Thiamin function, metabolism, uptake, and transport

Biochemistry

Volumn 53, Issue 5, 2014, Pages 821-835

  Manzetti, Sergio ^a,b   Zhang, Jin ^a,c   Van Der Spoel, David ^a  

^a UPPSALA UNIVERSITY   (Sweden)

^b Fjordforsk AS   (Norway)

^c ZHEJIANG UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE; ALKALINE PHOSPHATASE; ANIMALS; BIOLOGICAL TRANSPORT; BRAIN; ENERGY METABOLISM; HUMANS; IMMUNE SYSTEM; MEMBRANE TRANSPORT PROTEINS; ORGAN SPECIFICITY; THIAMINE; THIAMINE DEFICIENCY;

EID: 84894211744     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401618y     Document Type: Review

References (176)

1. Said, H. M. (2011) Intestinal absorption of water-soluble vitamins in health and disease Biochem. J. 437, 357-372
2. Gigliobianco, T., Gangolf, M., Lakaye, B., Pirson, B., von Ballmoos, C., Wins, P., and Bettendorff, L. (2013) An alternative role of FoF1-ATP synthase in Escherichia coli: Synthesis of thiamine triphosphate Sci. Rep. 3
3. Bettendorff, L. and Wins, P. (2013) Biochemistry of Thiamine and Thiamine Phosphate Compounds. In Encyclopedia of Biological Chemistry (William, J. L. and Lane, M. D., Eds.) pp 202-209, Academic Press, Waltham, MA.
4. Belanger, F. C., Leustek, T., Chu, B., and Kriz, A. L. (1995) Evidence for the thiamine biosynthetic pathway in higher-plant plastids and its developmental regulation Plant Mol. Biol. 29, 809-821
5. Goyer, A. (2010) Thiamine in plants: Aspects of its metabolism and functions Phytochemistry 71, 1615-1624
6. Bender, D. A. (1999) Optimum nutrition: Thiamin, biotin and pantothenate Proc. Nutr. Soc. 58, 427-434
7. Franken, J. and Stapert, F. (1954) Restoration of pyruvate breakdown in pigeion muscle homogenates impaired by thiamine deficiency Biochim. Biophys. Acta 14, 293-294
8. Asakawa, T., Wada, H., and Yamano, T. (1968) Enzymatic conversion of phenylpyruvate to phenylacetate Biochim. Biophys. Acta 170, 375-391
9. Spector, M. P. (2009) Metabolism, Central (Intermediary). In Encyclopedia of Microbiology (Moselio, S., Ed.) 3rd ed., pp 242-264, Academic Press, Oxford, U.K.
10. Rindi, G. and Laforenza, U. (2000) Thiamine intestinal transport and related issues: Recent aspects Proc. Soc. Exp. Biol. Med. 224, 246-255
11. Furdui, C. and Ragsdale, S. W. (2002) The roles of coenzyme A in the pyruvate:ferredoxin oxidoreductase reaction mechanism: Rate enhancement of electron transfer from a radical intermediate to an iron-sulfur cluster Biochemistry 41, 9921-9937
12. Tittmann, K. (2009) Reaction mechanisms of thiamin diphosphate enzymes: Redox reactions FEBS J. 276, 2454-2468
13. Schowen, R. L. (1998) Thiamin-dependent enzymes Comprehensive Biological Catalysis 2, 217-266
14. Chabrière, E., Charon, M. H., Volbeda, A., Pieulle, L., Hatchikian, E. C., and Fontecilla-Camps, J. C. (1999) Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate Nat. Struct. Mol. Biol. 6, 182-190
15. Sedewitz, B., Schleifer, K. H., and Götz, F. (1984) Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum J. Bacteriol. 160, 273-278
16. Koland, J. G., Miller, M. J., and Gennis, R. B. (1984) Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase Biochemistry 23, 445-453
17. Li, T., Huo, L., Pulley, C., and Liu, A. (2012) Decarboxylation mechanisms in biological system Bioorg. Chem. 43, 2-14
18. Bettendorff, L., Kolb, H.-A., and Schoffeniels, E. (1993) Thiamine triphosphate activates an anion channel of large unit conductance in neuroblastoma cells J. Membr. Biol. 136, 281-288
19. Gangolf, M., Czerniecki, J., Radermecker, M., Detry, O., Nisolle, M., Jouan, C., Martin, D., Chantraine, F., Lakaye, B., and Wins, P. (2010) Thiamine status in humans and content of phosphorylated thiamine derivatives in biopsies and cultured cells PLoS One 5, e13616
20. Gibson, G. E. and Blass, J. P. (2007) Thiamine-dependent processes and treatment strategies in neurodegeneration Antioxid. Redox Signaling 9, 1605-1620
21. Butterworth, R. F. and Besnard, A.-M. (1990) Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease Metab. Brain Dis. 5, 179-184
22. Perri, V., Sacchi, O., and Casella, C. (1970) Action of oxythiamine and pyrithiamine on the isolated rat superior cervical ganglion Exp. Physiol. 55, 36-43
23. Cooper, J. R. and Pincus, J. H. (1979) The role of thiamine in nervous tissue Neurochem. Res. 4, 223-239
24. Armett, C. J. and Cooper, J. R. (1965) The role of thiamine in nervous tissue: Effect of antimetabolites of the vitamin on conduction in mammalian nonmyelinated nerve fibers J. Pharmacol. Exp. Ther. 148, 137-143
25. Barchi, R. L. and Braun, P. E. (1972) A Membrane-associated Thiamine Triphosphatase from Rat Brain J. Biol. Chem. 247, 7668-7673
26. Tallaksen, C. and Taubøll, E. (2000) Excitatory effect of thiamin on CA1 pyramidal neurones in rat hippocampal slices in vitro Eur. J. Neurol. 7, 693-698
27. Nghiem, H.-O., Bettendorff, L., and Changeux, J.-P. (2000) Specific phosphorylation of Torpedo 43K rapsyn by endogenous kinase(s) with thiamine triphosphate as the phosphate donor FASEB J. 14, 543-554
28. Eder, L., Hirt, L., and Dunant, Y. (1976) Possible involvement of thiamine in acetylcholine release Nature 264, 186-188
29. Mulholland, P. J. (2006) Susceptibility of the cerebellum to thiamine deficiency Cerebellum 5, 55-63
30. Baî, A. (2008) Metabolic and structural role of thiamine in nervous tissues Cell. Mol. Neurobiol. 28, 923-931
31. Wang, Z.-B., Gan, Q., Rupert, R. L., Zeng, Y.-M., and Song, X.-J. (2005) Thiamine, pyridoxine, cyanocobalamin and their combination inhibit thermal, but not mechanical hyperalgesia in rats with primary sensory neuron injury Pain 114, 266-277
32. Song, X.-S., Huang, Z.-J., and Song, X.-J. (2009) Thiamine suppresses thermal hyperalgesia, inhibits hyperexcitability, and lessens alterations of sodium currents in injured, dorsal root ganglion neurons in rats Anesthesiology 110, 387-400
33. França, D. S., Souza, A. L., Almeida, K. R., Dolabella, S. l. S., Martinelli, C., and Coelho, M. M. (2001) B vitamins induce an antinociceptive effect in the acetic acid and formaldehyde models of nociception in mice Eur. J. Pharmacol. 421, 157-164
34. Huang, H.-M., Chen, H.-L., and Gibson, G. E. (2010) Thiamine and oxidants interact to modify cellular calcium stores Neurochem. Res. 35, 2107-2116
35. Jhala, S. S. and Hazell, A. S. (2011) Modeling neurodegenerative disease pathophysiology in thiamine deficiency: Consequences of impaired oxidative metabolism Neurochem. Int. 58, 248-260
36. Gangolf, M., Wins, P., Thiry, M., El Moualij, B., and Bettendorff, L. (2010) Thiamine triphosphate synthesis in rat brain occurs in mitochondria and is coupled to the respiratory chain J. Biol. Chem. 285, 583-594
37. Brown, R. D. (1990) The proton channel blocking agent omeprazole is an inhibitor of the thiamin shuttle J. Theor. Biol. 143, 565-573
38. Bettendorff, L., Peeters, M., Wins, P., and Schoffeniels, E. (1993) Metabolism of thiamine triphosphate in rat brain: Correlation with chloride permeability J. Neurochem. 60, 423-434
39. Losa, R., Sierra, M. I., Fernández, A., Blanco, D., and Buesa, J. M. (2005) Determination of thiamine and its phosphorylated forms in human plasma, erythrocytes and urine by HPLC and fluorescence detection: A preliminary study on cancer patients J. Pharm. Biomed. Anal. 37, 1025-1029
40. Nakagawasai, O. (2005) Behavioral and neurochemical alterations following thiamine deficiency in rodents: Relationship to functions of cholinergic neurons Yakugaku Zasshi 125, 549-554
41. Yusa, T. (1962) Studies on thiamine triphosphate II. Thiamin triphosphate as phosphate donor Plant Cell Physiol. 3, 95-103
42. Tallaksen, C. M. E., Bøhmer, T., Karlsen, J., and Bell, H. (1997) Determination of thiamin and its phosphate esters in human blood, plasma, and urine. In Methods in Enzymology (Donald, B. and McCormick, J. W. S. C. W., Eds.) pp 67-74, Academic Press, San Diego.
43. 2/halide system: Studies on the reversible nature of the inhibition and mechanism of protection of migratory responsiveness by ascorbate, levamisole, thiamine and cysteine Int. J. Immunopharmacol. 5, 377-389
44. Anderson, R. (1982) Enhancement of neutrophil motility by ascorbate, levamisole and thiamine by an anti-oxidant mechanism Int. J. Immunopharmacol. 4, 282
45. Katz, F. E., Parkar, M., Stanley, K., Murray, L. J., Clark, E. A., and Greaves, M. F. (1985) Chromosome mapping of cell membrane antigens expressed on activated B cells Eur. J. Immunol. 15, 103-106
46. Wegner, C. D., Gundel, R. H., Reilly, P., Haynes, N., Letts, L. G., and Rothlein, R. (1990) Intercellular adhesion molecule-1 (ICAM-1) in the pathogenesis of asthma Science 247, 456-459
47. Ottinger, C. A., Honeyfield, D. C., Densmore, C. L., and Iwanowicz, L. R. (2012) Impact of Thiamine Deficiency on T-cell Dependent and T-cell Independent Antibody Production in Lake Trout Journal of Aquatic Animal Health 24, 258-273
48. Ke, Z.-J., Calingasan, N. Y., DeGiorgio, L. A., Volpe, B. T., and Gibson, G. E. (2005) CD40-CD40L interactions promote neuronal death in a model of neurodegeneration due to mild impairment of oxidative metabolism Neurochem. Int. 47, 204-215
49. Zimitat, C. and Nixon, P. F. (2001) Glucose induced IEG expression in the thiamin-deficient rat brain Brain Res. 892, 218-227
50. Molina, P. E., Fan, J., Lang, C. H., Gelatto, M., and Abumrad, N. N. (1994) Thiamine deficiency regulates growth hormone and insulin-like growth factor-I system Clin. Nutr. 13 (Suppl. 1) 18-19
51. Yadav, U., Kalariya, N. M., Srivastava, S. K., and Ramana, K. V. (2010) Protective role of benfotiamine, a fat-soluble vitamin B1 analogue, in lipopolysaccharide-induced cytotoxic signals in murine macrophages Free Radical Biol. Med. 48, 1423-1434
52. Umezawa, K. (2006) Inhibition of tumor growth by NF-κB inhibitors Cancer Sci. 97, 990-995
53. Shoeb, M. and Ramana, K. V. (2012) Anti-inflammatory effects of benfotiamine are mediated through the regulation of the arachidonic acid pathway in macrophages Free Radical Biol. Med. 52, 182-190
54. Greenblatt, M., Bennett, W., Hollstein, M., and Harris, C. (1994) Mutations in the p53 tumor suppressor gene: Clues to cancer etiology and molecular pathogenesis Cancer Res. 54, 4855-4878
55. Luong, K. V. and Nguyen, L. T. (2013) The Beneficial Role of Thiamine in Parkinson Disease CNS Neurosci. Ther. 19, 461-468
56. + modulates p53 DNA binding specificity and function Mol. Cell. Biol. 24, 9958-9967
57. Ke, Z.-J., Bowen, W. M., and Gibson, G. E. (2006) Peripheral inflammatory mechanisms modulate microglial activation in response to mild impairment of oxidative metabolism Neurochem. Int. 49, 548-556
58. Ahn, I.-P., Kim, S., and Lee, Y.-H. (2005) Vitamin B1 functions as an activator of plant disease resistance Plant Physiol. 138, 1505-1515
59. Bowler, C. and Fluhr, R. (2000) The role of calcium and activated oxygens as signals for controlling cross-tolerance Trends Plant Sci. 5, 241-246
60. Breinig, F., Heintel, T., Schumacher, A., Meyerhans, A., and Schmitt, M. J. (2003) Specific activation of CMV-primed human T lymphocytes by cytomegalovirus pp65 expressed in fission yeast FEMS Immunol. Med. Microbiol. 38, 231-239
61. Brunette, M. G., Delvin, E., Hazel, B., and Scriver, C. R. (1972) Thiamine-responsive lactic acidosis in a patient with deficient low-Km pyruvate carboxylase activity in liver Pediatrics 50, 702-711
62. Bettendorff, L., Hennuy, B., Wins, P., and Schoffeniels, E. (1993) Thiamin and derivatives as modulators of rat brain chloride channels Neuroscience 52, 1009-1017
63. Mair, R. G., Otto, T. A., Knoth, R. L., Rabchenuk, S. A., and Langlais, P. J. (1991) Analysis of aversively conditioned learning and memory in rats recovered from pyrithiamine-induced thiamine deficiency Behav. Neurosci. 105, 351
64. Langlais, P. J. and Savage, L. M. (1995) Thiamine deficiency in rats produces cognitive and memory deficits on spatial tasks that correlate with tissue loss in diencephalon, cortex and white matter Behav. Brain Res. 68, 75-89
65. Onodera, K., Ogura, Y., and Kisara, K. (1981) Characteristics of muricide induced by thiamine deficiency and its suppression by antidepressants or intraventricular serotonin Physiol. Behav. 27, 847-853
66. Onodera, K., Saito, T., and Itoh, M. (1991) Changes in blood pressure and heart rate following dietary-induced thiamine deficiency in muricide rats Yakubutsu, Seishin, Kodo 11, 319
67. Nakagawasai, O., Tadano, T., Hozumi, S., Tan-No, K., Niijima, F., and Kisara, K. (2000) Immunohistochemical estimation of brain choline acetyltransferase and somatostatin related to the impairment of avoidance learning induced by thiamine deficiency Brain Res. Bull. 52, 189-196
68. Hills, J. I., Golub, M. S., Bettendorff, L., and Keen, C. L. (2012) The effect of thiamin tetrahydrofurfuryl disulfide on behavior of juvenile DBA/2J mice Neurotoxicol. Teratol. 34, 242-252
69. Butterworth, R. F. (1982) Neurotransmitter function in thiamine-deficiency encephalopathy Neurochem. Int. 4, 449-464
70. Gold, M., Hauser, R. A., and Chen, M. F. (1998) Plasma thiamine deficiency associated with Alzheimer's disease but not Parkinson's disease Metab. Brain Dis. 13, 43-53
71. Rindi, G., Patrini, C., Comincioli, V., and Reggiani, C. (1980) Thiamine content and turnover rates of some rat nervous regions, using labeled thiamine as a tracer Brain Res. 181, 369-380
72. Hazell, A. S. (2009) Astrocytes are a major target in thiamine deficiency and Wernicke's encephalopathy Neurochem. Int. 55, 129-135
73. Jordan, L. R., Zelaya, F. O., Rose, S. E., Bower, A. J., Galloway, G., Wholohan, T., and Nixon, P. F. (1998) Changes in the hippocampus induced by glucose in thiamin deficient rats detected by MRI Brain Res. 791, 347-351
74. Zhao, N., Zhong, C., Wang, Y., Zhao, Y., Gong, N., Zhou, G., Xu, T., and Hong, Z. (2008) Impaired hippocampal neurogenesis is involved in cognitive dysfunction induced by thiamine deficiency at early pre-pathological lesion stage Neurobiol. Dis. 29, 176-185
75. Gibson, G. E. and Zhang, H. (2002) Interactions of oxidative stress with thiamine homeostasis promote neurodegeneration Neurochem. Int. 40, 493-504
76. Carpenter, K. J. (2012) The discovery of thiamin Ann. Nutr. Metab. 61, 219-223
77. Balk, L., Hagerroth, P. A., Akerman, G., Hanson, M., Tjarnlund, U., Hansson, T., Hallgrimsson, G. T., Zebuhr, Y., Broman, D., Morner, T., and Sundberg, H. (2009) Wild birds of declining European species are dying from a thiamine deficiency syndrome Proc. Natl. Acad. Sci. U.S.A. 106, 12001-12006
78. Swank, R. L. (1940) Avian thiamin deficiency: A correlation of pathology and clinical behavior J. Exp. Med. 71, 683-702
79. Riley, S. C., Rinchard, J., Honeyfield, D. C., Evans, A. N., and Begnoche, L. (2011) Increasing Thiamine Concentrations in Lake Trout Eggs from Lakes Huron and Michigan Coincide with Low Alewife Abundance North American Journal of Fisheries Management 31, 1052-1064
80. Rocke, T. E. and Barker, I. (2010) Proposed link between paralytic syndrome and thiamine deficiency in Swedish gulls not substantiated Proc. Natl. Acad. Sci. U.S.A. 107, E14
81. Balk, L., Hagerroth, P. A., Akerman, G., Hanson, M., Tjarnlund, U., Hansson, T., Hallgrimsson, G. T., Zebuhr, Y., Broman, D., Morner, T., and Sundberg, H. (2010) Reply to Rocke and Barker: The question is not whether birds are affected by thiamine deficiency or botulism, it is about the order of events Proc. Natl. Acad. Sci. U.S.A. 107, E37
82. Sonne, C., Alstrup, A. K. O., and Therkildsen, O. R. (2012) A review of the factors causing paralysis in wild birds: Implications for the paralytic syndrome observed in the Baltic Sea Sci. Total Environ. 416, 32-39
83. Tillitt, D. E., Kraft, C. E., Honeyfield, D. C., and Fitzsimons, J. D. (2012) Thiamine deficiency: A viable hypothesis for paralytic syndrome in Baltic birds. Commentary on Sonne et al., 2012. A review of the factors causing paralysis in wild birds: Implications for the paralytic syndrome observed in the Baltic Sea. Science of the Total Environment 416:32-39 Sci. Total Environ. 433, 561-562
84. Greenwood, J., Love, E., and Pratt, O. (1982) Kinetics of thiamine transport across the blood-brain barrier in the rat J. Physiol. 327, 95-103
85. Bettendorff, L. (1995) Thiamine homeostasis in neuroblastoma cells Neurochem. Int. 26, 295-302
86. Matsuda, T. and Iwata, H. (1987) Decrease of high affinity ouabain binding in rat cerebellum and hypothalamus by thiamin deficiency Brain Res. 437, 375-378
87. Casirola, D., Patrini, C., Ferrari, G., and Rindi, G. (1990) Thiamin transport by human erythrocytes and ghosts J. Membr. Biol. 118, 11-18
88. Lemos, C., Faria, A., Meireles, M., Martel, F., Monteiro, R., and Calhau, C. (2012) Thiamine is a substrate of organic cation transporters in Caco-2 cells Eur. J. Pharmacol. 682, 37-42
89. Ferrari, G., Rindi, G., and D'Andrea, G. (1978) The action of inorganic phosphate on thiamin transport by rat everted jejunal sacs Pfluegers Arch. 376, 47-53
90. +) by the JAR Human Placental Choriocarcinoma Cell Line: Comparison with 5-Hydroxytryptamine Placenta 24, 361-369
91. + in human intestinal epithelial (Caco-2) cells Naunyn-Schmiedeberg's Arch. Pharmacol. 361, 505-513
92. Martel, F., Gründemann, D., Calhau, C., and Schömig, E. (2001) Apical uptake of organic cations by human intestinal Caco-2 cells: Putative involvement of ASF transporters Naunyn-Schmiedeberg's Arch. Pharmacol. 363, 40-49
93. +) by human intestinal Caco-2 cells is regulated by phosphorylation/dephosphorylation mechanisms Biochem. Pharmacol. 63, 1565-1573
94. Tallaksen, C., Sande, A., Bøhmer, T., Bell, H., and Karlsen, J. (1993) Kinetics of thiamin and thiamin phosphate esters in human blood, plasma and urine after 50 mg intravenously or orally Eur. J. Clin. Pharmacol. 44, 73-78
95. Weber, W. and Kewitz, H. (1985) Determination of thiamine in human plasma and its pharmacokinetics Eur. J. Clin. Pharmacol. 28, 213-219
96. Hayashi, K., Yoshida, S., and Kawasaki, T. (1981) Thiamine transport in the brush border membrane vesicles of the guinea-pig jejunum Biochim. Biophys. Acta 641, 106-113
97. Said, H. M., Ortiz, A., Kumar, C. K., Chatterjee, N., Dudeja, P. K., and Rubin, S. (1999) Transport of thiamine in human intestine: Mechanism and regulation in intestinal epithelial cell model Caco-2 Am. J. Physiol. 277, C645-C651
98. Chen, C.-P. (1978) Active transport of thiamine by freshly isolated rat hepatocytes J. Nutr. Sci. Vitaminol. 24, 351
99. + uptake by Caco-2 cells Pharmacol. Res. 48, 579-584
100. Komai, T. and Shindo, H. (1974) Transport of thiamine into red blood cells of the rat J. Nutr. Sci. Vitaminol. 20, 189-196
101. Davis, R. E. and Icke, G. C. (1983) Clinical chemistry of thiamin Adv. Clin. Chem. 23, 93-140
102. Yoshioka, K. (1984) Some properties of the thiamine uptake system in isolated rat hepatocytes Biochim. Biophys. Acta 778, 201-209
103. Venter, J. C., Adams, M. D., Myers, E. W., Li, P. W., Mural, R. J., Sutton, G. G., Smith, H. O., Yandell, M., Evans, C. A., and Holt, R. A. (2001) The sequence of the human genome Sci. Signaling 291, 1304
104. Venter, J. C., Adams, M. D., Myers, E. W., Li, P. W., Mural, R. J., Sutton, G. G., Smith, H. O., Yandell, M., Evans, C. A., Holt, R. A., Gocayne, J. D., Amanatides, P., Ballew, R. M., Huson, D. H., Wortman, J. R., Zhang, Q., Kodira, C. D., Zheng, X. H., Chen, L., Skupski, M., Subramanian, G., Thomas, P. D., Zhang, J., Gabor Miklos, G. L., Nelson, C., Broder, S., Clark, A. G., Nadeau, J., McKusick, V. A., Zinder, N., Levine, A. J., Roberts, R. J., Simon, M., Slayman, C., Hunkapiller, M., Bolanos, R., Delcher, A., Dew, I., Fasulo, D., Flanigan, M., Florea, L., Halpern, A., Hannenhalli, S., Kravitz, S., Levy, S., Mobarry, C., Reinert, K., Remington, K., Abu-Threideh, J., Beasley, E., Biddick, K., Bonazzi, V., Brandon, R., Cargill, M., Chandramouliswaran, I., Charlab, R., Chaturvedi, K., Deng, Z., Francesco, V. D., Dunn, P., Eilbeck, K., Evangelista, C., Gabrielian, A. E., Gan, W., Ge, W., Gong, F., Gu, Z., Guan, P., Heiman, T. J., Higgins, M. E., Ji, R.-R., Ke, Z., Ketchum, K. A., Lai, Z., Lei, Y., Li, Z., Li, J., Liang, Y., Lin, X., Lu, F., Merkulov, G. V., Milshina, N., Moore, H. M., Naik, A. K., Narayan, V. A., Neelam, B., Nusskern, D., Rusch, D. B., Salzberg, S., Shao, W., Shue, B., Sun, J., Wang, Z. Y., Wang, A., Wang, X., Wang, J., Wei, M.-H., Wides, R., Xiao, C., Yan, C., Yao, A., Ye, J., Zhan, M., Zhang, W., Zhang, H., Zhao, Q., Zheng, L., Zhong, F., Zhong, W., Zhu, S. C., Zhao, S., Gilbert, D., Baumhueter, S., Spier, G., Carter, C., Cravchik, A., Woodage, T., Ali, F., An, H., Awe, A., Baldwin, D., Baden, H., Barnstead, M., Barrow, I., Beeson, K., Busam, D., Carver, A., Center, A., Cheng, M. L., Curry, L., Danaher, S., Davenport, L., Desilets, R., Dietz, S., Dodson, K., Doup, L., Ferriera, S., Garg, N., Gluecksmann, A., Hart, B., Haynes, J., Haynes, C., Heiner, C., Hladun, S., Hostin, D., Houck, J., Howland, T., Ibegwam, C., Johnson, J., Kalush, F., Kline, L., Koduru, S., Love, A., Mann, F., May, D., McCawley, S., McIntosh, T., McMullen, I., Moy, M., Moy, L., Murphy, B., Nelson, K., Pfannkoch, C., Pratts, E., Puri, V., Qureshi, H., Reardon, M., Rodriguez, R., Rogers, Y.-H., Romblad, D., Ruhfel, B., Scott, R., Sitter, C., Smallwood, M., Stewart, E., Strong, R., Suh, E., Thomas, R., Tint, N. N., Tse, S., Vech, C., Wang, G., Wetter, J., Williams, S., Williams, M., Windsor, S., Winn-Deen, E., Wolfe, K., Zaveri, J., Zaveri, K., Abril, J. F., Guigó, R., Campbell, M. J., Sjolander, K. V., Karlak, B., Kejariwal, A., Mi, H., Lazareva, B., Hatton, T., Narechania, A., Diemer, K., Muruganujan, A., Guo, N., Sato, S., Bafna, V., Istrail, S., Lippert, R., Schwartz, R., Walenz, B., Yooseph, S., Allen, D., Basu, A., Baxendale, J., Blick, L., Caminha, M., Carnes-Stine, J., Caulkqq, P., Chiang, Y.-H., Coyne, M., Dahlke, C., Mays, A. D., Dombroski, M., Donnelly, M., Ely, D., Esparham, S., Fosler, C., Gire, H., Glanowski, S., Glasser, K., Glodek, A., Gorokhov, M., Graham, K., Gropman, B., Harris, M., Heil, J., Henderson, S., Hoover, J., Jennings, D., Jordan, C., Jordan, J., Kasha, J., Kagan, L., Kraft, C., Levitsky, A., Lewis, M., Liu, X., Lopez, J., Ma, D., Majoros, W., McDaniel, J., Murphy, S., Newman, M., Nguyen, T., Nguyen, N., Nodell, M., Pan, S., Peck, J., Peterson, M., Rowe, W., Sanders, R., Scott, J., Simpson, M., Smith, T., Sprague, A., Stockwell, T., Turner, R., Venter, E., Wang, M., Wen, M., Wu, D., Wu, M., Xia, A., Zandieh, A., and Zhu, X. (2001) The Sequence of the Human Genome Science 291, 1304-1351
105. Dutta, B., Huang, W., Molero, M., Kekuda, R., Leibach, F. H., Devoe, L. D., Ganapathy, V., and Prasad, P. D. (1999) Cloning of the human thiamine transporter, a member of the folate transporter family J. Biol. Chem. 274, 31925-31929
106. Said, H. M., Balamurugan, K., Subramanian, V. S., and Marchant, J. S. (2004) Expression and functional contribution of hTHTR-2 in thiamin absorption in human intestine Am. J. Physiol. 286, G491-G498
107. Zhao, R., Gao, F., Wang, Y., Diaz, G. A., Gelb, B. D., and Goldman, I. D. (2001) Impact of the reduced folate carrier on the accumulation of active thiamin metabolites in murine leukemia cells J. Biol. Chem. 276, 1114-1118
108. Zhao, R., Gao, F., and Goldman, I. D. (2002) Reduced folate carrier transports thiamine monophosphate: An alternative route for thiamine delivery into mammalian cells Am. J. Physiol. 282, C1512-C1517
109. Xu, K., Zhang, M., Zhao, Q., Yu, F., Guo, H., Wang, C., He, F., Ding, J., and Zhang, P. (2013) Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis Nature 497, 268-271
110. Oshima, Y. (1997) The phosphatase system in Saccharomyces cerevisiae Genes Genet. Syst. 72, 323-334
111. Matherly, L. H. and Goldman, I. D. (2003) Membrane transport of folates Vitam. Horm. 66, 403-456
112. Russel, F. G., Masereeuw, R., and van Aubel, R. A. (2002) Molecular aspects of renal anionic drug transport Annu. Rev. Physiol. 64, 563-594
113. Ganapathy, V., Smith, S. B., and Prasad, P. D. (2004) SLC19: The folate/thiamine transporter family Pfluegers Arch. 447, 641-646
114. Hediger, M. A., Romero, M. F., Peng, J.-B., Rolfs, A., Takanaga, H., and Bruford, E. A. (2004) The ABCs of solute carriers: Physiological, pathological and therapeutic implications of human membrane transport proteins Pfluegers Arch. 447, 465-468
115. Rodionov, D. A., Hebbeln, P., Eudes, A., ter Beek, J., Rodionova, I. A., Erkens, G. B., Slotboom, D. J., Gelfand, M. S., Osterman, A. L., and Hanson, A. D. (2009) A novel class of modular transporters for vitamins in prokaryotes J. Bacteriol. 191, 42-51
116. Eudy, J. D., Spiegelstein, O., Barber, R. C., Wlodarczyk, B. J., Talbot, J., and Finnell, R. H. (2000) Identification and Characterization of the Human and Mouse SLC19A3 Gene: A Novel Member of the Reduced Folate Family of Micronutrient Transporter Genes Mol. Genet. Metab. 71, 581-590
117. Dixon, K. H., Lanpher, B. C., Chiu, J., Kelley, K., and Cowan, K. H. (1994) A novel cDNA restores reduced folate carrier activity and methotrexate sensitivity to transport deficient cells J. Biol. Chem. 269, 17-20
118. Diaz, G. A., Banikazemi, M., Oishi, K., Desnick, R. J., and Gelb, B. D. (1999) Mutations in a new gene encoding a thiamine transporter cause thiamine-responsive megaloblastic anaemia syndrome Nat. Genet. 22, 309-312
119. Zhao, R. and Goldman, I. D. (2013) Folate and thiamine transporters mediated by facilitative carriers (SLC19A1-3 and SLC46A1) and folate receptors Mol. Aspects Med. 34, 373-385
120. Rajgopal, A., Edmondnson, A., Goldman, I. D., and Zhao, R. (2001) SLC19A3 encodes a second thiamine transporter ThTr2 Biochim. Biophys. Acta 1537, 175-178
121. Nabokina, S. M. and Said, H. M. (2004) Characterization of the 5′-regulatory region of the human thiamin transporter SLC19A3: In vitro and in vivo studies Am. J. Physiol. 287, G822-G829
122. Pao, S. S., Paulsen, I. T., and Saier, M. H. (1998) Major facilitator superfamily Microbiol. Mol. Biol. Rev. 62, 1-34
123. Hetenyi, C. and van der Spoel, D. (2002) Efficient docking of peptides to proteins without prior knowledge of the binding site Protein Sci. 11, 1729-1737
124. Hetenyi, C. and van der Spoel, D. (2006) Blind docking of drug-sized compounds to proteins with up to a thousand residues FEBS Lett. 580, 1447-1450
125. Hetenyi, C. and van der Spoel, D. (2011) Toward prediction of functional protein pockets using blind docking and pocket search algorithms Protein Sci. 20, 880-893
126. Erkens, G. B., Berntsson, R. P., Fulyani, F., Majsnerowska, M., Vujičić-Žagar, A., ter Beek, J., Poolman, B., and Slotboom, D. J. (2011) The structural basis of modularity in ECF-type ABC transporters Nat. Struct. Mol. Biol. 18, 755-760
127. Erkens, G. B. and Slotboom, D. J. (2010) Biochemical characterization of ThiT from Lactococcus lactis: A thiamin transporter with picomolar substrate binding affinity Biochemistry 49, 3203-3212
128. Majsnerowska, M., Hänelt, I., Wunnicke, D., Schäfer, L. V., Steinhoff, H.-J., and Slotboom, D. J. (2013) Substrate-Induced Conformational Changes in the S-Component ThiT from an Energy Coupling Factor Transporter Structure 21, 861-867
129. Wang, T., Fu, G., Pan, X., Wu, J., Gong, X., Wang, J., and Shi, Y. (2013) Structure of a bacterial energy-coupling factor transporter Nature 497, 272-276
130. Zhang, P. (2013) Structure and mechanism of energy-coupling factor transporters Trends Microbiol. 21, 652-659
131. Schömig, E., Lazar, A., and Gründemann, D. (2006) Extraneuronal monoamine transporter and organic cation transporters 1 and 2: A review of transport efficiency. In Neurotransmitter Transporters, pp 151-180, Springer, Berlin.
132. Amara, S. G. and Kuhar, M. J. (1993) Neurotransmitter transporters: Recent progress Annu. Rev. Neurosci. 16, 73-93
133. Koepsell, H., Lips, K., and Volk, C. (2007) Polyspecific organic cation transporters: Structure, function, physiological roles, and biopharmaceutical implications Pharm. Res. 24, 1227-1251
134. Koepsell, H., Schmitt, B., and Gorboulev, V. (2004) Organic cation transporters. In Reviews of physiology, biochemistry and pharmacology, pp 36-90, Springer, Berlin.
135. Bottalico, B., Larsson, I., Brodszki, J., Hernandez-Andrade, E., Casslén, B., Marsál, K., and Hansson, S. R. (2004) Norepinephrine Transporter (NET), Serotonin Transporter (SERT), Vesicular Monoamine Transporter (VMAT2) and Organic Cation Transporters (OCT1, 2 and EMT) in Human Placenta from Pre-eclamptic and Normotensive Pregnancies Placenta 25, 518-529
136. Ito, S. and Alcorn, J. (2003) Xenobiotic transporter expression and function in the human mammary gland Adv. Drug Delivery Rev. 55, 653-665
137. Gorboulev, V., Ulzheimer, J. C., Akhoundova, A., Ulzheimer-Teuber, I., Karbach, U., Quester, S., Baumann, C., Lang, F., Busch, A. E., and Koepsell, H. (1997) Cloning and characterization of two human polyspecific organic cation transporters DNA Cell Biol. 16, 871-881
138. Kekuda, R., Prasad, P. D., Wu, X., Wang, H., Fei, Y.-J., Leibach, F. H., and Ganapathy, V. (1998) Cloning and functional characterization of a potential-sensitive, polyspecific organic cation transporter (OCT3) most abundantly expressed in placenta J. Biol. Chem. 273, 15971-15979
139. Wu, X., George, R. L., Huang, W., Wang, H., Conway, S. J., Leibach, F. H., and Ganapathy, V. (2000) Structural and functional characteristics and tissue distribution pattern of rat OCTN1, an organic cation transporter, cloned from placenta Biochim. Biophys. Acta 1466, 315-327
140. Wu, X., Huang, W., Prasad, P. D., Seth, P., Rajan, D. P., Leibach, F. H., Chen, J., Conway, S. J., and Ganapathy, V. (1999) Functional Characteristics and Tissue Distribution Pattern of Organic Cation Transporter 2 (OCTN2), an Organic Cation/Carnitine Transporter J. Pharmacol. Exp. Ther. 290, 1482-1492
141. Kobayashi, D., Aizawa, S., Maeda, T., Tsuboi, I., Yabuuchi, H., Nezu, J.-i., Tsuji, A., and Tamai, I. (2004) Expression of organic cation transporter OCTN1 in hematopoietic cells during erythroid differentiation Exp. Hematol. 32, 1156-1162
142. Gründemann, D., Liebich, G., Kiefer, N., Köster, S., and Schömig, E. (1999) Selective substrates for non-neuronal monoamine transporters Mol. Pharmacol. 56, 1-10
143. Martel, F., Vetter, T., Russ, H., Gründemann, D., Azevedo, I., Koepsell, H., and Schömig, E. (1996) Transport of small organic cations in the rat liver Naunyn-Schmiedeberg's Arch. Pharmacol. 354, 320-326
144. Martel, F., Keating, E., Calhau, C., Gründemann, D., Schömig, E., and Azevedo, I. (2001) Regulation of human extraneuronal monoamine transporter (hEMT) expressed in HEK293 cells by intracellular second messenger systems Naunyn-Schmiedeberg's Arch. Pharmacol. 364, 487-495
145. Keating, E., Lemos, C., Monteiro, R., Azevedo, I., and Martel, F. (2004) The effect of a series of organic cations upon the plasmalemmal serotonin transporter, SERT Life Sci. 76, 103-119
146. Ugolev, A. M. (1972) Membrane Digestion Gut 13, 735-747
147. Dudeja, P. K., Tyagi, S., Kavilaveettil, R. J., Gill, R., and Said, H. M. (2001) Mechanism of thiamine uptake by human jejunal brush-border membrane vesicles Am. J. Physiol. 281, C786-C792
148. +/organic cation antiporter, kidney-specific multidrug and toxin extrusion 2 J. Am. Soc. Nephrol. 17, 2127-2135
149. Guan, L., Mirza, O., Verner, G., Iwata, S., and Kaback, H. R. (2007) Structural determination of wild-type lactose permease Proc. Natl. Acad. Sci. U.S.A. 104, 15294-15298
150. Martins, M. J., Negrão, M. R., Hipólito-Reis, C., and Azevedo, I. (2001) Arginine and a polyarginine peptide inhibit alkaline phosphatase activity: Possible consequences for cellular transport systems Clin. Biochem. 34, 435-437
151. Van Hoof, V. O. and De Broe, M. E. (1994) Interpretation and clinical significance of alkaline phosphatase isoenzyme patterns Crit. Rev. Clin. Lab. Sci. 31, 197-293
152. Iwashima, A. and Nishimura, H. (1979) Isolation of a thiamine-binding protein from Saccharomyces cerevisiae Biochim. Biophys. Acta 577, 217-220
153. Matsuda, T., Baba, A., and Iwata, H. (1978) Possible role of intestinal alkaline phosphatase activity in thiamine transport Experientia 34, 18-20
154. Calhau, C., Hipólito-Reis, C., and Azevedo, I. (1999) Alkaline phosphatase and exchange surfaces Clin. Biochem. 32, 153-154
155. Calhau, C., Martel, F., Hipólito-Reis, C., and Azevedo, I. (2000) Differences between duodenal and jejunal rat alkaline phosphatase Clin. Biochem. 33, 571-577
156. Nosaka, K., Kaneko, Y., Nishimura, H., and Iwashima, A. (1989) A possible role for acid phosphatase with thiamin-binding activity encoded by PHO3 in yeast FEMS Microbiol. Lett. 60, 55-59
157. Nosaka, K. (1990) High affinity of acid phosphatase encoded by PHO3 gene in Saccharomyces cerevisiae for thiamin phosphates Biochim. Biophys. Acta 1037, 147-154
158. Schaller, K. and Höller, H. (1975) Thiamine absorption in the rat. II. Intestinal alkaline phosphatase activity and thiamine absorption from rat small intestine in-vitro and in-vivo Int. J. Vitam. Nutr. Res. 45, 30
159. Young, G., Friedman, S., Yedlin, S., and Allers, D. (1981) Effect of fat feeding on intestinal alkaline phosphatase activity in tissue and serum Am. J. Physiol. 241, G461-G468
160. PetitClerc, C. and Plante, G. E. (1981) Renal transport of phosphate: Role of alkaline phosphatase Can. J. Physiol. Pharmacol. 59, 311-323
161. Tandon, S. and Prasad, S. (2000) Effect of thiamine on the cadmium-chelating capacity of thiol compounds Hum. Exp. Toxicol. 19, 523-528
162. Sussman, N., Eliakim, R., Rubin, D., Perlmutter, D., DeSchryver- Kecskemeti, K., and Alpers, D. (1989) Intestinal alkaline phosphatase is secreted bidirectionally from villous enterocytes Am. J. Physiol. 257, G14-G23
163. Fishman, W. H. (1974) Perspectives on alkaline phosphatase isoenzymes Am. J. Med. 56, 617-650
164. Kim, E. E. and Wyckoff, H. W. (1991) Reaction mechanism of alkaline phosphatase based on crystal structures: Two-metal ion catalysis J. Mol. Biol. 218, 449-464
165. Stange, E., Schneider, A., Schusdziarra, V., and Ditschuneit, H. (1984) Inhibitory effects of somatostatin on growth and differentiation in cultured intestinal mucosa Horm. Metab. Res. 16, 74
166. Rindi, G., Ricci, V., Gastaldi, G., and Patrini, C. (1995) Intestinal alkaline phosphatase can transphosphorylate thiamin to thiamin monophosphate during intestinal transport in the rat Arch. Physiol. Biochem. 103, 33-38
167. Llinas, P., Stura, E. A., Ménez, A., Kiss, Z., Stigbrand, T., Millán, J. L., and Le Du, M. H. (2005) Structural studies of human placental alkaline phosphatase in complex with functional ligands J. Mol. Biol. 350, 441-451
168. Malandrinos, G., Louloudi, M., and Hadjiliadis, N. (2006) Thiamine models and perspectives on the mechanism of action of thiamine-dependent enzymes Chem. Soc. Rev. 35, 684-692
169. Frank, R., Leeper, F., and Luisi, B. (2007) Structure, mechanism and catalytic duality of thiamine-dependent enzymes Cell. Mol. Life Sci. 64, 892-905
170. Makarchikov, A. F., Lakaye, B., Gulyai, I., Czerniecki, J., Coumans, B., Wins, P., Grisar, T., and Bettendorff, L. (2003) Thiamine triphosphate and thiamine triphosphatase activities: From bacteria to mammals Cell. Mol. Life Sci. 60, 1477-1488
171. Shikata, H., Koyama, S., Egi, Y., Yamada, K., and Kawasaki, T. (1989) Cytosolic adenylate kinase catalyzes the synthesis of thiamin triphosphate from thiamin diphosphate Biochem. Int. 18, 933
172. Lakaye, B., Makarchikov, A. F., Antunes, A. F., Zorzi, W., Coumans, B., De Pauw, E., Wins, P., Grisar, T., and Bettendorff, L. (2002) Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues J. Biol. Chem. 277, 13771-13777
173. Gonnet, G. H. (2012) Surprising results on phylogenetic tree building methods based on molecular sequences BMC Bioinf. 13, 148
174. Dolinsky, T., Nielsen, J., McCammon, J., and Baker, N. (2004) PDB2PQR: An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations Nucleic Acids Res. 32, W665-W667
175. Baker, N., Sept, D., Joseph, S., Holst, M., and McCammon, J. (2001) Electrostatics of nanosystems: Application to microtubules and the ribosome Proc. Natl. Acad. Sci. U.S.A. 98, 10037-10041
176. Sippl, M. J. and Wiederstein, M. (2008) A note on difficult structure alignment problems Bioinformatics 24, 426-427