrophilic cleft of the human organic cation transporter 2. J. Biol. Chem. 281:35272-35280 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 35272-35280
    • Pelis, R.M.1    Zhang, X.2    Danqprapai, Y.3    Wright, S.H.4
  • 197
    • 0033736393 scopus 로고    scopus 로고
    • Functional analysis of mutations in the OCTN2 transporter causing primary carnitine deficiency: Lack of genotype-phenotype correlation
    • Y. Wang, F. Taroni, B. Garavaglia, and N. Longo. Functional analysis of mutations in the OCTN2 transporter causing primary carnitine deficiency: lack of genotype-phenotype correlation. Hum. Mutat. 16:401-407 (2000).
    • (2000) Hum. Mutat. , vol.16 , pp. 401-407
    • Wang, Y.1    Taroni, F.2    Garavaglia, B.3    Longo, N.4
  • 199
    • 0033517087 scopus 로고    scopus 로고
    • Carnitine transporter OCTN2 mutations in systemic primary carnitine deficiency: A novel Arg169Gln mutation and a recurrent Arg282ter mutation associated with an unconventional splicing abnormality
    • B. Burwinkel, J. Kreuder, S. Schweitzer, M. Vorgerd, K. Gempel, K.-D. Gerbitz, and M. W. Kilimann. Carnitine transporter OCTN2 mutations in systemic primary carnitine deficiency: a novel Arg169Gln mutation and a recurrent Arg282ter mutation associated with an unconventional splicing abnormality. Biochem. Biophys. Res. Commun. 261:484-487 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 484-487
    • Burwinkel, B.1    Kreuder, J.2    Schweitzer, S.3    Vorgerd, M.4    Gempel, K.5    Gerbitz, K.-D.6    Kilimann, M.W.7
  • 201
    • 0005419068 scopus 로고    scopus 로고
    • Two novel missense mutations of the OCTN2 gene (W283R and V446F) in a patient with primary systemic carnitine deficiency
    • E. Mayatepek, J. Nezu, I. Tamai, A. Oku, M. Katsura, M. Shimane, and A. Tsuji. Two novel missense mutations of the OCTN2 gene (W283R and V446F) in a patient with primary systemic carnitine deficiency. Hum. Mutat. 15:118 (2000).
    • (2000) Hum. Mutat. , vol.15 , pp. 118
    • Mayatepek, E.1    Nezu, J.2    Tamai, I.3    Oku, A.4    Katsura, M.5    Shimane, M.6    Tsuji, A.7
  • 202
    • 0034049311 scopus 로고    scopus 로고
    • A missense mutation in the OCTN2 gene associated with residual carnitine transport activity
    • Y. Wang, M. A. Kelly, T. M. Cowan, and N. Longo. A missense mutation in the OCTN2 gene associated with residual carnitine transport activity. Hum. Mutat. 15:238-245 (2000).
    • (2000) Hum. Mutat. , vol.15 , pp. 238-245
    • Wang, Y.1    Kelly, M.A.2    Cowan, T.M.3    Longo, N.4
  • 203
    • 0034617263 scopus 로고    scopus 로고
    • Abnormal sodium stimulation of carnitine transport in primary carnitine deficiency
    • Y. Wang, T. A. Meadows, and N. Longo. Abnormal sodium stimulation of carnitine transport in primary carnitine deficiency. J. Biol. Chem. 275:20782-20786 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 20782-20786
    • Wang, Y.1    Meadows, T.A.2    Longo, N.3
  • 204
    • 0017325874 scopus 로고
    • Absorption and secretion of monoquaternary ammonium compounds by the isolated intestinal mucosa
    • K. Turnheim and F. O. Lauterbach. Absorption and secretion of monoquaternary ammonium compounds by the isolated intestinal mucosa. Biochem. Pharmac. 26:99-108 (1977).
    • (1977) Biochem. Pharmac. , vol.26 , pp. 99-108
    • Turnheim, K.1    Lauterbach, F.O.2
  • 205
    • 0018976653 scopus 로고
    • Interaction between intestinal absorption and secretion of monoquaternary ammonium compounds in guinea pigs-a concept for the absorption kinetics of organic cations
    • K. Turnheim and F. Lauterbach. Interaction between intestinal absorption and secretion of monoquaternary ammonium compounds in guinea pigs-a concept for the absorption kinetics of organic cations. J. Pharmacol. Exp. Ther. 212:418-424 (1980).
    • (1980) J. Pharmacol. Exp. Ther. , vol.212 , pp. 418-424
    • Turnheim, K.1    Lauterbach, F.2
  • 206
    • 33746887344 scopus 로고    scopus 로고
    • The transport of organic cations in the small intestine: Current knowledge and emerging concepts
    • M. K. Kim and C.-K. Shim. The transport of organic cations in the small intestine: current knowledge and emerging concepts. Arch. Pharm. Res. 29:605-616 (2006).
    • (2006) Arch. Pharm. Res. , vol.29 , pp. 605-616
    • Kim, M.K.1    Shim, C.-K.2
  • 207
    • 0026500180 scopus 로고
    • The function of Gp170, the multidrug-restistance gene product, in the brush border of rat intestinal mucosa
    • S. Hsing, Z. Gatmaitan, and I. M. Arias. The function of Gp170, the multidrug-restistance gene product, in the brush border of rat intestinal mucosa. Gastroenterology 102:879-885 (1992).
    • (1992) Gastroenterology , vol.102 , pp. 879-885
    • Hsing, S.1    Gatmaitan, Z.2    Arias, I.M.3
  • 209
    • 0034968246 scopus 로고    scopus 로고
    • Comparison of "type I" and "type II" organic cation transport by organic cation transporters and organic anion-transporting polypeptides
    • J. E. Van Montfoort, M. Müller, G. M. M. Groothuis, D. K. F. Meijer, H. Koepsell, and P. J. Meier. Comparison of "type I" and "type II" organic cation transport by organic cation transporters and organic anion-transporting polypeptides. J. Pharmacol. Exp. Ther. 298:110-115 (2001).
    • (2001) J. Pharmacol. Exp. Ther. , vol.298 , pp. 110-115
    • Van Montfoort, J.E.1    Müller, M.2    Groothuis, G.M.M.3    Meijer, D.K.F.4    Koepsell, H.5    Meier, P.J.6
  • 210
    • 0015811503 scopus 로고
    • Regulation of plasma choline by the renal tubule: Bidirectional transport of choline
    • M. Acara and B. Rennick. Regulation of plasma choline by the renal tubule: bidirectional transport of choline. Am. J. Physiol. 225:1123-1128 (1973).
    • (1973) Am. J. Physiol. , vol.225 , pp. 1123-1128
    • Acara, M.1    Rennick, B.2
  • 211
    • 0019615050 scopus 로고
    • Renal tubular transport and metabolism of organic cations by the rabbit
    • K. Besseghir, L. B. Pearce, and B. Rennick. Renal tubular transport and metabolism of organic cations by the rabbit. Am. J. Physiol. 241:F308-F314 (1981).
    • (1981) Am. J. Physiol. , vol.241
    • Besseghir, K.1    Pearce, L.B.2    Rennick, B.3
  • 212
    • 0001097160 scopus 로고
    • Renal excretion and tubular transport of organic anions and cations
    • Oxford University Press New York Oxford
    • F. Roch-Ramel, K. Besseghir, and H. Murer. Renal excretion and tubular transport of organic anions and cations. In E. E. Windhager (ed.), Handbook of Physiology, Oxford University Press, New York Oxford, 1992, pp. 2189-2262.
    • (1992) Handbook of Physiology , pp. 2189-2262
    • Roch-Ramel, F.1    Besseghir, K.2    Murer, H.3    Windhager, E.E.4
  • 213
    • 0028295299 scopus 로고
    • Specificity of transporters for 'organic anions' and 'organic cations' in the kidney
    • K. J. Ullrich. Specificity of transporters for 'organic anions' and 'organic cations' in the kidney. Biochim. Biophys. Acta 1197:45-62 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 45-62
    • Ullrich, K.J.1
  • 214
    • 0027771562 scopus 로고
    • Gender-associated differences in rat renal tubular amantadine transport and absence of stereoselective transport inhibition by quinine and quinidine in distal tubules
    • L. T. Y. Wong, M. R. Escobar, D. D. Smyth, and D. S. Sitar. Gender-associated differences in rat renal tubular amantadine transport and absence of stereoselective transport inhibition by quinine and quinidine in distal tubules. J. Pharmacol. Exp. Ther. 267:1440-1444 (1993).
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 1440-1444
    • Wong, L.T.Y.1    Escobar, M.R.2    Smyth, D.D.3    Sitar, D.S.4
  • 215
    • 0028924051 scopus 로고
    • Site-selective effect of bicarbonate on amantadine renal transport: Quinine-sensitive in proximal vs quinidine-sensitive sites in distal tubules
    • M. R. Escobar and D. S. Sitar. Site-selective effect of bicarbonate on amantadine renal transport: quinine-sensitive in proximal vs quinidine-sensitive sites in distal tubules. J. Pharmacol. Exp. Ther. 273:72-79 (1995).
    • (1995) J. Pharmacol. Exp. Ther. , vol.273 , pp. 72-79
    • Escobar, M.R.1    Sitar, D.S.2
  • 216
    • 0032942525 scopus 로고    scopus 로고
    • Molecular pharmacology of organic cation transporters in kidney
    • H. Koepsell, V. Gorboulev, and P. Arndt. Molecular pharmacology of organic cation transporters in kidney. J. Membr. Biol. 167:103-117 (1999).
    • (1999) J. Membr. Biol. , vol.167 , pp. 103-117
    • Koepsell, H.1    Gorboulev, V.2    Arndt, P.3
  • 217
    • 0037151099 scopus 로고    scopus 로고
    • The human organic cation transporter (hOCT2) recognizes the degree of substrate ionization
    • W. M. Barendt and S. H. Wright. The human organic cation transporter (hOCT2) recognizes the degree of substrate ionization. J. Biol. Chem. 277:22491-22496 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 22491-22496
    • Barendt, W.M.1    Wright, S.H.2
  • 218
    • 0035039326 scopus 로고    scopus 로고
    • Identification and characterization of human organic anion transporter 3 expressing predominantly in the kidney
    • S. H. Cha, T. Sekine, J.-I. Fukushima, Y. Kanai, Y. Kobayashi, T. Goya, and H. Endou. Identification and characterization of human organic anion transporter 3 expressing predominantly in the kidney. Mol. Pharmacol. 59:1277-1286 (2001).
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1277-1286
    • Cha, S.H.1    Sekine, T.2    Fukushima, J.-I.3    Kanai, Y.4    Kobayashi, Y.5    Goya, T.6    Endou, H.7
  • 219
    • 0026948004 scopus 로고
    • + transport
    • S. Gluck and R. Nelson. The role of the V-ATPase in renal epithelial H+ transport. J. Exp. Biol. 172:205-218 (1992).
    • (1992) J. Exp. Biol. , vol.172 , pp. 205-218
    • Gluck, S.1    Nelson, R.2
  • 220
    • 0020635466 scopus 로고
    • Cimetidine-procainamide pharmacokinetic interaction in man: Evidence of competition for tubular secretion of basic drugs
    • A. Somogyi, A. McLean, and B. Heinzow. Cimetidine-procainamide pharmacokinetic interaction in man: evidence of competition for tubular secretion of basic drugs. Eur. J. Clin. Pharmacol. 25:339-345 (1983).
    • (1983) Eur. J. Clin. Pharmacol. , vol.25 , pp. 339-345
    • Somogyi, A.1    McLean, A.2    Heinzow, B.3
  • 221
    • 0020488482 scopus 로고
    • Cimetidine reduces procainamide elimination
    • A. Somogyi and B. Heinzow. Cimetidine reduces procainamide elimination. N. Engl. J. Med. 307:1080 (1982).
    • (1982) N. Engl. J. Med. , vol.307 , pp. 1080
    • Somogyi, A.1    Heinzow, B.2
  • 222
    • 0031053808 scopus 로고    scopus 로고
    • An overview of metformin in the treatment of type 2 diabetes mellitus
    • M. B. Davidson and A. L. Peters. An overview of metformin in the treatment of type 2 diabetes mellitus. Am. J. Med. 102:99-110 (1997).
    • (1997) Am. J. Med. , vol.102 , pp. 99-110
    • Davidson, M.B.1    Peters, A.L.2
  • 223
    • 17744370731 scopus 로고    scopus 로고
    • Metformin and the polycystic ovary syndrome
    • J. E. Nestler. Metformin and the polycystic ovary syndrome. J. Clin. Endocrinol. Metab. 86:1430 (2001).
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 1430
    • Nestler, J.E.1
  • 224
    • 0028315971 scopus 로고
    • Metformin therapy in polycystic ovary syndrome reduces hyperinsulinemia, insulin resistance, hyperandrogenemia, and systolic blood pressure, while facilitating normal menses and pregnancy
    • E. M. Velazquez, S. Mendoza, T. Hamer, F. Sosa, and C. J. Glueck. Metformin therapy in polycystic ovary syndrome reduces hyperinsulinemia, insulin resistance, hyperandrogenemia, and systolic blood pressure, while facilitating normal menses and pregnancy. Metabolism 43:647-654 (1994).
    • (1994) Metabolism , vol.43 , pp. 647-654
    • Velazquez, E.M.1    Mendoza, S.2    Hamer, T.3    Sosa, F.4    Glueck, C.J.5
  • 228
    • 27744531970 scopus 로고    scopus 로고
    • Local inhibition of organic cation transporters increases extracellular serotonin in the medial hypothalamus
    • N. Feng, B. Mo, P. L. Johnson, M. Orchinik, C. A. Lowry, and K. J. Renner. Local inhibition of organic cation transporters increases extracellular serotonin in the medial hypothalamus. Brain Res. 1063:69-76 (2005).
    • (2005) Brain Res. , vol.1063 , pp. 69-76
    • Feng, N.1    Mo, B.2    Johnson, P.L.3    Orchinik, M.4    Lowry, C.A.5    Renner, K.J.6
  • 229
    • 0034672157 scopus 로고    scopus 로고
    • The human basophil: A new appreciation of its role in immune responses
    • F. H. Falcone, H. Haas, and B. F. Gibbs. The human basophil: a new appreciation of its role in immune responses. Blood 96:4028-4038 (2000).
    • (2000) Blood , vol.96 , pp. 4028-4038
    • Falcone, F.H.1    Haas, H.2    Gibbs, B.F.3
  • 230
    • 0029012725 scopus 로고
    • Murine hematopoietic progenitors are capable of both histamine synthesis and uptake
    • S. Corbel, E. Schneider, F. M. Lemoine, and M. Dy. Murine hematopoietic progenitors are capable of both histamine synthesis and uptake. Blood 86:531-539 (1995).
    • (1995) Blood , vol.86 , pp. 531-539
    • Corbel, S.1    Schneider, E.2    Lemoine, F.M.3    Dy, M.4
  • 231
    • 33646780267 scopus 로고    scopus 로고
    • Recent advances in molecular pharmacology of the histamine systems: Organic cation transporters as a histamine transporter and histamine metabolism
    • M. Ogasawara, K. Yamauchi, Y.-i. Satoh, R. Yamaji, K. Inui, J. W. Jonker, A. H. Schinkel, and K. Maeyama. Recent advances in molecular pharmacology of the histamine systems: organic cation transporters as a histamine transporter and histamine metabolism. J. Pharmacol. Sci. 101:24-30 (2006).
    • (2006) J. Pharmacol. Sci. , vol.101 , pp. 24-30
    • Ogasawara, M.1    Yamauchi, K.2    Satoh, Y.-I.3    Yamaji, R.4    Inui, K.5    Jonker, J.W.6    Schinkel, A.H.7    Maeyama, K.8
  • 232
    • 27744602975 scopus 로고    scopus 로고
    • Association between tubular toxicity of cisplatin and expression of organic cation transporter rOCT2 (Slc22a2) in the rat
    • A. Yonezawa, S. Masuda, K. Nishihara, I. Yano, T. Katsura, and K.-i. Inui. Association between tubular toxicity of cisplatin and expression of organic cation transporter rOCT2 (Slc22a2) in the rat. Biochem. Pharmacol. 70:1823-1831 (2005).
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1823-1831
    • Yonezawa, A.1    Masuda, S.2    Nishihara, K.3    Yano, I.4    Katsura, T.5    Inui, K.-I.6
  • 233
    • 33751168746 scopus 로고    scopus 로고
    • Cisplatin and oxaliplatin, but not nedaplatin, are substrates of human organic cation transporters (SLC22A1-3) and multidrug and toxin extrusion family
    • A. Yonezawa, S. Masuda, S. Yokoo, T. Katsura, and K.-i. Inui. Cisplatin and oxaliplatin, but not nedaplatin, are substrates of human organic cation transporters (SLC22A1-3 and multidrug and toxin extrusion family. J. Pharmacol. Ex. Ther. 319:879-886 (2006).
    • (2006) J. Pharmacol. Ex. Ther. , vol.319 , pp. 879-886
    • Yonezawa, A.1    Masuda, S.2    Yokoo, S.3    Katsura, T.4    Inui, K.-I.5
  • 234
    • 0036211864 scopus 로고    scopus 로고
    • Carriers involved in targeting the cytostatic bile acid-cisplatin derivatives cis-diammine-chloro-cholylglycinate-platinum(II) and cis-diammine-bisursodeoxycholate-platinum(II) toward liver cells
    • O. Briz, M. A. Serrano, N. Rebollo, B. Hagenbuch, P. J. Meier, H. Koepsell, and J. J. G. Marin. Carriers involved in targeting the cytostatic bile acid-cisplatin derivatives cis-diammine-chloro-cholylglycinate-platinum(II) and cis-diammine-bisursodeoxycholate-platinum(II) toward liver cells. Mol. Pharmacol. 61:853-860 (2002).
    • (2002) Mol. Pharmacol. , vol.61 , pp. 853-860
    • Briz, O.1    Serrano, M.A.2    Rebollo, N.3    Hagenbuch, B.4    Meier, P.J.5    Koepsell, H.6    Marin, J.J.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.