메뉴 건너뛰기




Volumn 213, Issue 1, 2015, Pages 191-212

Physiological role of taurine – from organism to organelle

Author keywords

apoptosis; cell volume regulation; hypoxia; lung function; membrane dynamics; mitochondrial function

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN; TAURINE; TAURINE TRANSPORTER;

EID: 85028211565     PISSN: 17481708     EISSN: 17481716     Source Type: Journal    
DOI: 10.1111/apha.12365     Document Type: Review
Times cited : (267)

References (212)
  • 1
    • 0027495394 scopus 로고
    • The content of free amino acids in the human duodenal mucosa
    • Ahlman, B., Leijonmarck, C.E. & Wernerman, J. 1993. The content of free amino acids in the human duodenal mucosa. Clin Nutr 12, 266–271.
    • (1993) Clin Nutr , vol.12 , pp. 266-271
    • Ahlman, B.1    Leijonmarck, C.E.2    Wernerman, J.3
  • 2
    • 84889682544 scopus 로고    scopus 로고
    • Taurine reverses endosulfan-induced oxidative stress and apoptosis in adult rat testis
    • Aly, H.A. & Khafagy, R.M. 2014. Taurine reverses endosulfan-induced oxidative stress and apoptosis in adult rat testis. Food Chem Toxicol 64, 1–9.
    • (2014) Food Chem Toxicol , vol.64 , pp. 1-9
    • Aly, H.A.1    Khafagy, R.M.2
  • 3
    • 60349087926 scopus 로고    scopus 로고
    • Taurine uptake across the human intestinal brush-border membrane is via two transporters: H(+)-coupled PAT1 (SLC36A1) and Na(+)- and Cl(−)-dependent TauT (SLC6A6)
    • Anderson, C.M., Howard, A., Walters, J.R., Ganapathy, V. & Thwaites, D.T. 2009. Taurine uptake across the human intestinal brush-border membrane is via two transporters: H(+)-coupled PAT1 (SLC36A1) and Na(+)- and Cl(−)-dependent TauT (SLC6A6). J Physiol 587, 731–744.
    • (2009) J Physiol , vol.587 , pp. 731-744
    • Anderson, C.M.1    Howard, A.2    Walters, J.R.3    Ganapathy, V.4    Thwaites, D.T.5
  • 4
    • 0023697974 scopus 로고
    • The antioxidant action of taurine, hypotaurine and their metabolic precursors
    • Aruoma, O.I., Halliwell, B., Hoey, B.M. & Butler, J. 1988. The antioxidant action of taurine, hypotaurine and their metabolic precursors. Biochem J 256, 251–255.
    • (1988) Biochem J , vol.256 , pp. 251-255
    • Aruoma, O.I.1    Halliwell, B.2    Hoey, B.M.3    Butler, J.4
  • 5
    • 0036399617 scopus 로고    scopus 로고
    • Effect of taurine on sarcoplasmic reticulum function and force in skinned fast-twitch skeletal muscle fibres of the rat
    • Bakker, A.J. & Berg, H.M. 2002. Effect of taurine on sarcoplasmic reticulum function and force in skinned fast-twitch skeletal muscle fibres of the rat. J Physiol 538, 185–194.
    • (2002) J Physiol , vol.538 , pp. 185-194
    • Bakker, A.J.1    Berg, H.M.2
  • 6
    • 0026651701 scopus 로고
    • Taurine protects against oxidant injury to rat alveolar pneumocytes
    • Banks, M.A., Porter, D.W., Martin, W.G. & Castranova, V. 1992. Taurine protects against oxidant injury to rat alveolar pneumocytes. Adv Exp Med Biol 315, 341–354.
    • (1992) Adv Exp Med Biol , vol.315 , pp. 341-354
    • Banks, M.A.1    Porter, D.W.2    Martin, W.G.3    Castranova, V.4
  • 7
    • 0037098715 scopus 로고    scopus 로고
    • Carrier-mediated uptake and release of taurine from Bergmann glia in rat cerebellar slices
    • Barakat, L., Wang, D. & Bordey, A. 2002. Carrier-mediated uptake and release of taurine from Bergmann glia in rat cerebellar slices. J Physiol 541, 753–767.
    • (2002) J Physiol , vol.541 , pp. 753-767
    • Barakat, L.1    Wang, D.2    Bordey, A.3
  • 9
    • 0032931584 scopus 로고    scopus 로고
    • Effect of muscle glycogen on glucose, lactate and amino acid metabolism during exercise and recovery in human subjects
    • Blomstrand, E. & Saltin, B. 1999. Effect of muscle glycogen on glucose, lactate and amino acid metabolism during exercise and recovery in human subjects. J Physiol 514(Pt 1), 293–302.
    • (1999) J Physiol , vol.514 , pp. 293-302
    • Blomstrand, E.1    Saltin, B.2
  • 10
    • 33947610711 scopus 로고    scopus 로고
    • Taurine as a marker for foetal wellbeing?
    • de Boo, H.A. & Harding, J.E. 2007. Taurine as a marker for foetal wellbeing? Neonatology 91, 145–154.
    • (2007) Neonatology , vol.91 , pp. 145-154
    • de Boo, H.A.1    Harding, J.E.2
  • 11
    • 67649400331 scopus 로고    scopus 로고
    • Taurine protects transformed rat retinal ganglion cells from hypoxia-induced apoptosis by preventing mitochondrial dysfunction
    • Chen, K., Zhang, Q., Wang, J., Liu, F., Mi, M., Xu, H., Chen, F. & Zeng, K. 2009. Taurine protects transformed rat retinal ganglion cells from hypoxia-induced apoptosis by preventing mitochondrial dysfunction. Brain Res 1279, 131–138.
    • (2009) Brain Res , vol.1279 , pp. 131-138
    • Chen, K.1    Zhang, Q.2    Wang, J.3    Liu, F.4    Mi, M.5    Xu, H.6    Chen, F.7    Zeng, K.8
  • 13
    • 22144492553 scopus 로고    scopus 로고
    • High expression of the taurine transporter TauT in primary cilia of NIH3T3 fibroblasts
    • Christensen, S.T., Voss, J.W., Teilmann, S.C. & Lambert, I.H. 2005. High expression of the taurine transporter TauT in primary cilia of NIH3T3 fibroblasts. Cell Biol Int 29, 347–351.
    • (2005) Cell Biol Int , vol.29 , pp. 347-351
    • Christensen, S.T.1    Voss, J.W.2    Teilmann, S.C.3    Lambert, I.H.4
  • 14
    • 84862762426 scopus 로고    scopus 로고
    • Taurine protects rat testes against doxorubicin-induced oxidative stress as well as p53, Fas and caspase 12-mediated apoptosis
    • Das, J., Ghosh, J., Manna, P. & Sil, P.C. 2012. Taurine protects rat testes against doxorubicin-induced oxidative stress as well as p53, Fas and caspase 12-mediated apoptosis. Amino Acids 42, 1839–1855.
    • (2012) Amino Acids , vol.42 , pp. 1839-1855
    • Das, J.1    Ghosh, J.2    Manna, P.3    Sil, P.C.4
  • 15
    • 84875881075 scopus 로고    scopus 로고
    • Taurine transport in human placental trophoblast is important for regulation of cell differentiation and survival
    • Desforges, M., Parsons, L., Westwood, M., Sibley, C.P. & Greenwood, S.L. 2013. Taurine transport in human placental trophoblast is important for regulation of cell differentiation and survival. Cell Death Dis 4, e559.
    • (2013) Cell Death Dis , vol.4
    • Desforges, M.1    Parsons, L.2    Westwood, M.3    Sibley, C.P.4    Greenwood, S.L.5
  • 17
    • 34548477656 scopus 로고    scopus 로고
    • Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase
    • Dominy, J.E. Jr, Simmons, C.R., Hirschberger, L.L., Hwang, J., Coloso, R.M. & Stipanuk, M.H. 2007. Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. J Biol Chem 282, 25189–25198.
    • (2007) J Biol Chem , vol.282 , pp. 25189-25198
    • Dominy, J.E.1    Simmons, C.R.2    Hirschberger, L.L.3    Hwang, J.4    Coloso, R.M.5    Stipanuk, M.H.6
  • 18
    • 0023145969 scopus 로고
    • Effect of guanidinoethyl sulfonate on taurine concentrations and fetal growth in pregnant rats
    • Ejiri, K., Akahori, S., Kudo, K., Sekiba, K. & Ubuka, T. 1987. Effect of guanidinoethyl sulfonate on taurine concentrations and fetal growth in pregnant rats. Biol Neonate 51, 234–240.
    • (1987) Biol Neonate , vol.51 , pp. 234-240
    • Ejiri, K.1    Akahori, S.2    Kudo, K.3    Sekiba, K.4    Ubuka, T.5
  • 19
    • 0033232989 scopus 로고    scopus 로고
    • Growth factors and taurine protect against excitotoxicity by stabilizing calcium homeostasis and energy metabolism
    • El, I.A. & Trenkner, E. 1999. Growth factors and taurine protect against excitotoxicity by stabilizing calcium homeostasis and energy metabolism. J Neurosci 19, 9459–9468.
    • (1999) J Neurosci , vol.19 , pp. 9459-9468
    • El, I.A.1    Trenkner, E.2
  • 20
    • 84890118861 scopus 로고    scopus 로고
    • The p53 protein and its molecular network: modelling a missing link between DNA damage and cell fate
    • Elias, J., Dimitrio, L., Clairambault, J. & Natalini, R. 2014. The p53 protein and its molecular network: modelling a missing link between DNA damage and cell fate. Biochim Biophys Acta 1844, 232–247.
    • (2014) Biochim Biophys Acta , vol.1844 , pp. 232-247
    • Elias, J.1    Dimitrio, L.2    Clairambault, J.3    Natalini, R.4
  • 21
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: a review of programmed cell death
    • Elmore, S. 2007. Apoptosis: a review of programmed cell death. Toxicol Pathol 35, 495–516.
    • (2007) Toxicol Pathol , vol.35 , pp. 495-516
    • Elmore, S.1
  • 22
    • 13844309773 scopus 로고    scopus 로고
    • 2+-mediated potentiation of the swelling-induced taurine efflux from HeLa cells: on the role of calmodulin and novel protein kinase C isoforms
    • 2+-mediated potentiation of the swelling-induced taurine efflux from HeLa cells: on the role of calmodulin and novel protein kinase C isoforms. J Membr Biol 201, 59–75.
    • (2004) J Membr Biol , vol.201 , pp. 59-75
    • Falktoft, B.1    Lambert, I.H.2
  • 24
    • 47249104375 scopus 로고    scopus 로고
    • Volume-sensitive NADPH oxidase activity and taurine efflux in NIH3T3 mouse fibroblasts
    • Friis, M.B., Vorum, K.G. & Lambert, I.H. 2008. Volume-sensitive NADPH oxidase activity and taurine efflux in NIH3T3 mouse fibroblasts. Am J Physiol Cell Physiol 294, C1552–C1565.
    • (2008) Am J Physiol Cell Physiol , vol.294 , pp. C1552-C1565
    • Friis, M.B.1    Vorum, K.G.2    Lambert, I.H.3
  • 25
    • 84865961065 scopus 로고    scopus 로고
    • Intestinal drug transport via the proton-coupled amino acid transporter PAT1 (SLC36A1) is inhibited by Gly-X(aa) dipeptides
    • Frolund, S., Langthaler, L., Kall, M.A., Holm, R. & Nielsen, C.U. 2012. Intestinal drug transport via the proton-coupled amino acid transporter PAT1 (SLC36A1) is inhibited by Gly-X(aa) dipeptides. Mol Pharm 9, 2761–2769.
    • (2012) Mol Pharm , vol.9 , pp. 2761-2769
    • Frolund, S.1    Langthaler, L.2    Kall, M.A.3    Holm, R.4    Nielsen, C.U.5
  • 26
    • 33746921195 scopus 로고    scopus 로고
    • Oxidative stress in hepatic ischemia-reperfusion injury: the role of antioxidants and iron chelating compounds
    • Galaris, D., Barbouti, A. & Korantzopoulos, P. 2006. Oxidative stress in hepatic ischemia-reperfusion injury: the role of antioxidants and iron chelating compounds. Curr Pharm Des 12, 2875–2890.
    • (2006) Curr Pharm Des , vol.12 , pp. 2875-2890
    • Galaris, D.1    Barbouti, A.2    Korantzopoulos, P.3
  • 27
    • 84855335568 scopus 로고    scopus 로고
    • Targeting the restricted alpha-subunit repertoire of airway smooth muscle GABAA receptors augments airway smooth muscle relaxation
    • Gallos, G., Yim, P., Chang, S., Zhang, Y., Xu, D., Cook, J.M., Gerthoffer, W.T. & Emala, C.W. Sr 2012. Targeting the restricted alpha-subunit repertoire of airway smooth muscle GABAA receptors augments airway smooth muscle relaxation. Am J Physiol Lung Cell Mol Physiol 302, L248–L256.
    • (2012) Am J Physiol Lung Cell Mol Physiol , vol.302 , pp. L248-L256
    • Gallos, G.1    Yim, P.2    Chang, S.3    Zhang, Y.4    Xu, D.5    Cook, J.M.6    Gerthoffer, W.T.7    Emala, C.W.8
  • 28
    • 0026682738 scopus 로고
    • Urinary taurine excretion as a function of taurine intake in adult cats
    • Glass, E.N., Odle, J. & Baker, D.H. 1992. Urinary taurine excretion as a function of taurine intake in adult cats. J Nutr 122, 1135–1142.
    • (1992) J Nutr , vol.122 , pp. 1135-1142
    • Glass, E.N.1    Odle, J.2    Baker, D.H.3
  • 29
    • 0042242703 scopus 로고    scopus 로고
    • Effects of taurine deficiency and chronic methanol administration on rat retina, optic nerve and brain amino acids and monoamines
    • Gonzalez-Quevedo, A., Obregon, F., Urbina, M., Rousso, T. & Lima, L. 2003. Effects of taurine deficiency and chronic methanol administration on rat retina, optic nerve and brain amino acids and monoamines. Nutr Neurosci 6, 253–261.
    • (2003) Nutr Neurosci , vol.6 , pp. 253-261
    • Gonzalez-Quevedo, A.1    Obregon, F.2    Urbina, M.3    Rousso, T.4    Lima, L.5
  • 30
    • 67650079051 scopus 로고    scopus 로고
    • Taurine supplementation increases skeletal muscle force production and protects muscle function during and after high-frequency in vitro stimulation
    • Goodman, C.A., Horvath, D., Stathis, C., Mori, T., Croft, K., Murphy, R.M. & Hayes, A. 2009. Taurine supplementation increases skeletal muscle force production and protects muscle function during and after high-frequency in vitro stimulation. J Appl Physiol 107, 144–154.
    • (2009) J Appl Physiol , vol.107 , pp. 144-154
    • Goodman, C.A.1    Horvath, D.2    Stathis, C.3    Mori, T.4    Croft, K.5    Murphy, R.M.6    Hayes, A.7
  • 31
    • 0022977888 scopus 로고
    • 2-induced alterations. A histologic, ultrastructural, and freeze-fracture study
    • 2-induced alterations. A histologic, ultrastructural, and freeze-fracture study. Am J Pathol 125, 585–600.
    • (1986) Am J Pathol , vol.125 , pp. 585-600
    • Gordon, R.E.1    Shaked, A.A.2    Solano, D.F.3
  • 32
    • 0033839060 scopus 로고    scopus 로고
    • Suppression of bleomycin-induced nitric oxide production in mice by taurine and niacin
    • Gurujeyalakshmi, G., Wang, Y. & Giri, S.N. 2000. Suppression of bleomycin-induced nitric oxide production in mice by taurine and niacin. Nitric Oxide 4, 399–411.
    • (2000) Nitric Oxide , vol.4 , pp. 399-411
    • Gurujeyalakshmi, G.1    Wang, Y.2    Giri, S.N.3
  • 33
    • 0025776367 scopus 로고
    • Interaction of taurine with methionine: inhibition of myocardial phospholipid methyltransferase
    • Hamaguchi, T., Azuma, J. & Schaffer, S. 1991. Interaction of taurine with methionine: inhibition of myocardial phospholipid methyltransferase. J Cardiovasc Pharmacol 18, 224–230.
    • (1991) J Cardiovasc Pharmacol , vol.18 , pp. 224-230
    • Hamaguchi, T.1    Azuma, J.2    Schaffer, S.3
  • 34
    • 33749555278 scopus 로고    scopus 로고
    • The effect of taurine depletion on the contractile properties and fatigue in fast-twitch skeletal muscle of the mouse
    • Hamilton, E.J., Berg, H.M., Easton, C.J. & Bakker, A.J. 2006. The effect of taurine depletion on the contractile properties and fatigue in fast-twitch skeletal muscle of the mouse. Amino Acids 31, 273–278.
    • (2006) Amino Acids , vol.31 , pp. 273-278
    • Hamilton, E.J.1    Berg, H.M.2    Easton, C.J.3    Bakker, A.J.4
  • 35
    • 84878774330 scopus 로고    scopus 로고
    • Knockdown of TauT expression impairs human embryonic kidney 293 cell development
    • Han, X. & Chesney, R.W. 2013. Knockdown of TauT expression impairs human embryonic kidney 293 cell development. Adv Exp Med Biol 776, 307–320.
    • (2013) Adv Exp Med Biol , vol.776 , pp. 307-320
    • Han, X.1    Chesney, R.W.2
  • 36
    • 0030391499 scopus 로고    scopus 로고
    • Role of conserved peptide in taurine transporter inactivation modulated by protein kinase C
    • Han, X., Budreau, A.M. & Chesney, R.W. 1996. Role of conserved peptide in taurine transporter inactivation modulated by protein kinase C. J Am Soc Nephrol 7, 2088–2096.
    • (1996) J Am Soc Nephrol , vol.7 , pp. 2088-2096
    • Han, X.1    Budreau, A.M.2    Chesney, R.W.3
  • 38
    • 67449095329 scopus 로고    scopus 로고
    • Functional TauT protects against acute kidney injury
    • Han, X., Yue, J. & Chesney, R.W. 2009. Functional TauT protects against acute kidney injury. J Am Soc Nephrol 20, 1323–1332.
    • (2009) J Am Soc Nephrol , vol.20 , pp. 1323-1332
    • Han, X.1    Yue, J.2    Chesney, R.W.3
  • 41
    • 84863512959 scopus 로고    scopus 로고
    • Down-regulation of the taurine transporter TauT during hypoosmotic stress in NIH3T3 mouse fibroblasts
    • Hansen, D.B., Friis, M.B., Hoffmann, E.K. & Lambert, I.H. 2012. Down-regulation of the taurine transporter TauT during hypoosmotic stress in NIH3T3 mouse fibroblasts. J Membr Biol 245, 77–87.
    • (2012) J Membr Biol , vol.245 , pp. 77-87
    • Hansen, D.B.1    Friis, M.B.2    Hoffmann, E.K.3    Lambert, I.H.4
  • 43
    • 8144229293 scopus 로고    scopus 로고
    • Taurine in neonatal nutrition–revisited
    • Heird, W.C. 2004. Taurine in neonatal nutrition–revisited. Arch Dis Child Fetal Neonatal Ed 89, F473–F474.
    • (2004) Arch Dis Child Fetal Neonatal Ed , vol.89 , pp. F473-F474
    • Heird, W.C.1
  • 45
    • 77954757143 scopus 로고    scopus 로고
    • Proton-assisted amino-acid transporters are conserved regulators of proliferation and amino-acid-dependent mTORC1 activation
    • Heublein, S., Kazi, S., Ogmundsdottir, M.H., Attwood, E.V., Kala, S., Boyd, C.A., Wilson, C. & Goberdhan, D.C. 2010. Proton-assisted amino-acid transporters are conserved regulators of proliferation and amino-acid-dependent mTORC1 activation. Oncogene 29, 4068–4079.
    • (2010) Oncogene , vol.29 , pp. 4068-4079
    • Heublein, S.1    Kazi, S.2    Ogmundsdottir, M.H.3    Attwood, E.V.4    Kala, S.5    Boyd, C.A.6    Wilson, C.7    Goberdhan, D.C.8
  • 47
    • 0024593744 scopus 로고
    • Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability
    • Hidalgo, I.J., Raub, T.J. & Borchardt, R.T. 1989. Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability. Gastroenterology 96, 736–749.
    • (1989) Gastroenterology , vol.96 , pp. 736-749
    • Hidalgo, I.J.1    Raub, T.J.2    Borchardt, R.T.3
  • 48
    • 0001046034 scopus 로고
    • The role of amino acids and taurine in isosmotic intracellular regulation in Ehrlich ascites mouse tumour cells
    • Hoffmann, E.K. & Hendil, K.B. 1976. The role of amino acids and taurine in isosmotic intracellular regulation in Ehrlich ascites mouse tumour cells. J Comp Physiol 108, 279–286.
    • (1976) J Comp Physiol , vol.108 , pp. 279-286
    • Hoffmann, E.K.1    Hendil, K.B.2
  • 49
    • 0020645258 scopus 로고
    • Amino acid transport and cell volume regulation in Ehrlich ascites tumour cells
    • Hoffmann, E.K. & Lambert, I.H. 1983. Amino acid transport and cell volume regulation in Ehrlich ascites tumour cells. J Physiol 338, 613–625.
    • (1983) J Physiol , vol.338 , pp. 613-625
    • Hoffmann, E.K.1    Lambert, I.H.2
  • 50
    • 84893464588 scopus 로고    scopus 로고
    • Ion channels and transporters in the development of drug resistance in cancer cells
    • Hoffmann, E.K. & Lambert, I.H. 2014. Ion channels and transporters in the development of drug resistance in cancer cells. Philos Trans R Soc Lond B Biol Sci 369, 20130109.
    • (2014) Philos Trans R Soc Lond B Biol Sci , vol.369 , pp. 20130109
    • Hoffmann, E.K.1    Lambert, I.H.2
  • 51
    • 0035999166 scopus 로고    scopus 로고
    • Neopterin inhibits ATP-induced calcium release in alveolar epithelial cells in vitro
    • Hoffmann, G., Gollnick, F. & Meyer, R. 2002. Neopterin inhibits ATP-induced calcium release in alveolar epithelial cells in vitro. Mediators Inflamm 11, 181–185.
    • (2002) Mediators Inflamm , vol.11 , pp. 181-185
    • Hoffmann, G.1    Gollnick, F.2    Meyer, R.3
  • 52
    • 55949107533 scopus 로고    scopus 로고
    • Physiology of cell volume regulation in vertebrates
    • Hoffmann, E.K., Lambert, I.H. & Pedersen, S.F. 2009. Physiology of cell volume regulation in vertebrates. Physiol Rev 89, 193–277.
    • (2009) Physiol Rev , vol.89 , pp. 193-277
    • Hoffmann, E.K.1    Lambert, I.H.2    Pedersen, S.F.3
  • 53
    • 84901048943 scopus 로고    scopus 로고
    • Functions of volume-sensitive and calcium activated chloride channels
    • Hoffmann, E.K., Holm, N.B. & Lambert, I.H. 2014. Functions of volume-sensitive and calcium activated chloride channels. IUBMB Life 66, 257–267.
    • (2014) IUBMB Life , vol.66 , pp. 257-267
    • Hoffmann, E.K.1    Holm, N.B.2    Lambert, I.H.3
  • 54
    • 84879575580 scopus 로고    scopus 로고
    • Volume-sensitive release of organic osmolytes in the human lung epithelial cell line A
    • Holm, J.B., Grygorczyk, R. & Lambert, I.H. 2013. Volume-sensitive release of organic osmolytes in the human lung epithelial cell line A. Am J Physiol Cell Physiol 305, C48–C60.
    • (2013) Am J Physiol Cell Physiol , vol.305 , pp. C48-C60
    • Holm, J.B.1    Grygorczyk, R.2    Lambert, I.H.3
  • 55
    • 0021526810 scopus 로고
    • Taurine and hypotaurine transport by a single system in cultured neuroblastoma cells
    • Holopainen, I. & Kontro, P. 1984. Taurine and hypotaurine transport by a single system in cultured neuroblastoma cells. Acta Physiol Scand 122, 381–386.
    • (1984) Acta Physiol Scand , vol.122 , pp. 381-386
    • Holopainen, I.1    Kontro, P.2
  • 56
    • 0017870847 scopus 로고
    • Taurine: sodium-dependent, high-affinity transport into rat brain synaptosomes
    • Hruska, R.E., Padjen, A., Bressler, R. & Yamamura, H.I. 1978. Taurine: sodium-dependent, high-affinity transport into rat brain synaptosomes. Mol Pharmacol 14, 77–85.
    • (1978) Mol Pharmacol , vol.14 , pp. 77-85
    • Hruska, R.E.1    Padjen, A.2    Bressler, R.3    Yamamura, H.I.4
  • 57
    • 33947098441 scopus 로고    scopus 로고
    • Maternal taurine supplementation in the late pregnant rat stimulates postnatal growth and induces obesity and insulin resistance in adult offspring
    • Hultman, K., Alexanderson, C., Manneras, L., Sandberg, M., Holmang, A. & Jansson, T. 2007. Maternal taurine supplementation in the late pregnant rat stimulates postnatal growth and induces obesity and insulin resistance in adult offspring. J Physiol 579, 823–833.
    • (2007) J Physiol , vol.579 , pp. 823-833
    • Hultman, K.1    Alexanderson, C.2    Manneras, L.3    Sandberg, M.4    Holmang, A.5    Jansson, T.6
  • 58
    • 0026595620 scopus 로고
    • Physiological actions of taurine
    • Huxtable, R.J. 1992. Physiological actions of taurine. Physiol Rev 72, 101–163.
    • (1992) Physiol Rev , vol.72 , pp. 101-163
    • Huxtable, R.J.1
  • 59
    • 0015843454 scopus 로고
    • Effect of taurine on a muscle intracellular membrane
    • Huxtable, R. & Bressler, R. 1973. Effect of taurine on a muscle intracellular membrane. Biochim Biophys Acta 323, 573–583.
    • (1973) Biochim Biophys Acta , vol.323 , pp. 573-583
    • Huxtable, R.1    Bressler, R.2
  • 62
    • 0014274181 scopus 로고
    • Biochemistry and physiology of taurine and taurine derivatives
    • Jacobsen, J.G. & Smith, L.H. 1968. Biochemistry and physiology of taurine and taurine derivatives. Physiol Rev 48, 424–511.
    • (1968) Physiol Rev , vol.48 , pp. 424-511
    • Jacobsen, J.G.1    Smith, L.H.2
  • 63
    • 56649124742 scopus 로고    scopus 로고
    • Casein kinase 2 regulates the active uptake of the organic osmolyte taurine in NIH3T3 mouse fibroblasts
    • Jacobsen, J.H., Clement, C.A., Friis, M.B. & Lambert, I.H. 2008. Casein kinase 2 regulates the active uptake of the organic osmolyte taurine in NIH3T3 mouse fibroblasts. Pflugers Arch 457, 327–337.
    • (2008) Pflugers Arch , vol.457 , pp. 327-337
    • Jacobsen, J.H.1    Clement, C.A.2    Friis, M.B.3    Lambert, I.H.4
  • 65
    • 0027185505 scopus 로고
    • Polarity of taurine transport in cultured renal epithelial cell lines: LLC-PK1 and MDCK
    • Jones, D.P., Miller, L.A. & Chesney, R.W. 1993. Polarity of taurine transport in cultured renal epithelial cell lines: LLC-PK1 and MDCK. Am J Physiol 265, F137–F145.
    • (1993) Am J Physiol , vol.265 , pp. F137-F145
    • Jones, D.P.1    Miller, L.A.2    Chesney, R.W.3
  • 66
    • 77956052517 scopus 로고    scopus 로고
    • Effect of beta-alanine treatment on mitochondrial taurine level and 5-taurinomethyluridine content
    • Jong, C.J., Ito, T., Mozaffari, M., Azuma, J. & Schaffer, S. 2010. Effect of beta-alanine treatment on mitochondrial taurine level and 5-taurinomethyluridine content. J Biomed Sci 17(Suppl 1), S25.
    • (2010) J Biomed Sci , vol.17 , pp. S25
    • Jong, C.J.1    Ito, T.2    Mozaffari, M.3    Azuma, J.4    Schaffer, S.5
  • 67
    • 84862264118 scopus 로고    scopus 로고
    • Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production
    • Jong, C.J., Azuma, J. & Schaffer, S. 2012. Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production. Amino Acids 42, 2223–2232.
    • (2012) Amino Acids , vol.42 , pp. 2223-2232
    • Jong, C.J.1    Azuma, J.2    Schaffer, S.3
  • 68
    • 84874807416 scopus 로고    scopus 로고
    • Double mutation at the putative protein kinase C phosphorylation sites Thr151 plus Thr323 in the mouse leukotrieneD4 receptor eliminates homologous desensitization
    • Jorgensen, S.T., Eriksen, H.N., Dausell, J., Jespersen, T., Lambert, I.H. & Hoffmann, E.K. 2013. Double mutation at the putative protein kinase C phosphorylation sites Thr151 plus Thr323 in the mouse leukotrieneD4 receptor eliminates homologous desensitization. Cell Physiol Biochem 31, 366–378.
    • (2013) Cell Physiol Biochem , vol.31 , pp. 366-378
    • Jorgensen, S.T.1    Eriksen, H.N.2    Dausell, J.3    Jespersen, T.4    Lambert, I.H.5    Hoffmann, E.K.6
  • 70
    • 0842301309 scopus 로고    scopus 로고
    • Inhibition of release of taurine and excitatory amino acids in ischemia and neuroprotection
    • Kimelberg, H.K., Nestor, N.B. & Feustel, P.J. 2004. Inhibition of release of taurine and excitatory amino acids in ischemia and neuroprotection. Neurochem Res 29, 267–274.
    • (2004) Neurochem Res , vol.29 , pp. 267-274
    • Kimelberg, H.K.1    Nestor, N.B.2    Feustel, P.J.3
  • 71
    • 33749355316 scopus 로고    scopus 로고
    • Cholesterol modulates the volume-regulated anion current in Ehrlich-Lettre ascites cells via effects on Rho and F-actin
    • Klausen, T.K., Hougaard, C., Hoffmann, E.K. & Pedersen, S.F. 2006. Cholesterol modulates the volume-regulated anion current in Ehrlich-Lettre ascites cells via effects on Rho and F-actin. Am J Physiol Cell Physiol 291, C757–C771.
    • (2006) Am J Physiol Cell Physiol , vol.291 , pp. C757-C771
    • Klausen, T.K.1    Hougaard, C.2    Hoffmann, E.K.3    Pedersen, S.F.4
  • 72
    • 0018243603 scopus 로고
    • Taurine: an essential nutrient for the cat
    • Knopf, K., Sturman, J.A., Armstrong, M. & Hayes, K.C. 1978. Taurine: an essential nutrient for the cat. J Nutr 108, 773–778.
    • (1978) J Nutr , vol.108 , pp. 773-778
    • Knopf, K.1    Sturman, J.A.2    Armstrong, M.3    Hayes, K.C.4
  • 73
    • 18344401810 scopus 로고
    • [On pH dependibility of transport of neutral amino acids in Ehrlich ascites tumor cells]
    • Kromphardt, H. 1965. [On pH dependibility of transport of neutral amino acids in Ehrlich ascites tumor cells]. Biochem Z 343, 283–293.
    • (1965) Biochem Z , vol.343 , pp. 283-293
    • Kromphardt, H.1
  • 74
    • 0017798929 scopus 로고
    • The identification of taurine receptors from rat heart sarcolemma
    • Kulakowski, E.C., Maturo, J. & Schaffer, S.W. 1978. The identification of taurine receptors from rat heart sarcolemma. Biochem Biophys Res Commun 80, 936–941.
    • (1978) Biochem Biophys Res Commun , vol.80 , pp. 936-941
    • Kulakowski, E.C.1    Maturo, J.2    Schaffer, S.W.3
  • 75
    • 0019847990 scopus 로고
    • Solubilization and characterization of cardiac sarcolemmal taurine-binding proteins
    • Kulakowski, E.C., Maturo, J. & Schaffer, S.W. 1981. Solubilization and characterization of cardiac sarcolemmal taurine-binding proteins. Arch Biochem Biophys 210, 204–209.
    • (1981) Arch Biochem Biophys , vol.210 , pp. 204-209
    • Kulakowski, E.C.1    Maturo, J.2    Schaffer, S.W.3
  • 76
    • 0023444302 scopus 로고
    • Biosynthesis of taurine peptides in brain cytoplasmic fraction in vitro
    • Lahdesmaki, P. 1987. Biosynthesis of taurine peptides in brain cytoplasmic fraction in vitro. Int J Neurosci 37, 79–84.
    • (1987) Int J Neurosci , vol.37 , pp. 79-84
    • Lahdesmaki, P.1
  • 79
    • 0001643625 scopus 로고
    • Na-dependent taurine uptake in Ehrlich ascites tumor cells
    • Lambert, I.H. 1984. Na-dependent taurine uptake in Ehrlich ascites tumor cells. Mol Physiol 6, 233–246.
    • (1984) Mol Physiol , vol.6 , pp. 233-246
    • Lambert, I.H.1
  • 80
    • 0021792259 scopus 로고
    • Taurine transport in Ehrlich ascites tumour cells Specificity and chloride dependence
    • Lambert, I.H. 1985. Taurine transport in Ehrlich ascites tumour cells Specificity and chloride dependence. Mol Physiol 7, 323–332.
    • (1985) Mol Physiol , vol.7 , pp. 323-332
    • Lambert, I.H.1
  • 81
    • 0023081406 scopus 로고
    • Effect of arachidonic acid, fatty acids, prostaglandins, and leukotrienes on volume regulation in Ehrlich ascites tumor cells
    • Lambert, I.H. 1987. Effect of arachidonic acid, fatty acids, prostaglandins, and leukotrienes on volume regulation in Ehrlich ascites tumor cells. J Membr Biol 98, 207–221.
    • (1987) J Membr Biol , vol.98 , pp. 207-221
    • Lambert, I.H.1
  • 82
    • 0442296909 scopus 로고
    • Effect of arachidonic acid on conductive Na, K and anion transport in Ehrlich ascites tumor cells under isotonic and hypotonic conditions
    • Lambert, I.H. 1991. Effect of arachidonic acid on conductive Na, K and anion transport in Ehrlich ascites tumor cells under isotonic and hypotonic conditions. Cell Physiol Biochem 1, 177–194.
    • (1991) Cell Physiol Biochem , vol.1 , pp. 177-194
    • Lambert, I.H.1
  • 83
    • 0031837948 scopus 로고    scopus 로고
    • Regulation of the taurine content in Ehrlich ascites tumour cells
    • Lambert, I.H. 1998. Regulation of the taurine content in Ehrlich ascites tumour cells. Adv Exp Med Biol 442, 269–276.
    • (1998) Adv Exp Med Biol , vol.442 , pp. 269-276
    • Lambert, I.H.1
  • 84
    • 0042931146 scopus 로고    scopus 로고
    • Reactive oxygen species regulate swelling-induced taurine efflux in NIH3T3 mouse fibroblasts
    • Lambert, I.H. 2003a. Reactive oxygen species regulate swelling-induced taurine efflux in NIH3T3 mouse fibroblasts. J Membr Biol 192, 19–32.
    • (2003) J Membr Biol , vol.192 , pp. 19-32
    • Lambert, I.H.1
  • 85
    • 1542568452 scopus 로고    scopus 로고
    • Regulation of the volume-sensitive taurine efflux pathway in NIH3T3 mouse fibroblasts
    • J.B. Lombardini, S.W. Schaffer, &, J. Azuma, (eds), Academic/Plenum Publisher, New York
    • Lambert, I.H. 2003b. Regulation of the volume-sensitive taurine efflux pathway in NIH3T3 mouse fibroblasts. In: J.B. Lombardini, S.W. Schaffer & J. Azuma (eds) Taurine in the 21st Century, pp. 115–122. Academic/Plenum Publisher, New York.
    • (2003) Taurine in the 21st Century , pp. 115-122
    • Lambert, I.H.1
  • 86
    • 0442326342 scopus 로고    scopus 로고
    • Regulation of the cellular content of the organic osmolyte taurine in mammalian cells
    • Lambert, I.H. 2004. Regulation of the cellular content of the organic osmolyte taurine in mammalian cells. Neurochem Res 29, 27–63.
    • (2004) Neurochem Res , vol.29 , pp. 27-63
    • Lambert, I.H.1
  • 87
    • 34547101967 scopus 로고    scopus 로고
    • Activation and inactivation of the volume-sensitive taurine leak pathway in NIH3T3 fibroblasts and Ehrlich Lettre acites cells
    • Lambert, I.H. 2007. Activation and inactivation of the volume-sensitive taurine leak pathway in NIH3T3 fibroblasts and Ehrlich Lettre acites cells. Am J Physiol Cell Physiol 293, C390–C400.
    • (2007) Am J Physiol Cell Physiol , vol.293 , pp. C390-C400
    • Lambert, I.H.1
  • 88
    • 0033854466 scopus 로고    scopus 로고
    • Lysophosphatidylcholine induces taurine release from HeLa cells
    • Lambert, I.H. & Falktoft, B. 2000. Lysophosphatidylcholine induces taurine release from HeLa cells. J Membr Biol 176, 175–185.
    • (2000) J Membr Biol , vol.176 , pp. 175-185
    • Lambert, I.H.1    Falktoft, B.2
  • 89
    • 0034798392 scopus 로고    scopus 로고
    • Lysophosphatidylcholine-induced taurine release in HeLa cells involves protein kinase activity
    • Lambert, I.H. & Falktoft, B. 2001. Lysophosphatidylcholine-induced taurine release in HeLa cells involves protein kinase activity. Comp Biochem Physiol A Mol Integr Physiol 130, 577–584.
    • (2001) Comp Biochem Physiol A Mol Integr Physiol , vol.130 , pp. 577-584
    • Lambert, I.H.1    Falktoft, B.2
  • 90
    • 83755186689 scopus 로고    scopus 로고
    • Regulation of taurine transport systems by protein kinase CK2 in mammalian cells
    • Lambert, I.H. & Hansen, D.B. 2011. Regulation of taurine transport systems by protein kinase CK2 in mammalian cells. Cell Physiol Biochem 28, 1099–1110.
    • (2011) Cell Physiol Biochem , vol.28 , pp. 1099-1110
    • Lambert, I.H.1    Hansen, D.B.2
  • 91
    • 0020409344 scopus 로고
    • Amino acid metabolism and protein turnover under different osmotic conditions in Ehrlich ascites tumor cells
    • Lambert, I.H. & Hoffmann, E.K. 1982. Amino acid metabolism and protein turnover under different osmotic conditions in Ehrlich ascites tumor cells. Mol Physiol 2, 273–286.
    • (1982) Mol Physiol , vol.2 , pp. 273-286
    • Lambert, I.H.1    Hoffmann, E.K.2
  • 92
    • 0027534417 scopus 로고
    • Regulation of taurine transport in Ehrlich ascites tumor cells
    • Lambert, I.H. & Hoffmann, E.K. 1993. Regulation of taurine transport in Ehrlich ascites tumor cells. J Membr Biol 131, 67–79.
    • (1993) J Membr Biol , vol.131 , pp. 67-79
    • Lambert, I.H.1    Hoffmann, E.K.2
  • 94
    • 55949120166 scopus 로고    scopus 로고
    • Cell volume regulation: physiology and pathophysiology
    • Lambert, I.H., Hoffmann, E.K. & Pedersen, S.F. 2008. Cell volume regulation: physiology and pathophysiology. Acta Physiol Scand 194, 255–282.
    • (2008) Acta Physiol Scand , vol.194 , pp. 255-282
    • Lambert, I.H.1    Hoffmann, E.K.2    Pedersen, S.F.3
  • 95
    • 84901747390 scopus 로고    scopus 로고
    • mTOR ensures increased release and reduced uptake of the organic osmolyte taurine under hypoosmotic conditions in mouse fibroblasts
    • Lambert, I.H., Jensen, J.V. & Pedersen, P.A. 2014. mTOR ensures increased release and reduced uptake of the organic osmolyte taurine under hypoosmotic conditions in mouse fibroblasts. Am J Physiol Cell Physiol 306, C1028–C1040.
    • (2014) Am J Physiol Cell Physiol , vol.306 , pp. C1028-C1040
    • Lambert, I.H.1    Jensen, J.V.2    Pedersen, P.A.3
  • 96
    • 84868117000 scopus 로고    scopus 로고
    • Role of ion transport in control of apoptotic cell death
    • Lang, F. & Hoffmann, E.K. 2012. Role of ion transport in control of apoptotic cell death. Compr Physiol 2, 2037–2061.
    • (2012) Compr Physiol , vol.2 , pp. 2037-2061
    • Lang, F.1    Hoffmann, E.K.2
  • 97
    • 0034061029 scopus 로고    scopus 로고
    • The involvement of caspases in the CD95(Fas/Apo-1) but not swelling-induced cellular taurine release from Jurkat T-lymphocytes
    • Lang, F., Madlung, J., Siemen, D., Ellory, C., Lepple-Wienhues, A. & Gulbins, E. 2000. The involvement of caspases in the CD95(Fas/Apo-1) but not swelling-induced cellular taurine release from Jurkat T-lymphocytes. Pflugers Arch 440, 93–99.
    • (2000) Pflugers Arch , vol.440 , pp. 93-99
    • Lang, F.1    Madlung, J.2    Siemen, D.3    Ellory, C.4    Lepple-Wienhues, A.5    Gulbins, E.6
  • 100
    • 79960281458 scopus 로고    scopus 로고
    • GABA(A) receptor and glycine receptor activation by paracrine/autocrine release of endogenous agonists: more than a simple communication pathway
    • Le-Corronc, H., Rigo, J.M., Branchereau, P. & Legendre, P. 2011. GABA(A) receptor and glycine receptor activation by paracrine/autocrine release of endogenous agonists: more than a simple communication pathway. Mol Neurobiol 44, 28–52.
    • (2011) Mol Neurobiol , vol.44 , pp. 28-52
    • Le-Corronc, H.1    Rigo, J.M.2    Branchereau, P.3    Legendre, P.4
  • 101
    • 0025769896 scopus 로고
    • Inhibition by taurine of the phosphorylation of specific synaptosomal proteins in the rat cortex: effects of taurine on the stimulation of calcium uptake in mitochondria and inhibition of phosphoinositide turnover
    • Li, Y.P. & Lombardini, J.B. 1991. Inhibition by taurine of the phosphorylation of specific synaptosomal proteins in the rat cortex: effects of taurine on the stimulation of calcium uptake in mitochondria and inhibition of phosphoinositide turnover. Brain Res 553, 89–96.
    • (1991) Brain Res , vol.553 , pp. 89-96
    • Li, Y.P.1    Lombardini, J.B.2
  • 102
    • 84874122566 scopus 로고    scopus 로고
    • Targeting mitochondrial reactive oxygen species as novel therapy for inflammatory diseases and cancers
    • Li, X., Fang, P., Mai, J., Choi, E.T., Wang, H. & Yang, X.F. 2013. Targeting mitochondrial reactive oxygen species as novel therapy for inflammatory diseases and cancers. J Hematol Oncol 6, 19.
    • (2013) J Hematol Oncol , vol.6 , pp. 19
    • Li, X.1    Fang, P.2    Mai, J.3    Choi, E.T.4    Wang, H.5    Yang, X.F.6
  • 103
    • 84878802041 scopus 로고    scopus 로고
    • Inhibitory effects of taurine on STZ-induced apoptosis of pancreatic islet cells
    • Lin, S., Yang, J., Wu, G., Liu, M., Lv, Q., Yang, Q. & Hu, J. 2013. Inhibitory effects of taurine on STZ-induced apoptosis of pancreatic islet cells. Adv Exp Med Biol 775, 287–297.
    • (2013) Adv Exp Med Biol , vol.775 , pp. 287-297
    • Lin, S.1    Yang, J.2    Wu, G.3    Liu, M.4    Lv, Q.5    Yang, Q.6    Hu, J.7
  • 104
    • 0027102017 scopus 로고
    • Cloning and expression of a cDNA encoding the transporter of taurine and beta-alanine in mouse brain
    • Liu, Q.R., Lopez-Corcuera, B., Nelson, H., Mandiyan, S. & Nelson, N. 1992. Cloning and expression of a cDNA encoding the transporter of taurine and beta-alanine in mouse brain. Proc Natl Acad Sci USA 89, 12145–12149.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12145-12149
    • Liu, Q.R.1    Lopez-Corcuera, B.2    Nelson, H.3    Mandiyan, S.4    Nelson, N.5
  • 105
    • 0031810199 scopus 로고    scopus 로고
    • Increased phosphorylation of specific rat cardiac and retinal proteins in taurine-depleted animals: isolation and identification of the phosphoproteins
    • Lombardini, J.B. 1998. Increased phosphorylation of specific rat cardiac and retinal proteins in taurine-depleted animals: isolation and identification of the phosphoproteins. Adv Exp Med Biol 442, 441–447.
    • (1998) Adv Exp Med Biol , vol.442 , pp. 441-447
    • Lombardini, J.B.1
  • 106
    • 84891136849 scopus 로고    scopus 로고
    • Congenital taurine deficiency in mice is associated with reduced sensitivity to nociceptive chemical stimulation
    • Lotsch, J., Hummel, T., Warskulat, U., Coste, O., Haussinger, D., Geisslinger, G. & Tegeder, I. 2014. Congenital taurine deficiency in mice is associated with reduced sensitivity to nociceptive chemical stimulation. Neuroscience 259, 63–70.
    • (2014) Neuroscience , vol.259 , pp. 63-70
    • Lotsch, J.1    Hummel, T.2    Warskulat, U.3    Coste, O.4    Haussinger, D.5    Geisslinger, G.6    Tegeder, I.7
  • 107
    • 13544259553 scopus 로고    scopus 로고
    • Taurine attenuates CD3/interleukin-2-induced T cell apoptosis in an in vitro model of activation-induced cell death (AICD)
    • Maher, S.G., Condron, C.E.M., Bouchier-Hayes, D.J. & Toomey, D.M. 2005. Taurine attenuates CD3/interleukin-2-induced T cell apoptosis in an in vitro model of activation-induced cell death (AICD). Clin Exp Immunol 139, 279–286.
    • (2005) Clin Exp Immunol , vol.139 , pp. 279-286
    • Maher, S.G.1    Condron, C.E.M.2    Bouchier-Hayes, D.J.3    Toomey, D.M.4
  • 108
    • 0021686172 scopus 로고
    • Mass spectrometric analyses of brain synaptic peptides containing taurine
    • Marnela, K.M., Timonen, M. & Lahdesmaki, P. 1984. Mass spectrometric analyses of brain synaptic peptides containing taurine. J Neurochem 43, 1650–1653.
    • (1984) J Neurochem , vol.43 , pp. 1650-1653
    • Marnela, K.M.1    Timonen, M.2    Lahdesmaki, P.3
  • 109
    • 0018645334 scopus 로고
    • High affinity transport of taurine and beta-alanine and low affinity transport of gamma-aminobutyric acid by a single transport system in cultured glioma cells
    • Martin, D.L. & Shain, W. 1979. High affinity transport of taurine and beta-alanine and low affinity transport of gamma-aminobutyric acid by a single transport system in cultured glioma cells. J Biol Chem 254, 7076–7084.
    • (1979) J Biol Chem , vol.254 , pp. 7076-7084
    • Martin, D.L.1    Shain, W.2
  • 110
    • 35148878173 scopus 로고    scopus 로고
    • Taurine intestinal absorption and renal excretion test in diabetic patients: a pilot study
    • Merheb, M., Daher, R.T., Nasrallah, M., Sabra, R., Ziyadeh, F.N. & Barada, K. 2007. Taurine intestinal absorption and renal excretion test in diabetic patients: a pilot study. Diabetes Care 30, 2652–2654.
    • (2007) Diabetes Care , vol.30 , pp. 2652-2654
    • Merheb, M.1    Daher, R.T.2    Nasrallah, M.3    Sabra, R.4    Ziyadeh, F.N.5    Barada, K.6
  • 111
    • 0027353724 scopus 로고
    • Gamma-aminobutyric acid and the liver
    • Minuk, G.Y. 1993. Gamma-aminobutyric acid and the liver. Dig Dis 11, 45–54.
    • (1993) Dig Dis , vol.11 , pp. 45-54
    • Minuk, G.Y.1
  • 112
    • 0024363203 scopus 로고
    • Active transport of taurine in rabbit jejunal brush-border membrane vesicles
    • Miyamoto, Y., Tiruppathi, C., Ganapathy, V. & Leibach, F.H. 1989. Active transport of taurine in rabbit jejunal brush-border membrane vesicles. Am J Physiol 257, G65–G72.
    • (1989) Am J Physiol , vol.257 , pp. G65-G72
    • Miyamoto, Y.1    Tiruppathi, C.2    Ganapathy, V.3    Leibach, F.H.4
  • 113
    • 16444383251 scopus 로고    scopus 로고
    • Regulation of the human taurine transporter by TNF-alpha and an anti-inflammatory function of taurine in human intestinal Caco-2 cells
    • Mochizuki, T., Satsu, H., Nakano, T. & Shimizu, M. 2004. Regulation of the human taurine transporter by TNF-alpha and an anti-inflammatory function of taurine in human intestinal Caco-2 cells. BioFactors 21, 141–144.
    • (2004) BioFactors , vol.21 , pp. 141-144
    • Mochizuki, T.1    Satsu, H.2    Nakano, T.3    Shimizu, M.4
  • 114
    • 0029930870 scopus 로고    scopus 로고
    • Phosphorylation is involved in the regulation of the taurine influx via the beta-system in Ehrlich ascites tumor cells
    • Mollerup, J. & Lambert, I.H. 1996. Phosphorylation is involved in the regulation of the taurine influx via the beta-system in Ehrlich ascites tumor cells. J Membr Biol 150, 73–82.
    • (1996) J Membr Biol , vol.150 , pp. 73-82
    • Mollerup, J.1    Lambert, I.H.2
  • 115
    • 0032574949 scopus 로고    scopus 로고
    • +-coupled taurine transport in Ehrlich ascites tumour cells
    • +-coupled taurine transport in Ehrlich ascites tumour cells. Biochim Biophys Acta 1371, 335–344.
    • (1998) Biochim Biophys Acta , vol.1371 , pp. 335-344
    • Mollerup, J.1    Lambert, I.H.2
  • 116
    • 84879580492 scopus 로고    scopus 로고
    • Potential link between cysteinyl-leukotriene receptors and release of bioactive amino acids in regulation of lung function. Focus on “Volume-sensitive release of organic osmolytes in the human lung epithelial cell line A549: role of the 5-lipoxygenase”
    • Mongin, A.A. 2013. Potential link between cysteinyl-leukotriene receptors and release of bioactive amino acids in regulation of lung function. Focus on “Volume-sensitive release of organic osmolytes in the human lung epithelial cell line A549: role of the 5-lipoxygenase”. Am J Physiol Cell Physiol 305, C24–C25.
    • (2013) Am J Physiol Cell Physiol , vol.305 , pp. C24-C25
    • Mongin, A.A.1
  • 117
    • 0033127924 scopus 로고    scopus 로고
    • [3H]taurine and D-[3H]aspartate release from astrocyte cultures are differently regulated by tyrosine kinases
    • Mongin, A.A., Reddi, J.M., Charniga, C. & Kimelberg, H.K. 1999. [3H]taurine and D-[3H]aspartate release from astrocyte cultures are differently regulated by tyrosine kinases. Am J Physiol 276, C1226–C1230.
    • (1999) Am J Physiol , vol.276 , pp. C1226-C1230
    • Mongin, A.A.1    Reddi, J.M.2    Charniga, C.3    Kimelberg, H.K.4
  • 118
    • 0030739658 scopus 로고    scopus 로고
    • Volume regulation in NIH/3T3 cells not expressing P-glycoprotein. II. Chloride and amino acid fluxes
    • Moran, J., Miranda, D., Pena-Segura, C. & Pasantes-Morales, H. 1997. Volume regulation in NIH/3T3 cells not expressing P-glycoprotein. II. Chloride and amino acid fluxes. Am J Physiol 272, C1804–C1809.
    • (1997) Am J Physiol , vol.272 , pp. C1804-C1809
    • Moran, J.1    Miranda, D.2    Pena-Segura, C.3    Pasantes-Morales, H.4
  • 119
    • 77956026508 scopus 로고    scopus 로고
    • Taurine in morning spot urine for the useful assessment of dietary seafood intake in Japanese children and adolescents
    • Mori, M., Mori, H., Hamada, A. & Yamori, Y. 2010. Taurine in morning spot urine for the useful assessment of dietary seafood intake in Japanese children and adolescents. J Biomed Sci 17(Suppl 1), S43.
    • (2010) J Biomed Sci , vol.17 , pp. S43
    • Mori, M.1    Mori, H.2    Hamada, A.3    Yamori, Y.4
  • 120
    • 74849126625 scopus 로고    scopus 로고
    • Roles of NADPH oxidase in occurrence of gastric damage and expression of cyclooxygenase-2 during ischemia/reperfusion in rat stomachs
    • Nakagiri, A. & Murakami, M. 2009. Roles of NADPH oxidase in occurrence of gastric damage and expression of cyclooxygenase-2 during ischemia/reperfusion in rat stomachs. J Pharmacol Sci 111, 352–360.
    • (2009) J Pharmacol Sci , vol.111 , pp. 352-360
    • Nakagiri, A.1    Murakami, M.2
  • 121
    • 0038246445 scopus 로고    scopus 로고
    • The effect of taurine on the cholesterol metabolism in rats fed diets supplemented with cholestyramine or high amounts of bile acid
    • Nishimura, N., Umeda, C., Oda, H. & Yokogoshi, H. 2003. The effect of taurine on the cholesterol metabolism in rats fed diets supplemented with cholestyramine or high amounts of bile acid. J Nutr Sci Vitaminol (Tokyo) 49, 21–26.
    • (2003) J Nutr Sci Vitaminol (Tokyo) , vol.49 , pp. 21-26
    • Nishimura, N.1    Umeda, C.2    Oda, H.3    Yokogoshi, H.4
  • 122
    • 0035806896 scopus 로고    scopus 로고
    • Taurine prevents the decrease in expression and secretion of extracellular superoxide dismutase induced by homocysteine: amelioration of homocysteine-induced endoplasmic reticulum stress by taurine
    • Nonaka, H., Tsujino, T., Watari, Y., Emoto, N. & Yokoyama, M. 2001. Taurine prevents the decrease in expression and secretion of extracellular superoxide dismutase induced by homocysteine: amelioration of homocysteine-induced endoplasmic reticulum stress by taurine. Circulation 104, 1165–1170.
    • (2001) Circulation , vol.104 , pp. 1165-1170
    • Nonaka, H.1    Tsujino, T.2    Watari, Y.3    Emoto, N.4    Yokoyama, M.5
  • 123
    • 0031850059 scopus 로고    scopus 로고
    • Intrauterine growth restriction is associated with a reduced activity of placental taurine transporters
    • Norberg, S., Powell, T.L. & Jansson, T. 1998. Intrauterine growth restriction is associated with a reduced activity of placental taurine transporters. Pediatr Res 44, 233–238.
    • (1998) Pediatr Res , vol.44 , pp. 233-238
    • Norberg, S.1    Powell, T.L.2    Jansson, T.3
  • 124
    • 84871260456 scopus 로고    scopus 로고
    • Proton-assisted amino acid transporter PAT1 complexes with Rag GTPases and activates TORC1 on late endosomal and lysosomal membranes
    • Ogmundsdottir, M.H., Heublein, S., Kazi, S., Reynolds, B., Visvalingam, S.M., Shaw, M.K. & Goberdhan, D.C. 2012. Proton-assisted amino acid transporter PAT1 complexes with Rag GTPases and activates TORC1 on late endosomal and lysosomal membranes. PLoS ONE 7, e36616.
    • (2012) PLoS ONE , vol.7
    • Ogmundsdottir, M.H.1    Heublein, S.2    Kazi, S.3    Reynolds, B.4    Visvalingam, S.M.5    Shaw, M.K.6    Goberdhan, D.C.7
  • 125
    • 29544438892 scopus 로고    scopus 로고
    • Taurine prevents myocardial ischemia/reperfusion-induced oxidative stress and apoptosis in prolonged hypothermic rat heart preservation
    • Oriyanhan, W., Yamazaki, K., Miwa, S., Takaba, K., Ikeda, T. & Komeda, M. 2005. Taurine prevents myocardial ischemia/reperfusion-induced oxidative stress and apoptosis in prolonged hypothermic rat heart preservation. Heart Vessels 20, 278–285.
    • (2005) Heart Vessels , vol.20 , pp. 278-285
    • Oriyanhan, W.1    Yamazaki, K.2    Miwa, S.3    Takaba, K.4    Ikeda, T.5    Komeda, M.6
  • 127
    • 0038612957 scopus 로고    scopus 로고
    • Reactive oxygen species are important mediators of taurine release from skeletal muscle cells
    • Ørtenblad, N., Young, J.F., Oksbjerg, N., Nielsen, J.H. & Lambert, I.H. 2003. Reactive oxygen species are important mediators of taurine release from skeletal muscle cells. Am J Physiol 284, C1362–C1373.
    • (2003) Am J Physiol , vol.284 , pp. C1362-C1373
    • Ørtenblad, N.1    Young, J.F.2    Oksbjerg, N.3    Nielsen, J.H.4    Lambert, I.H.5
  • 129
    • 0027218528 scopus 로고
    • Taurine chloramine inhibits the synthesis of nitric oxide and the release of tumor necrosis factor in activated RAW 264.7 cells
    • Park, E., Quinn, M.R., Wright, C.E. & Schuller-Levis, G. 1993. Taurine chloramine inhibits the synthesis of nitric oxide and the release of tumor necrosis factor in activated RAW 264.7 cells. J Leukoc Biol 54, 119–124.
    • (1993) J Leukoc Biol , vol.54 , pp. 119-124
    • Park, E.1    Quinn, M.R.2    Wright, C.E.3    Schuller-Levis, G.4
  • 130
    • 84926471677 scopus 로고    scopus 로고
    • Development of a novel cysteine sulfinic acid decarboxylase knockout mouse: dietary taurine reduces neonatal mortality
    • Park, E., Park, S.Y., Dobkin, C. & Schuller-Levis, G. 2014. Development of a novel cysteine sulfinic acid decarboxylase knockout mouse: dietary taurine reduces neonatal mortality. J Amino Acids 2014, 346809.
    • (2014) J Amino Acids , vol.2014 , pp. 346809
    • Park, E.1    Park, S.Y.2    Dobkin, C.3    Schuller-Levis, G.4
  • 134
    • 0037098739 scopus 로고    scopus 로고
    • Rho family GTP binding proteins are involved in the regulatory volume decrease process in NIH3T3 mouse fibroblasts
    • Pedersen, S.F., Beisner, K.H., Hougaard, C., Willumsen, B.M., Lambert, I.H. & Hoffmann, E.K. 2002. Rho family GTP binding proteins are involved in the regulatory volume decrease process in NIH3T3 mouse fibroblasts. J Physiol 541, 779–796.
    • (2002) J Physiol , vol.541 , pp. 779-796
    • Pedersen, S.F.1    Beisner, K.H.2    Hougaard, C.3    Willumsen, B.M.4    Lambert, I.H.5    Hoffmann, E.K.6
  • 135
    • 77649172085 scopus 로고    scopus 로고
    • 5-Lipoxygenase inhibitors: a review of recent developments and patents
    • Pergola, C. & Werz, O. 2010. 5-Lipoxygenase inhibitors: a review of recent developments and patents. Expert Opin Ther Pat 20, 355–375.
    • (2010) Expert Opin Ther Pat , vol.20 , pp. 355-375
    • Pergola, C.1    Werz, O.2
  • 136
    • 0036278286 scopus 로고    scopus 로고
    • Downregulation of taurine uptake in multidrug resistant Ehrlich ascites tumor cells
    • Poulsen, K.A., Litman, T., Eriksen, J., Mollerup, J. & Lambert, I.H. 2002. Downregulation of taurine uptake in multidrug resistant Ehrlich ascites tumor cells. Amino Acids 22, 333–350.
    • (2002) Amino Acids , vol.22 , pp. 333-350
    • Poulsen, K.A.1    Litman, T.2    Eriksen, J.3    Mollerup, J.4    Lambert, I.H.5
  • 137
    • 36048952649 scopus 로고    scopus 로고
    • Induction of group VIA phospholipase A2 activity during in vitro ischemia in C2C12 myotubes is associated with changes in the level of its splice variants
    • Poulsen, K.A., Pedersen, S.F., Kolko, M. & Lambert, I.H. 2007. Induction of group VIA phospholipase A2 activity during in vitro ischemia in C2C12 myotubes is associated with changes in the level of its splice variants. Am J Physiol Cell Physiol 293, C1605–C1615.
    • (2007) Am J Physiol Cell Physiol , vol.293 , pp. C1605-C1615
    • Poulsen, K.A.1    Pedersen, S.F.2    Kolko, M.3    Lambert, I.H.4
  • 140
    • 0034694976 scopus 로고    scopus 로고
    • Molecular characterization of taurine transport in bovine aortic endothelial cells
    • Qian, X., Vinnakota, S., Edwards, C. & Sarkar, H.K. 2000. Molecular characterization of taurine transport in bovine aortic endothelial cells. Biochim Biophys Acta 1509, 324–334.
    • (2000) Biochim Biophys Acta , vol.1509 , pp. 324-334
    • Qian, X.1    Vinnakota, S.2    Edwards, C.3    Sarkar, H.K.4
  • 142
    • 77952312969 scopus 로고    scopus 로고
    • Regulation of the activity of 5-lipoxygenase, a key enzyme in leukotriene biosynthesis
    • Radmark, O. & Samuelsson, B. 2010. Regulation of the activity of 5-lipoxygenase, a key enzyme in leukotriene biosynthesis. Biochem Biophys Res Commun 396, 105–110.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 105-110
    • Radmark, O.1    Samuelsson, B.2
  • 143
    • 0028234290 scopus 로고
    • Molecular identity and calmodulin-mediated regulation of the taurine transporter in a human retinal pigment epithelial cell line
    • Ramamoorthy, S., Del Monte, M.A., Leibach, F.H. & Ganapathy, V. 1994. Molecular identity and calmodulin-mediated regulation of the taurine transporter in a human retinal pigment epithelial cell line. Curr Eye Res 13, 523–529.
    • (1994) Curr Eye Res , vol.13 , pp. 523-529
    • Ramamoorthy, S.1    Del Monte, M.A.2    Leibach, F.H.3    Ganapathy, V.4
  • 144
    • 84897083891 scopus 로고    scopus 로고
    • Multiple mechanisms mediate the taurine-induced proliferation of neural stem/progenitor cells from the subventricular zone of the adult mouse
    • Ramos-Mandujano, G., Hernandez-Benitez, R. & Pasantes-Morales, H. 2014. Multiple mechanisms mediate the taurine-induced proliferation of neural stem/progenitor cells from the subventricular zone of the adult mouse. Stem Cell Res 12, 690–702.
    • (2014) Stem Cell Res , vol.12 , pp. 690-702
    • Ramos-Mandujano, G.1    Hernandez-Benitez, R.2    Pasantes-Morales, H.3
  • 145
    • 0022474689 scopus 로고
    • Taurine concentrations in the diet, plasma, urine and breast milk of vegans compared with omnivores
    • Rana, S.K. & Sanders, T.A. 1986. Taurine concentrations in the diet, plasma, urine and breast milk of vegans compared with omnivores. Br J Nutr 56, 17–27.
    • (1986) Br J Nutr , vol.56 , pp. 17-27
    • Rana, S.K.1    Sanders, T.A.2
  • 148
    • 70349495362 scopus 로고    scopus 로고
    • Protection by taurine of rat brain cortical slices against oxygen glucose deprivation- and reoxygenation-induced damage
    • Ricci, L., Valoti, M., Sgaragli, G. & Frosini, M. 2009. Protection by taurine of rat brain cortical slices against oxygen glucose deprivation- and reoxygenation-induced damage. Eur J Pharmacol 621, 26–32.
    • (2009) Eur J Pharmacol , vol.621 , pp. 26-32
    • Ricci, L.1    Valoti, M.2    Sgaragli, G.3    Frosini, M.4
  • 150
    • 24644436850 scopus 로고    scopus 로고
    • Transepithelial taurine transport in caco-2 cell monolayers
    • Roig-Perez, S., Moreto, M. & Ferrer, R. 2005. Transepithelial taurine transport in caco-2 cell monolayers. J Membr Biol 204, 85–92.
    • (2005) J Membr Biol , vol.204 , pp. 85-92
    • Roig-Perez, S.1    Moreto, M.2    Ferrer, R.3
  • 151
    • 4644227801 scopus 로고    scopus 로고
    • Human placental taurine transporter in uncomplicated and IUGR pregnancies: cellular localization, protein expression, and regulation
    • Roos, S., Powell, T.L. & Jansson, T. 2004. Human placental taurine transporter in uncomplicated and IUGR pregnancies: cellular localization, protein expression, and regulation. Am J Physiol Regul Integr Comp Physiol 287, R886–R893.
    • (2004) Am J Physiol Regul Integr Comp Physiol , vol.287 , pp. R886-R893
    • Roos, S.1    Powell, T.L.2    Jansson, T.3
  • 152
    • 58349106216 scopus 로고    scopus 로고
    • Regulation of placental amino acid transporter activity by mammalian target of rapamycin
    • Roos, S., Kanai, Y., Prasad, P.D., Powell, T.L. & Jansson, T. 2009. Regulation of placental amino acid transporter activity by mammalian target of rapamycin. Am J Physiol Cell Physiol 296, C142–C150.
    • (2009) Am J Physiol Cell Physiol , vol.296 , pp. C142-C150
    • Roos, S.1    Kanai, Y.2    Prasad, P.D.3    Powell, T.L.4    Jansson, T.5
  • 154
    • 0024598132 scopus 로고
    • Taurine uptake by glial cells in the bullfrog symphathetic ganglia
    • Sakai, S., Tosake, T., Tasaka, J., Hashigushi, T. & Yoshihama, I. 1989. Taurine uptake by glial cells in the bullfrog symphathetic ganglia. Neurochem Int 14, 193–198.
    • (1989) Neurochem Int , vol.14 , pp. 193-198
    • Sakai, S.1    Tosake, T.2    Tasaka, J.3    Hashigushi, T.4    Yoshihama, I.5
  • 155
    • 0026741657 scopus 로고
    • Changes in taurine transport evoked by hyperosmolarity in cultured astrocytes
    • Sanchez-Olea, R., Moran, J. & Pasantes-Morales, H. 1992. Changes in taurine transport evoked by hyperosmolarity in cultured astrocytes. J Neurosci Res 32, 86–92.
    • (1992) J Neurosci Res , vol.32 , pp. 86-92
    • Sanchez-Olea, R.1    Moran, J.2    Pasantes-Morales, H.3
  • 156
    • 0032487633 scopus 로고    scopus 로고
    • Mechanisms of ischemia-induced taurine release in mouse hippocampal slices
    • Saransaari, P. & Oja, S.S. 1998. Mechanisms of ischemia-induced taurine release in mouse hippocampal slices. Brain Res 807, 118–124.
    • (1998) Brain Res , vol.807 , pp. 118-124
    • Saransaari, P.1    Oja, S.S.2
  • 157
    • 1542778732 scopus 로고    scopus 로고
    • Electrophysiological properties of the mouse Na+/Cl(−)-dependent taurine transporter (mTauT-1): steady-state kinetics: stoichiometry of taurine transport
    • Sarkar, H.K., Wright, E.M., Boorer, K.J. & Loo, D.D. 2003. Electrophysiological properties of the mouse Na+/Cl(−)-dependent taurine transporter (mTauT-1): steady-state kinetics: stoichiometry of taurine transport. Adv Exp Med Biol 526, 197–204.
    • (2003) Adv Exp Med Biol , vol.526 , pp. 197-204
    • Sarkar, H.K.1    Wright, E.M.2    Boorer, K.J.3    Loo, D.D.4
  • 158
    • 0019753853 scopus 로고
    • Taurine transport by reconstituted membrane vesicles
    • Schaffer, S.W., Kulakowski, E.C. & Kramer, J.H. 1981. Taurine transport by reconstituted membrane vesicles. Adv Exp Med Biol 139, 143–160.
    • (1981) Adv Exp Med Biol , vol.139 , pp. 143-160
    • Schaffer, S.W.1    Kulakowski, E.C.2    Kramer, J.H.3
  • 159
    • 0028073565 scopus 로고
    • Mechanisms underlying physiological and pharmacological actions of taurine on myocardial calcium transport
    • Schaffer, S.W., Ballard, C. & Azuma, J. 1994. Mechanisms underlying physiological and pharmacological actions of taurine on myocardial calcium transport. Adv Exp Med Biol 359, 171–180.
    • (1994) Adv Exp Med Biol , vol.359 , pp. 171-180
    • Schaffer, S.W.1    Ballard, C.2    Azuma, J.3
  • 161
    • 77956022823 scopus 로고    scopus 로고
    • Physiological roles of taurine in heart and muscle
    • Schaffer, S.W., Jong, C.J., Ramila, K.C. & Azuma, J. 2010. Physiological roles of taurine in heart and muscle. J Biomed Sci 17(Suppl 1), S2.
    • (2010) J Biomed Sci , vol.17 , pp. S2
    • Schaffer, S.W.1    Jong, C.J.2    Ramila, K.C.3    Azuma, J.4
  • 162
    • 84893295882 scopus 로고    scopus 로고
    • Effect of taurine on ischemia-reperfusion injury
    • Schaffer, S.W., Jong, C.J., Ito, T. & Azuma, J. 2014. Effect of taurine on ischemia-reperfusion injury. Amino Acids 46, 21–30.
    • (2014) Amino Acids , vol.46 , pp. 21-30
    • Schaffer, S.W.1    Jong, C.J.2    Ito, T.3    Azuma, J.4
  • 163
    • 34548052424 scopus 로고    scopus 로고
    • Translation matters: protein synthesis defects in inherited disease
    • Scheper, G.C., van der Knaap, M.S. & Proud, C.G. 2007. Translation matters: protein synthesis defects in inherited disease. Nat Rev Genet 8, 711–723.
    • (2007) Nat Rev Genet , vol.8 , pp. 711-723
    • Scheper, G.C.1    van der Knaap, M.S.2    Proud, C.G.3
  • 164
    • 0642285743 scopus 로고    scopus 로고
    • Taurine: new implications for an old amino acid
    • Schuller-Levis, G.B. & Park, E. 2003. Taurine: new implications for an old amino acid. FEMS Microbiol Lett 226, 195–202.
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 195-202
    • Schuller-Levis, G.B.1    Park, E.2
  • 165
    • 0033667679 scopus 로고    scopus 로고
    • Physiological significance of taurine and the taurine transporter in intestinal epithelial cells
    • Shimizu, M. & Satsu, H. 2000. Physiological significance of taurine and the taurine transporter in intestinal epithelial cells. Amino Acids 19, 605–614.
    • (2000) Amino Acids , vol.19 , pp. 605-614
    • Shimizu, M.1    Satsu, H.2
  • 168
    • 0842344402 scopus 로고    scopus 로고
    • Role of the liver in regulation of body cysteine and taurine levels: a brief review
    • Stipanuk, M.H. 2004. Role of the liver in regulation of body cysteine and taurine levels: a brief review. Neurochem Res 29, 105–110.
    • (2004) Neurochem Res , vol.29 , pp. 105-110
    • Stipanuk, M.H.1
  • 169
    • 0036845192 scopus 로고    scopus 로고
    • Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels
    • Stipanuk, M.H., Londono, M., Lee, J.I., Hu, M. & Yu, A.F. 2002. Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels. J Nutr 132, 3369–3378.
    • (2002) J Nutr , vol.132 , pp. 3369-3378
    • Stipanuk, M.H.1    Londono, M.2    Lee, J.I.3    Hu, M.4    Yu, A.F.5
  • 170
    • 33646807833 scopus 로고    scopus 로고
    • Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism
    • Stipanuk, M.H., Dominy, J.E. Jr, Lee, J.I. & Coloso, R.M. 2006. Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism. J Nutr 136, 1652S–1659S.
    • (2006) J Nutr , vol.136 , pp. 1652S-1659S
    • Stipanuk, M.H.1    Dominy, J.E.2    Lee, J.I.3    Coloso, R.M.4
  • 171
    • 0026262114 scopus 로고
    • Dietary taurine and feline reproduction and development
    • Sturman, J.A. 1991. Dietary taurine and feline reproduction and development. J Nutr 121, S166–S170.
    • (1991) J Nutr , vol.121 , pp. S166-S170
    • Sturman, J.A.1
  • 172
    • 0027497781 scopus 로고
    • Taurine in development
    • Sturman, J.A. 1993. Taurine in development. Physiol Rev 73, 119–147.
    • (1993) Physiol Rev , vol.73 , pp. 119-147
    • Sturman, J.A.1
  • 173
    • 34848841763 scopus 로고    scopus 로고
    • Specific timing of taurine supplementation affects learning ability in mice
    • Suge, R., Hosoe, N., Furube, M., Yamamoto, T., Hirayama, A., Hirano, S. & Nomura, M. 2007. Specific timing of taurine supplementation affects learning ability in mice. Life Sci 81, 1228–1234.
    • (2007) Life Sci , vol.81 , pp. 1228-1234
    • Suge, R.1    Hosoe, N.2    Furube, M.3    Yamamoto, T.4    Hirayama, A.5    Hirano, S.6    Nomura, M.7
  • 174
    • 0037011177 scopus 로고    scopus 로고
    • Taurine as a constituent of mitochondrial tRNAs: new insights into the functions of taurine and human mitochondrial diseases
    • Suzuki, T., Suzuki, T., Wada, T., Saigo, K. & Watanabe, K. 2002. Taurine as a constituent of mitochondrial tRNAs: new insights into the functions of taurine and human mitochondrial diseases. EMBO J 21, 6581–6589.
    • (2002) EMBO J , vol.21 , pp. 6581-6589
    • Suzuki, T.1    Suzuki, T.2    Wada, T.3    Saigo, K.4    Watanabe, K.5
  • 175
    • 0037377561 scopus 로고    scopus 로고
    • Taurine transporter in primary cultured neonatal rat heart cells: a comparison between cardiac myocytes and nonmyocytes
    • Takahashi, K., Azuma, M., Yamada, T., Ohyabu, Y., Takahashi, K., Schaffer, S.W. & Azuma, J. 2003a. Taurine transporter in primary cultured neonatal rat heart cells: a comparison between cardiac myocytes and nonmyocytes. Biochem Pharmacol 65, 1181–1187.
    • (2003) Biochem Pharmacol , vol.65 , pp. 1181-1187
    • Takahashi, K.1    Azuma, M.2    Yamada, T.3    Ohyabu, Y.4    Takahashi, K.5    Schaffer, S.W.6    Azuma, J.7
  • 178
    • 0034607267 scopus 로고    scopus 로고
    • A hyperosmotic stress-induced mRNA of carp cell encodes Na(+)- and Cl(−)-dependent high affinity taurine transporter
    • Takeuchi, K., Toyohara, H. & Sakaguchi, M. 2000. A hyperosmotic stress-induced mRNA of carp cell encodes Na(+)- and Cl(−)-dependent high affinity taurine transporter. Biochim Biophys Acta 1464, 219–230.
    • (2000) Biochim Biophys Acta , vol.1464 , pp. 219-230
    • Takeuchi, K.1    Toyohara, H.2    Sakaguchi, M.3
  • 181
    • 42649095381 scopus 로고    scopus 로고
    • Calcium-dependent release of adenosine and uridine nucleotides from A549 cells
    • Tatur, S., Kreda, S., Lazarowski, E. & Grygorczyk, R. 2008. Calcium-dependent release of adenosine and uridine nucleotides from A549 cells. Purinergic Signal 4, 139–146.
    • (2008) Purinergic Signal , vol.4 , pp. 139-146
    • Tatur, S.1    Kreda, S.2    Lazarowski, E.3    Grygorczyk, R.4
  • 182
    • 0012768372 scopus 로고
    • Characterization of the Na-dependent taurine influx in flounder erythrocytes
    • Thoroed, S.M. & Fugelli, K. 1993. Characterization of the Na-dependent taurine influx in flounder erythrocytes. J Comp Physiol 163, 307–316.
    • (1993) J Comp Physiol , vol.163 , pp. 307-316
    • Thoroed, S.M.1    Fugelli, K.2
  • 183
    • 0027177499 scopus 로고
    • Na(+)-independent, H(+)-coupled transepithelial beta-alanine absorption by human intestinal Caco-2 cell monolayers
    • Thwaites, D.T., McEwan, G.T., Brown, C.D., Hirst, B.H. & Simmons, N.L. 1993. Na(+)-independent, H(+)-coupled transepithelial beta-alanine absorption by human intestinal Caco-2 cell monolayers. J Biol Chem 268, 18438–18441.
    • (1993) J Biol Chem , vol.268 , pp. 18438-18441
    • Thwaites, D.T.1    McEwan, G.T.2    Brown, C.D.3    Hirst, B.H.4    Simmons, N.L.5
  • 184
    • 52049118519 scopus 로고    scopus 로고
    • Function of taurine transporter (Slc6a6/TauT) as a GABA transporting protein and its relevance to GABA transport in rat retinal capillary endothelial cells
    • Tomi, M., Tajima, A., Tachikawa, M. & Hosoya, K. 2008. Function of taurine transporter (Slc6a6/TauT) as a GABA transporting protein and its relevance to GABA transport in rat retinal capillary endothelial cells. Biochim Biophys Acta 1778, 2138–2142.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2138-2142
    • Tomi, M.1    Tajima, A.2    Tachikawa, M.3    Hosoya, K.4
  • 185
    • 0029015111 scopus 로고
    • Plasma and whole blood taurine concentrations respond differently to taurine supplementation (humans) and depletion (cats)
    • Trautwein, E.A. & Hayes, K.C. 1995. Plasma and whole blood taurine concentrations respond differently to taurine supplementation (humans) and depletion (cats). Z Ernahrungswiss 34, 137–142.
    • (1995) Z Ernahrungswiss , vol.34 , pp. 137-142
    • Trautwein, E.A.1    Hayes, K.C.2
  • 186
    • 44949251896 scopus 로고    scopus 로고
    • Production of hypotaurine from L-cysteinesulfinate by rat liver mitochondria
    • Ubuka, T., Okada, A. & Nakamura, H. 2008. Production of hypotaurine from L-cysteinesulfinate by rat liver mitochondria. Amino Acids 35, 53–58.
    • (2008) Amino Acids , vol.35 , pp. 53-58
    • Ubuka, T.1    Okada, A.2    Nakamura, H.3
  • 187
    • 0026774290 scopus 로고
    • Molecular cloning of the cDNA for an MDCK cell Na(+)- and Cl(−)- dependent taurine transporter that is regulated by hypertonicity
    • Uchida, S., Kwon, H.M., Yamauchi, A., Preston, A.S., Marumo, F. & Handler, J.S. 1992. Molecular cloning of the cDNA for an MDCK cell Na(+)- and Cl(−)- dependent taurine transporter that is regulated by hypertonicity. Proc Natl Acad Sci USA 89, 8230–8234.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8230-8234
    • Uchida, S.1    Kwon, H.M.2    Yamauchi, A.3    Preston, A.S.4    Marumo, F.5    Handler, J.S.6
  • 188
    • 34548066563 scopus 로고    scopus 로고
    • Enzymes of the taurine biosynthetic pathway are expressed in rat mammary gland
    • Ueki, I. & Stipanuk, M.H. 2007. Enzymes of the taurine biosynthetic pathway are expressed in rat mammary gland. J Nutr 137, 1887–1894.
    • (2007) J Nutr , vol.137 , pp. 1887-1894
    • Ueki, I.1    Stipanuk, M.H.2
  • 189
    • 60249086784 scopus 로고    scopus 로고
    • 3T3-L1 adipocytes and rat adipose tissue have a high capacity for taurine synthesis by the cysteine dioxygenase/cysteinesulfinate decarboxylase and cysteamine dioxygenase pathways
    • Ueki, I. & Stipanuk, M.H. 2009. 3T3-L1 adipocytes and rat adipose tissue have a high capacity for taurine synthesis by the cysteine dioxygenase/cysteinesulfinate decarboxylase and cysteamine dioxygenase pathways. J Nutr 139, 207–214.
    • (2009) J Nutr , vol.139 , pp. 207-214
    • Ueki, I.1    Stipanuk, M.H.2
  • 190
    • 80053225374 scopus 로고    scopus 로고
    • Knockout of the murine cysteine dioxygenase gene results in severe impairment in ability to synthesize taurine and an increased catabolism of cysteine to hydrogen sulfide
    • Ueki, I., Roman, H.B., Valli, A., Fieselmann, K., Lam, J., Peters, R., Hirschberger, L.L. & Stipanuk, M.H. 2011. Knockout of the murine cysteine dioxygenase gene results in severe impairment in ability to synthesize taurine and an increased catabolism of cysteine to hydrogen sulfide. Am J Physiol Endocrinol Metab 301, E668–E684.
    • (2011) Am J Physiol Endocrinol Metab , vol.301 , pp. E668-E684
    • Ueki, I.1    Roman, H.B.2    Valli, A.3    Fieselmann, K.4    Lam, J.5    Peters, R.6    Hirschberger, L.L.7    Stipanuk, M.H.8
  • 191
    • 84861155977 scopus 로고    scopus 로고
    • Extrahepatic tissues compensate for loss of hepatic taurine synthesis in mice with liver-specific knockout of cysteine dioxygenase
    • Ueki, I., Roman, H.B., Hirschberger, L.L., Junior, C. & Stipanuk, M.H. 2012. Extrahepatic tissues compensate for loss of hepatic taurine synthesis in mice with liver-specific knockout of cysteine dioxygenase. Am J Physiol Endocrinol Metab 302, E1292–E1299.
    • (2012) Am J Physiol Endocrinol Metab , vol.302 , pp. E1292-E1299
    • Ueki, I.1    Roman, H.B.2    Hirschberger, L.L.3    Junior, C.4    Stipanuk, M.H.5
  • 192
  • 193
    • 78549262974 scopus 로고    scopus 로고
    • Acute cholesterol depletion leads to net loss of the organic osmolyte Taurine in Ehrlich Lettré tumor cells
    • Villumsen, K.R., Duelund, L. & Lambert, I.H. 2010. Acute cholesterol depletion leads to net loss of the organic osmolyte Taurine in Ehrlich Lettré tumor cells. Amino Acids 39, 1521–1536.
    • (2010) Amino Acids , vol.39 , pp. 1521-1536
    • Villumsen, K.R.1    Duelund, L.2    Lambert, I.H.3
  • 194
    • 0034912910 scopus 로고    scopus 로고
    • Taurine protects against carbon tetrachloride toxicity in the cultured neurons and in vivo
    • Vohra, B.P. & Hui, X. 2001. Taurine protects against carbon tetrachloride toxicity in the cultured neurons and in vivo. Arch Physiol Biochem 109, 90–94.
    • (2001) Arch Physiol Biochem , vol.109 , pp. 90-94
    • Vohra, B.P.1    Hui, X.2
  • 195
    • 11244343929 scopus 로고    scopus 로고
    • Regulation of the expression and subcellular localisation of the taurine transporter TauT in mouse NIH3T3 fibroblasts
    • Voss, J.W., Pedersen, S.F., Christensen, S.T. & Lambert, I.H. 2004. Regulation of the expression and subcellular localisation of the taurine transporter TauT in mouse NIH3T3 fibroblasts. Eur J Biochem 271, 4646–4658.
    • (2004) Eur J Biochem , vol.271 , pp. 4646-4658
    • Voss, J.W.1    Pedersen, S.F.2    Christensen, S.T.3    Lambert, I.H.4
  • 197
    • 2442715460 scopus 로고    scopus 로고
    • Taurine transporter knockout depletes muscle taurine levels and results in severe skeletal muscle impairment but leaves cardiac function uncompromised
    • Warskulat, U., Flogel, U., Jacoby, C., Hartwig, H.G., Thewissen, M., Merx, M.W., Molojavyi, A., Heller-Stilb, B., Schrader, J. & Haussinger, D. 2004. Taurine transporter knockout depletes muscle taurine levels and results in severe skeletal muscle impairment but leaves cardiac function uncompromised. FASEB J 18, 577–579.
    • (2004) FASEB J , vol.18 , pp. 577-579
    • Warskulat, U.1    Flogel, U.2    Jacoby, C.3    Hartwig, H.G.4    Thewissen, M.5    Merx, M.W.6    Molojavyi, A.7    Heller-Stilb, B.8    Schrader, J.9    Haussinger, D.10
  • 200
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • Weiss, S.J., Klein, R., Slivka, A. & Wei, M. 1982. Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J Clin Invest 70, 598–607.
    • (1982) J Clin Invest , vol.70 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 202
    • 0023912886 scopus 로고
    • Taurine transport by rabbit kidney brush-border membranes: coupling to sodium, chloride, and the membrane potential
    • Wolff, N.A. & Kinne, R. 1988. Taurine transport by rabbit kidney brush-border membranes: coupling to sodium, chloride, and the membrane potential. J Membr Biol 102, 131–139.
    • (1988) J Membr Biol , vol.102 , pp. 131-139
    • Wolff, N.A.1    Kinne, R.2
  • 204
    • 0001350263 scopus 로고    scopus 로고
    • Taurine prevents high-glucose-induced human vascular endothelial cell apoptosis
    • Wu, Q.D., Wang, J.H., Fennessy, F., Redmond, H.P. & Bouchier-Hayes, D. 1999. Taurine prevents high-glucose-induced human vascular endothelial cell apoptosis. Am J Physiol 277, C1229–C1238.
    • (1999) Am J Physiol , vol.277 , pp. C1229-C1238
    • Wu, Q.D.1    Wang, J.H.2    Fennessy, F.3    Redmond, H.P.4    Bouchier-Hayes, D.5
  • 206
    • 0028249037 scopus 로고
    • Nutritional factors for stroke and major cardiovascular diseases: international epidemiological comparison of dietary prevention
    • Yamori, Y., Nara, Y., Mizushima, S., Sawamura, M. & Horie, R. 1994. Nutritional factors for stroke and major cardiovascular diseases: international epidemiological comparison of dietary prevention. Health Rep 6, 22–27.
    • (1994) Health Rep , vol.6 , pp. 22-27
    • Yamori, Y.1    Nara, Y.2    Mizushima, S.3    Sawamura, M.4    Horie, R.5
  • 207
    • 0028178708 scopus 로고
    • Identification of the GABAA receptor subtype mRNA in human pancreatic tissue
    • Yang, W., Reyes, A.A. & Lan, N.C. 1994. Identification of the GABAA receptor subtype mRNA in human pancreatic tissue. FEBS Lett 346, 257–262.
    • (1994) FEBS Lett , vol.346 , pp. 257-262
    • Yang, W.1    Reyes, A.A.2    Lan, N.C.3
  • 208
    • 84899819129 scopus 로고    scopus 로고
    • Role of SLC6A6 in promoting the survival and multidrug resistance of colorectal cancer
    • Yasunaga, M. & Matsumura, Y. 2014. Role of SLC6A6 in promoting the survival and multidrug resistance of colorectal cancer. Sci Rep 4, 4852.
    • (2014) Sci Rep , vol.4 , pp. 4852
    • Yasunaga, M.1    Matsumura, Y.2
  • 209
    • 34249743522 scopus 로고    scopus 로고
    • Effects of taurine in cellular responses to oxidative stress in young and middle-aged rat liver
    • Yildirim, Z., Kilic, N., Ozer, C., Babul, A., Take, G. & Erdogan, D. 2007. Effects of taurine in cellular responses to oxidative stress in young and middle-aged rat liver. Ann N Y Acad Sci 1100, 553–561.
    • (2007) Ann N Y Acad Sci , vol.1100 , pp. 553-561
    • Yildirim, Z.1    Kilic, N.2    Ozer, C.3    Babul, A.4    Take, G.5    Erdogan, D.6
  • 210
    • 0024431110 scopus 로고
    • Ionic requirements for amino acid transport
    • Zelikovic, I. & Chesney, R.W. 1989. Ionic requirements for amino acid transport. Am J Kidney Dis 14, 313–316.
    • (1989) Am J Kidney Dis , vol.14 , pp. 313-316
    • Zelikovic, I.1    Chesney, R.W.2
  • 211
    • 77957549814 scopus 로고    scopus 로고
    • Effects of taurine on glial cells apoptosis and taurine transporter expression in retina under diabetic conditions
    • Zeng, K., Xu, H., Mi, M., Chen, K., Zhu, J., Yi, L., Zhang, T., Zhang, Q. & Yu, X. 2010. Effects of taurine on glial cells apoptosis and taurine transporter expression in retina under diabetic conditions. Neurochem Res 35, 1566–1574.
    • (2010) Neurochem Res , vol.35 , pp. 1566-1574
    • Zeng, K.1    Xu, H.2    Mi, M.3    Chen, K.4    Zhu, J.5    Yi, L.6    Zhang, T.7    Zhang, Q.8    Yu, X.9
  • 212
    • 0031004550 scopus 로고    scopus 로고
    • Intracellular generation of reactive oxygen species in endothelial cells exposed to anoxia-reoxygenation
    • Zulueta, J.J., Sawhney, R., Yu, F.S., Cote, C.C. & Hassoun, P.M. 1997. Intracellular generation of reactive oxygen species in endothelial cells exposed to anoxia-reoxygenation. Am J Physiol 272, L897–L902.
    • (1997) Am J Physiol , vol.272 , pp. L897-L902
    • Zulueta, J.J.1    Sawhney, R.2    Yu, F.S.3    Cote, C.C.4    Hassoun, P.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.