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Volumn 24, Issue 5, 2009, Pages 469-474

Genetic variations in the MCT1 (SLC16A1) gene in the Chinese population of Singapore

Author keywords

Lactate transport; MCT1; Pharmacogenetics; Single nucleotide polymorphism

Indexed keywords

ADENINE; ASPARTIC ACID; CYTIDINE; GENOMIC DNA; GLUTAMINE; GUANOSINE; ISOLEUCINE; MONOCARBOXYLATE TRANSPORTER 1; THYMIDINE; VALINE;

EID: 71449119541     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.2133/dmpk.24.469     Document Type: Article
Times cited : (16)

References (25)
  • 1
    • 0033569442 scopus 로고    scopus 로고
    • The proton-linked monocarboxylate transporter (MCT) family: Structure, function and regulation
    • Halestrap, A. P. and Price, N. T.: The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation. Biochem. J., 343: 281-299 (1999).
    • (1999) Biochem. J , vol.343 , pp. 281-299
    • Halestrap, A.P.1    Price, N.T.2
  • 2
    • 1242340302 scopus 로고    scopus 로고
    • The SLC16 gene family - from monocarboxylate transporter (MCTs) to aromatic amino acid trnasporters and beyond
    • Halestrap, A. P. and Meredith, D.: The SLC16 gene family - from monocarboxylate transporter (MCTs) to aromatic amino acid trnasporters and beyond. Eur. J. Physiol., 447: 619-628 (2004).
    • (2004) Eur. J. Physiol , vol.447 , pp. 619-628
    • Halestrap, A.P.1    Meredith, D.2
  • 3
    • 48749086146 scopus 로고    scopus 로고
    • The SLC16 monocarboxylate transporter family
    • Meredith, D. and Christian, H. C.: The SLC16 monocarboxylate transporter family. Xenobiotica, 38: 1072-1106 (2008).
    • (2008) Xenobiotica , vol.38 , pp. 1072-1106
    • Meredith, D.1    Christian, H.C.2
  • 4
    • 0043212093 scopus 로고    scopus 로고
    • Molecular features, regulation, and function of monocarboxylate transporters: Implications for drug delivery
    • Enerson, B. E. and Drewes, L. R.: Molecular features, regulation, and function of monocarboxylate transporters: implications for drug delivery. J. Pharm. Sci., 92: 1531-1544 (2003).
    • (2003) J. Pharm. Sci , vol.92 , pp. 1531-1544
    • Enerson, B.E.1    Drewes, L.R.2
  • 6
    • 0042133224 scopus 로고    scopus 로고
    • Transport mechanism for lovastatin acid in bovine kidney NBL-1 cells: Kinetic evidences imply involvement of monocarboxylate transporter 4
    • Nagasawa, K., Nagai, K., Ishimoto, A. and Fujimoto, S.: Transport mechanism for lovastatin acid in bovine kidney NBL-1 cells: kinetic evidences imply involvement of monocarboxylate transporter 4. Int. J. Pharm., 262: 63-73 (2003).
    • (2003) Int. J. Pharm , vol.262 , pp. 63-73
    • Nagasawa, K.1    Nagai, K.2    Ishimoto, A.3    Fujimoto, S.4
  • 7
    • 0027723663 scopus 로고
    • Transport mechanism of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors at the blood-brain barrier
    • Tsuji, A., Saheki, A., Tamai, I. and Terasaki, T.: Transport mechanism of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors at the blood-brain barrier. J. Pharmacol. Exp. Ther., 267: 1085-1090 (1993).
    • (1993) J. Pharmacol. Exp. Ther , vol.267 , pp. 1085-1090
    • Tsuji, A.1    Saheki, A.2    Tamai, I.3    Terasaki, T.4
  • 8
    • 0034059327 scopus 로고    scopus 로고
    • Atorvastatin transport in the Caco-2 cell model: Contributions of P-glycoprotein and the proton-monocarboxylic acid co-transporter
    • Wu, X., Whitfield, L. R. and Stewart, B. H.: Atorvastatin transport in the Caco-2 cell model: contributions of P-glycoprotein and the proton-monocarboxylic acid co-transporter. Pharm Res., 17: 209-215 (2000).
    • (2000) Pharm Res , vol.17 , pp. 209-215
    • Wu, X.1    Whitfield, L.R.2    Stewart, B.H.3
  • 9
    • 4644337779 scopus 로고    scopus 로고
    • GHB (gamma-hydroxybutyrate) carrier-mediated transport across the blood-brain barrier
    • Bhattacharya, I. and Boje, K. M.: GHB (gamma-hydroxybutyrate) carrier-mediated transport across the blood-brain barrier. J. Pharmacol. Exp. Ther., 311: 92-98 (2004).
    • (2004) J. Pharmacol. Exp. Ther , vol.311 , pp. 92-98
    • Bhattacharya, I.1    Boje, K.M.2
  • 10
    • 0029838295 scopus 로고    scopus 로고
    • Nicotinic acid transport mediated by pHdependent anion antiporter and proton cotransporter in rabbit intestinal brush-border membrane
    • Takanaga H., Maeda H., Yabuuchi H., Tamai, I., Higashida, H. and Tsuji, A.: Nicotinic acid transport mediated by pHdependent anion antiporter and proton cotransporter in rabbit intestinal brush-border membrane. J. Pharm. Pharmacol., 48: 1073-1077 (1996).
    • (1996) J. Pharm. Pharmacol , vol.48 , pp. 1073-1077
    • Takanaga, H.1    Maeda, H.2    Yabuuchi, H.3    Tamai, I.4    Higashida, H.5    Tsuji, A.6
  • 11
    • 0035662969 scopus 로고    scopus 로고
    • MCT1-mediated transport of L-lactic acid at the inner blood-retinal barrier: A possible route for delivery of monocarboxylic acid drugs to the retina
    • Hosoya, K., Kondo, T., Tomi, M., Takanaga, H., Ohtsuki, S. and Terasaki, T.: MCT1-mediated transport of L-lactic acid at the inner blood-retinal barrier: a possible route for delivery of monocarboxylic acid drugs to the retina. Pharm. Res., 18: 1669-1676 (2001).
    • (2001) Pharm. Res , vol.18 , pp. 1669-1676
    • Hosoya, K.1    Kondo, T.2    Tomi, M.3    Takanaga, H.4    Ohtsuki, S.5    Terasaki, T.6
  • 12
    • 0034663601 scopus 로고    scopus 로고
    • The low-affinity monocarboxylate transporter MCT4 is adapted to the export of lactate in highly glycolytic cells
    • Dimmer, K. S., Friedrich, B., Lang, F., Deitmer, J. W. and Broer, S.: The low-affinity monocarboxylate transporter MCT4 is adapted to the export of lactate in highly glycolytic cells. Biochem. J., 350: 219-227 (2000).
    • (2000) Biochem. J , vol.350 , pp. 219-227
    • Dimmer, K.S.1    Friedrich, B.2    Lang, F.3    Deitmer, J.W.4    Broer, S.5
  • 13
    • 85047682693 scopus 로고    scopus 로고
    • The expression of lactate transporters (MCT1 and MCT4) in heart and muscle
    • Bonen, A.: The expression of lactate transporters (MCT1 and MCT4) in heart and muscle. Eur. J. Appl. Physiol., 86: 6-11 (2001).
    • (2001) Eur. J. Appl. Physiol , vol.86 , pp. 6-11
    • Bonen, A.1
  • 14
    • 0036301412 scopus 로고    scopus 로고
    • Relative distribution of three major lactate transporters in frozen human tissues and their localization in unfixed skeletal muscle
    • Fishbein, W. N., Merezhinskaya, N. and Foellmer, J. W.: Relative distribution of three major lactate transporters in frozen human tissues and their localization in unfixed skeletal muscle. Muscle Nerve., 26: 101-112 (2002).
    • (2002) Muscle Nerve , vol.26 , pp. 101-112
    • Fishbein, W.N.1    Merezhinskaya, N.2    Foellmer, J.W.3
  • 15
    • 24944534020 scopus 로고    scopus 로고
    • Transport mechanism for L-lactic acid in human myocytes using human prototypic embryonal rhabdomyosarcoma cell line (RD cells)
    • Kobayashi, M., Fujita, I., Itagaki, S., Hirano, T. and Iseki, K.: Transport mechanism for L-lactic acid in human myocytes using human prototypic embryonal rhabdomyosarcoma cell line (RD cells). Biol. Pharm. Bull., 28: 1197-1201 (2005).
    • (2005) Biol. Pharm. Bull , vol.28 , pp. 1197-1201
    • Kobayashi, M.1    Fujita, I.2    Itagaki, S.3    Hirano, T.4    Iseki, K.5
  • 17
    • 0034525940 scopus 로고    scopus 로고
    • Characterization of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscle
    • Manning Fox, J. E., Meredith, D. and Halestrap, A. P.: Characterization of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscle. J. Physiol., 529: 285-293 (2000).
    • (2000) J. Physiol , vol.529 , pp. 285-293
    • Manning Fox, J.E.1    Meredith, D.2    Halestrap, A.P.3
  • 18
    • 0022827980 scopus 로고
    • Lactate transporter defect: A new disease of muscle
    • Fishbein, W. N.: Lactate transporter defect: a new disease of muscle. Science, 234: 1254-1256 (1986).
    • (1986) Science , vol.234 , pp. 1254-1256
    • Fishbein, W.N.1
  • 19
    • 0033970668 scopus 로고    scopus 로고
    • Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport
    • Merezhinskyaya, N., Fishbein, W. N., Davis, J. I. and Foellmer, J. W.: Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport. Muscle Nerve., 23: 90-97 (2000).
    • (2000) Muscle Nerve , vol.23 , pp. 90-97
    • Merezhinskyaya, N.1    Fishbein, W.N.2    Davis, J.I.3    Foellmer, J.W.4
  • 20
    • 0036290173 scopus 로고    scopus 로고
    • The human monocarboxylate transporter, MCT1: Genomic organization and promoter analysis
    • Cuff, M. A. and Shirazi-Beechey, S. P.: The human monocarboxylate transporter, MCT1: genomic organization and promoter analysis. Biochem. Biophys. Res. Commun., 292: 1048-1056 (2002).
    • (2002) Biochem. Biophys. Res. Commun , vol.292 , pp. 1048-1056
    • Cuff, M.A.1    Shirazi-Beechey, S.P.2
  • 21
    • 33646917296 scopus 로고    scopus 로고
    • The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by Hypoxia through a HIF-1a-dependent mechanism
    • Ullah, M. S., Davies, A. J. and Halestrap, A. P.: The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by Hypoxia through a HIF-1a-dependent mechanism. J. Biol. Chem., 281: 9030-9037 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 9030-9037
    • Ullah, M.S.1    Davies, A.J.2    Halestrap, A.P.3
  • 22
    • 0028294023 scopus 로고
    • Molecular characterization of a membrane transporter for lactate, pyruvate, and other monocarboxylates: Implications for the Cori cycle
    • Kim-Garcia, C., Goldstein, J. L., Pathak, R. K., Anderson, G. W. and Brown, M. S.: Molecular characterization of a membrane transporter for lactate, pyruvate, and other monocarboxylates: implications for the Cori cycle. Cell, 76: 865-873 (1994).
    • (1994) Cell , vol.76 , pp. 865-873
    • Kim-Garcia, C.1    Goldstein, J.L.2    Pathak, R.K.3    Anderson, G.W.4    Brown, M.S.5
  • 23
    • 0027238681 scopus 로고
    • Two different, overlapping pathways of transcription initiation are active on the TATA-less human androgen receptor promoter
    • Faber, P. W., Rooji, H. C., Schipper, H. J., Brinkmann, A. O. and Trapman, J.: Two different, overlapping pathways of transcription initiation are active on the TATA-less human androgen receptor promoter. J. Biol. Chem., 268: 9296-9301 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 9296-9301
    • Faber, P.W.1    Rooji, H.C.2    Schipper, H.J.3    Brinkmann, A.O.4    Trapman, J.5
  • 24
    • 0027980124 scopus 로고
    • Start site selection at the TATA-less carbamoyl-phosphate synthase (glutamine-hydrolyzing)/aspartate carbamoyltransferase/dihydroorotase promoter
    • Kollmar, R., Sukow, K. A., Sponagle, S. K. and Farnham, P. J.: Start site selection at the TATA-less carbamoyl-phosphate synthase (glutamine-hydrolyzing)/aspartate carbamoyltransferase/dihydroorotase promoter. J. Biol. Chem., 269: 2252-2257 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 2252-2257
    • Kollmar, R.1    Sukow, K.A.2    Sponagle, S.K.3    Farnham, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.