메뉴 건너뛰기




Volumn 159, Issue 2, 2010, Pages 419-427

Functional characterization of nonsynonymous single nucleotide polymorphisms in the human organic anion transporter 4 (hOAT4)

Author keywords

Genetic variants; Oestrone sulphate transport; Organic anion transporter; Single nucleotide polymorphisms

Indexed keywords

ESTRONE SULFATE; ORGANIC ANION TRANSPORTER 4; TETRYLAMMONIUM;

EID: 75649122519     PISSN: 00071188     EISSN: 14765381     Source Type: Journal    
DOI: 10.1111/j.1476-5381.2009.00545.x     Document Type: Article
Times cited : (31)

References (37)
  • 2
    • 22944433202 scopus 로고    scopus 로고
    • Functional consequences of single nucleotide polymorphisms in the human organic anion transporter hOAT1 (SLC22A6)
    • Bleasby K, Hall LA, Perry JL, Mohrenweiser HW, Pritchard JB (2005). Functional consequences of single nucleotide polymorphisms in the human organic anion transporter hOAT1 (SLC22A6). J Pharmacol Exp Ther 314 : 923 931.
    • (2005) J Pharmacol Exp Ther , vol.314 , pp. 923-931
    • Bleasby, K.1    Hall, L.A.2    Perry, J.L.3    Mohrenweiser, H.W.4    Pritchard, J.B.5
  • 3
    • 0000518648 scopus 로고    scopus 로고
    • Molecular cloning and characterization of multispecific organic anion transporter 4 expressed in the placenta
    • Cha SH, Sekine T, Kusuhara H, Yu E, Kim JY, Kim DK et al. (2000). Molecular cloning and characterization of multispecific organic anion transporter 4 expressed in the placenta. J Biol Chem 275 : 4507 4512.
    • (2000) J Biol Chem , vol.275 , pp. 4507-4512
    • Cha, S.H.1    Sekine, T.2    Kusuhara, H.3    Yu, E.4    Kim, J.Y.5    Kim, D.K.6
  • 4
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Web Server issue
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X et al. (2007). MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35 (Web Server issue W375 W383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5    Wang, X.6
  • 5
    • 1842732504 scopus 로고    scopus 로고
    • Human organic anion transporter 4 is a renal apical organic anion/dicarboxylate exchanger in the proximal tubules
    • Ekaratanawong S, Anzai N, Jutabha P, Miyazaki H, Noshiro R, Takeda M et al. (2004). Human organic anion transporter 4 is a renal apical organic anion/dicarboxylate exchanger in the proximal tubules. J Pharmacol Sci 94 : 297 304.
    • (2004) J Pharmacol Sci , vol.94 , pp. 297-304
    • Ekaratanawong, S.1    Anzai, N.2    Jutabha, P.3    Miyazaki, H.4    Noshiro, R.5    Takeda, M.6
  • 6
    • 57649131249 scopus 로고    scopus 로고
    • Implications of the alternating access model for organic anion transporter kinetics
    • Eraly SA (2008). Implications of the alternating access model for organic anion transporter kinetics. J Membr Biol 226 : 35 42.
    • (2008) J Membr Biol , vol.226 , pp. 35-42
    • Eraly, S.A.1
  • 8
    • 0035826582 scopus 로고    scopus 로고
    • Arginine 454 and lysine 370 are essential for the anion specificity of the organic anion transporter, rOAT3
    • Feng B, Dresser MJ, Shu Y, Johns SJ, Giacomini KM (2001). Arginine 454 and lysine 370 are essential for the anion specificity of the organic anion transporter, rOAT3. Biochemistry 40 : 5511 5520.
    • (2001) Biochemistry , vol.40 , pp. 5511-5520
    • Feng, B.1    Dresser, M.J.2    Shu, Y.3    Johns, S.J.4    Giacomini, K.M.5
  • 9
    • 0037118701 scopus 로고    scopus 로고
    • Role of aromatic transmembrane residues of the organic anion transporter, rOAT3, in substrate recognition
    • Feng B, Shu Y, Giacomini KM (2002). Role of aromatic transmembrane residues of the organic anion transporter, rOAT3, in substrate recognition. Biochemistry 41 : 8941 8947.
    • (2002) Biochemistry , vol.41 , pp. 8941-8947
    • Feng, B.1    Shu, Y.2    Giacomini, K.M.3
  • 10
    • 2342597868 scopus 로고    scopus 로고
    • Apical expression or expression in a non polarized cell of hOAT1 inverses regulation by epidermal growth factor (EGF) as compared to basolateral hOAT1
    • Hesse D, Sauvant C, Holzinger H, Gekle M (2004). Apical expression or expression in a non polarized cell of hOAT1 inverses regulation by epidermal growth factor (EGF) as compared to basolateral hOAT1. Cell Physiol Biochem 14 : 177 186.
    • (2004) Cell Physiol Biochem , vol.14 , pp. 177-186
    • Hesse, D.1    Sauvant, C.2    Holzinger, H.3    Gekle, M.4
  • 11
    • 59149084250 scopus 로고    scopus 로고
    • COX-2 inhibition attenuates endotoxin-induced downregulation of organic anion transporters in the rat renal cortex
    • Hocherl K, Schmidt C, Bucher M (2009). COX-2 inhibition attenuates endotoxin-induced downregulation of organic anion transporters in the rat renal cortex. Kidney Int 75 : 373 380.
    • (2009) Kidney Int , vol.75 , pp. 373-380
    • Hocherl, K.1    Schmidt, C.2    Bucher, M.3
  • 12
    • 3843123206 scopus 로고    scopus 로고
    • Critical amino acid residues in transmembrane domain 1 of the human organic anion transporter hOAT1
    • Hong M, Zhou F, You G (2004). Critical amino acid residues in transmembrane domain 1 of the human organic anion transporter hOAT1. J Biol Chem 279 : 31478 31482.
    • (2004) J Biol Chem , vol.279 , pp. 31478-31482
    • Hong, M.1    Zhou, F.2    You, G.3
  • 13
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN (2003). Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301 : 616 620.
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 14
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24 : 946 950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 16
    • 44949262069 scopus 로고    scopus 로고
    • Identification and characterization of single nucleotide polymorphisms of SLC22A11 (hOAT4) in Korean women osteoporosis patients
    • Lee WK, Kwak JO, Hwang JS, Suh CK, Cha SH (2008). Identification and characterization of single nucleotide polymorphisms of SLC22A11 (hOAT4) in Korean women osteoporosis patients. Mol Cells 25 : 265 271.
    • (2008) Mol Cells , vol.25 , pp. 265-271
    • Lee, W.K.1    Kwak, J.O.2    Hwang, J.S.3    Suh, C.K.4    Cha, S.H.5
  • 17
    • 0038209381 scopus 로고    scopus 로고
    • Polymorphisms of OATP-C (SLC21A6) and OAT3 (SLC22A8) genes: Consequences for pravastatin pharmacokinetics
    • URL. [accessed on 12 November 2009 Y.*Ieiri I.*Suzuki H.*Kimura M.*Kawabata K.*Hirota T.*et al.
    • Lopez R, Lloyd A (1997). ClustalW WWW Service at the European Bioinformatics Institute. URL http://www.ebi.ac.uk/Tools/clustalw2/ [accessed on 12 November 2009 Y, Ieiri I, Suzuki H, Kimura M, Kawabata K, Hirota T et al. (2003). Polymorphisms of OATP-C (SLC21A6) and OAT3 (SLC22A8) genes: consequences for pravastatin pharmacokinetics. Clin Pharmacol Ther 73 : 554 565.
    • (1997) Clin Pharmacol Ther , vol.73 , pp. 554-565
    • Lopez, R.1    Lloyd, A.2
  • 18
    • 46149091944 scopus 로고    scopus 로고
    • Analysis of regulatory polymorphisms in organic ion transporter genes (SLC22A) in the kidney
    • Ogasawara K, Terada T, Motohashi H, Asaka J, Aoki M, Katsura T et al. (2008). Analysis of regulatory polymorphisms in organic ion transporter genes (SLC22A) in the kidney. J Hum Genet 53 : 607 614.
    • (2008) J Hum Genet , vol.53 , pp. 607-614
    • Ogasawara, K.1    Terada, T.2    Motohashi, H.3    Asaka, J.4    Aoki, M.5    Katsura, T.6
  • 19
    • 33846010171 scopus 로고    scopus 로고
    • A three-dimensional model of human organic anion transporter 1: Aromatic amino acids required for substrate transport
    • Perry JL, Dembla-Rajpal N, Hall LA, Pritchard JB (2006). A three-dimensional model of human organic anion transporter 1: aromatic amino acids required for substrate transport. J Biol Chem 281 : 38071 38079.
    • (2006) J Biol Chem , vol.281 , pp. 38071-38079
    • Perry, J.L.1    Dembla-Rajpal, N.2    Hall, L.A.3    Pritchard, J.B.4
  • 20
    • 0029361476 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A (1995). Comparative protein modeling by satisfaction of spatial restraints. Mol Med Today 1 : 270 277.
    • (1995) Mol Med Today , vol.1 , pp. 270-277
    • Sali, A.1
  • 22
    • 0345530115 scopus 로고    scopus 로고
    • Short-term regulation of basolateral organic anion uptake in proximal tubular opossum kidney cells: Prostaglandin E2 acts via receptor-mediated activation of protein kinase A
    • Sauvant C, Holzinger H, Gekle M (2003). Short-term regulation of basolateral organic anion uptake in proximal tubular opossum kidney cells: prostaglandin E2 acts via receptor-mediated activation of protein kinase A. J Am Soc Nephrol 14 : 3017 3026.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 3017-3026
    • Sauvant, C.1    Holzinger, H.2    Gekle, M.3
  • 23
    • 48749084010 scopus 로고    scopus 로고
    • Physiology, structure, and regulation of the cloned organic anion transporters
    • Srimaroeng C, Perry JL, Pritchard JB (2008). Physiology, structure, and regulation of the cloned organic anion transporters. Xenobiotica 38 : 889 935.
    • (2008) Xenobiotica , vol.38 , pp. 889-935
    • Srimaroeng, C.1    Perry, J.L.2    Pritchard, J.B.3
  • 24
    • 2442479788 scopus 로고    scopus 로고
    • Role of glycosylation in the organic anion transporter OAT1
    • DOI 10.1074/jbc.M400197200
    • Tanaka K, Xu W, Zhou F, You G (2004). Role of glycosylation in the organic anion transporter OAT1. J Biol Chem 279 : 14961 14966. (Pubitemid 38618888)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 14961-14966
    • Tanaka, K.1    Xu, W.2    Zhou, F.3    You, G.4
  • 25
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 : 4673 4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 28
    • 33747068033 scopus 로고    scopus 로고
    • Torsemide renal clearance and genetic variation in luminal and basolateral organic anion transporters
    • Vormfelde SV, Schirmer M, Hagos Y, Toliat MR, Engelhardt S, Meineke I et al. (2006). Torsemide renal clearance and genetic variation in luminal and basolateral organic anion transporters. Br J Clin Pharmacol 62 : 323 335.
    • (2006) Br J Clin Pharmacol , vol.62 , pp. 323-335
    • Vormfelde, S.V.1    Schirmer, M.2    Hagos, Y.3    Toliat, M.R.4    Engelhardt, S.5    Meineke, I.6
  • 29
    • 31644434086 scopus 로고    scopus 로고
    • Analyses of coding region polymorphisms in apical and basolateral human organic anion transporter (OAT) genes [OAT1 (NKT), OAT2, OAT3, OAT4, URAT (RST)
    • Xu G, Bhatnagar V, Wen G, Hamilton BA, Eraly SA, Nigam SK (2005). Analyses of coding region polymorphisms in apical and basolateral human organic anion transporter (OAT) genes [OAT1 (NKT), OAT2, OAT3, OAT4, URAT (RST) Kidney Int 68 : 1491 1499.
    • (2005) Kidney Int , vol.68 , pp. 1491-1499
    • Xu, G.1    Bhatnagar, V.2    Wen, G.3    Hamilton, B.A.4    Eraly, S.A.5    Nigam, S.K.6
  • 30
    • 0036842911 scopus 로고    scopus 로고
    • Structure, function, and regulation of renal organic anion transporters
    • You G (2002). Structure, function, and regulation of renal organic anion transporters. Med Res Rev 22 : 602 616.
    • (2002) Med Res Rev , vol.22 , pp. 602-616
    • You, G.1
  • 31
    • 0034616345 scopus 로고    scopus 로고
    • Regulation of mOAT-mediated organic anion transport by okadaic acid and protein kinase C in LLC-PK(1) cells
    • You G, Kuze K, Kohanski RA, Amsler K, Henderson S (2000). Regulation of mOAT-mediated organic anion transport by okadaic acid and protein kinase C in LLC-PK(1) cells. J Biol Chem 275 : 10278 10284.
    • (2000) J Biol Chem , vol.275 , pp. 10278-10284
    • You, G.1    Kuze, K.2    Kohanski, R.A.3    Amsler, K.4    Henderson, S.5
  • 32
    • 57749119509 scopus 로고    scopus 로고
    • Organic anion transporter OAT1 undergoes constitutive and protein kinase C-regulated trafficking through a dynamin- and clathrin-dependent pathway
    • Zhang Q, Hong M, Duan P, Pan Z, Ma J, You G (2008). Organic anion transporter OAT1 undergoes constitutive and protein kinase C-regulated trafficking through a dynamin- and clathrin-dependent pathway. J Biol Chem 283 : 32570 32579.
    • (2008) J Biol Chem , vol.283 , pp. 32570-32579
    • Zhang, Q.1    Hong, M.2    Duan, P.3    Pan, Z.4    Ma, J.5    You, G.6
  • 33
    • 33845446759 scopus 로고    scopus 로고
    • Molecular insights into the structure-function relationship of organic anion transporters OATs
    • Zhou F, You G (2007). Molecular insights into the structure-function relationship of organic anion transporters OATs. Pharm Res 24 : 28 36.
    • (2007) Pharm Res , vol.24 , pp. 28-36
    • Zhou, F.1    You, G.2
  • 34
    • 9444256962 scopus 로고    scopus 로고
    • Mutational analysis of histidine residues in human organic anion transporter 4 (hOAT4)
    • DOI 10.1042/BJ20040751
    • Zhou F, Pan Z, Ma J, You G (2004a). Mutational analysis of histidine residues in human organic anion transporter 4 (hOAT4). Biochem J 384 (Pt 1 87 92. (Pubitemid 39564164)
    • (2004) Biochemical Journal , vol.384 , Issue.1 , pp. 87-92
    • Zhou, F.1    Pan, Z.2    Ma, J.3    You, G.4
  • 35
    • 2142772675 scopus 로고    scopus 로고
    • The role of glycine residues in the function of human organic anion transporter 4
    • DOI 10.1124/mol.65.5.1141
    • Zhou F, Tanaka K, Pan Z, Ma J, You G (2004b). The role of glycine residues in the function of human organic anion transporter 4. Mol Pharmacol 65 : 1141 1147. (Pubitemid 38543485)
    • (2004) Molecular Pharmacology , vol.65 , Issue.5 , pp. 1141-1147
    • Zhou, F.1    Tanaka, K.2    Pan, Z.3    Ma, J.4    You, G.5
  • 36
    • 14944353459 scopus 로고    scopus 로고
    • The role of N-linked glycosylation in protein folding, membrane targeting, and substrate binding of human organic anion transporter hOAT4
    • Zhou F, Xu W, Hong M, Pan Z, Sinko PJ, Ma J et al. (2005). The role of N-linked glycosylation in protein folding, membrane targeting, and substrate binding of human organic anion transporter hOAT4. Mol Pharmacol 67 : 868 876.
    • (2005) Mol Pharmacol , vol.67 , pp. 868-876
    • Zhou, F.1    Xu, W.2    Hong, M.3    Pan, Z.4    Sinko, P.J.5    Ma, J.6
  • 37
    • 34547134693 scopus 로고    scopus 로고
    • Regulation of human organic anion transporter 4 by progesterone and protein kinase C in human placental BeWo cells
    • Zhou F, Hong M, You G (2007). Regulation of human organic anion transporter 4 by progesterone and protein kinase C in human placental BeWo cells. Am J Physiol Endocrinol Metab 293 : E57 E61.
    • (2007) Am J Physiol Endocrinol Metab , vol.293
    • Zhou, F.1    Hong, M.2    You, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.