메뉴 건너뛰기




Volumn 47, Issue 2, 2013, Pages 699-710

Expression of taurine transporter (TauT) is modulated by heat shock factor 1 (HSF1) in motor neurons of ALS.

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; DNA BINDING PROTEIN; HSF1 PROTEIN, MOUSE; MEMBRANE PROTEIN; TAURINE TRANSPORTER; TRANSCRIPTION FACTOR;

EID: 84891084712     PISSN: None     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-012-8371-9     Document Type: Article
Times cited : (29)

References (40)
  • 1
    • 0035978743 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • 1. LP Rowland NA Shneider 2001 Amyotrophic lateral sclerosis N Engl J Med 344 1688 1700 11386269 10.1056/NEJM200105313442207 1:CAS:528:DC%2BD3MXkslWjtbo%3D Rowland LP, Shneider NA (2001) Amyotrophic lateral sclerosis. N Engl J Med 344:1688–1700
    • (2001) N Engl J Med , vol.344 , pp. 1688-1700
    • Rowland, LP1    Shneider, NA2
  • 2
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • 2. DR Rosen 1993 Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis Nature 362 59 62 8446170 10.1038/362059a0 1:CAS:528:DyaK3sXhvV2hs74%3D Rosen DR (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362:59–62
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, DR1
  • 3
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation
    • 3. ME Gurney H Pu AY Chiu MC Dal Canto CY Polchow DD Alexander J Caliendo A Hentati YW Kwon HX Deng 1994 Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation Science 264 1772 1775 8209258 10.1126/science.8209258 1:CAS:528:DyaK2cXksFGisbk%3D Gurney ME, Pu H, Chiu AY, Dal Canto MC, Polchow CY, Alexander DD, Caliendo J, Hentati A, Kwon YW, Deng HX (1994) Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science 264:1772–1775
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, ME1    Pu, H2    Chiu, AY3    Dal Canto, MC4    Polchow, CY5    Alexander, DD6    Caliendo, J7    Hentati, A8    Kwon, YW9    Deng, HX10
  • 4
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • 4. LI Bruijn MW Becher MK Lee KL Anderson NA Jenkins NG Copeland SS Sisodia JD Rothstein DR Borchelt DL Price DW Cleveland 1997 ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions Neuron 18 327 338 9052802 10.1016/S0896-6273(00)80272-X 1:CAS:528:DyaK2sXhslersLk%3D Bruijn LI, Becher MW, Lee MK, Anderson KL, Jenkins NA, Copeland NG, Sisodia SS, Rothstein JD, Borchelt DR, Price DL, Cleveland DW (1997) ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 18:327–338
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, LI1    Becher, MW2    Lee, MK3    Anderson, KL4    Jenkins, NA5    Copeland, NG6    Sisodia, SS7    Rothstein, JD8    Borchelt, DR9    Price, DL10    Cleveland, DW11
  • 5
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • 5. LI Bruijn MK Houseweart S Kato KL Anderson SD Anderson E Ohama AG Reaume RW Scott DW Cleveland 1998 Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1 Science 281 1851 1854 9743498 10.1126/science.281.5384.1851 1:CAS:528:DyaK1cXmtVKgt7c%3D Bruijn LI, Houseweart MK, Kato S, Anderson KL, Anderson SD, Ohama E, Reaume AG, Scott RW, Cleveland DW (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281:1851–1854
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, LI1    Houseweart, MK2    Kato, S3    Anderson, KL4    Anderson, SD5    Ohama, E6    Reaume, AG7    Scott, RW8    Cleveland, DW9
  • 6
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • 6. PC Wong CA Pardo DR Borchelt MK Lee NG Copeland NA Jenkins SS Sisodia DW Cleveland DL Price 1995 An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria Neuron 14 1105 1116 7605627 10.1016/0896-6273(95)90259-7 1:CAS:528:DyaK2MXms1Wrtr8%3D Wong PC, Pardo CA, Borchelt DR, Lee MK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW, Price DL (1995) An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14:1105–1116
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, PC1    Pardo, CA2    Borchelt, DR3    Lee, MK4    Copeland, NG5    Jenkins, NA6    Sisodia, SS7    Cleveland, DW8    Price, DL9
  • 7
    • 0042232390 scopus 로고    scopus 로고
    • Prospects for the pharmacotherapy of amyotrophic lateral sclerosis: old strategies and new paradigms for the third millennium
    • 7. BW Festoff Z Suo BA Citron 2003 Prospects for the pharmacotherapy of amyotrophic lateral sclerosis: old strategies and new paradigms for the third millennium CNS Drugs 17 699 717 12873154 10.2165/00023210-200317100-00002 1:CAS:528:DC%2BD3sXntl2nsLs%3D Festoff BW, Suo Z, Citron BA (2003) Prospects for the pharmacotherapy of amyotrophic lateral sclerosis: old strategies and new paradigms for the third millennium. CNS Drugs 17:699–717
    • (2003) CNS Drugs , vol.17 , pp. 699-717
    • Festoff, BW1    Suo, Z2    Citron, BA3
  • 8
    • 15944377898 scopus 로고    scopus 로고
    • Pharmacologic approaches to the treatment of amyotrophic lateral sclerosis
    • 8. EG McGeer PL McGeer 2005 Pharmacologic approaches to the treatment of amyotrophic lateral sclerosis BioDrugs 19 31 37 15691215 10.2165/00063030-200519010-00004 1:CAS:528:DC%2BD2MXjtleltLs%3D McGeer EG, McGeer PL (2005) Pharmacologic approaches to the treatment of amyotrophic lateral sclerosis. BioDrugs 19:31–37
    • (2005) BioDrugs , vol.19 , pp. 31-37
    • McGeer, EG1    McGeer, PL2
  • 9
    • 0037380729 scopus 로고    scopus 로고
    • Of mice and men: reconciling preclinical ALS mouse studies and human clinical trials
    • 9. JD Rothstein 2003 Of mice and men: reconciling preclinical ALS mouse studies and human clinical trials Ann Neurol 53 423 426 12666108 10.1002/ana.10561 Rothstein JD (2003) Of mice and men: reconciling preclinical ALS mouse studies and human clinical trials. Ann Neurol 53:423–426
    • (2003) Ann Neurol , vol.53 , pp. 423-426
    • Rothstein, JD1
  • 10
    • 1842854596 scopus 로고    scopus 로고
    • Current pharmacological management of amyotrophic lateral sclerosis and a role for rational polypharmacy
    • 10. MD Weiss P Weydt GT Carter 2004 Current pharmacological management of amyotrophic lateral sclerosis and a role for rational polypharmacy Expert Opin Pharmacother 5 735 746 15102560 10.1517/14656566.5.4.735 Weiss MD, Weydt P, Carter GT (2004) Current pharmacological management of amyotrophic lateral sclerosis and a role for rational polypharmacy. Expert Opin Pharmacother 5:735–746
    • (2004) Expert Opin Pharmacother , vol.5 , pp. 735-746
    • Weiss, MD1    Weydt, P2    Carter, GT3
  • 11
    • 0023804850 scopus 로고
    • The neuroexcitotoxic amino acids glutamate and aspartate are altered in the spinal cord and brain in amyotrophic lateral sclerosis
    • 11. A Plaitakis E Constantakakis J Smith 1988 The neuroexcitotoxic amino acids glutamate and aspartate are altered in the spinal cord and brain in amyotrophic lateral sclerosis Ann Neurol 24 446 449 2906529 10.1002/ana.410240314 1:CAS:528:DyaL1cXmt1Ort7Y%3D Plaitakis A, Constantakakis E, Smith J (1988) The neuroexcitotoxic amino acids glutamate and aspartate are altered in the spinal cord and brain in amyotrophic lateral sclerosis. Ann Neurol 24:446–449
    • (1988) Ann Neurol , vol.24 , pp. 446-449
    • Plaitakis, A1    Constantakakis, E2    Smith, J3
  • 12
    • 0036892683 scopus 로고    scopus 로고
    • Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis
    • 12. M Urushitani J Kurisu K Tsukita R Takahashi 2002 Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis J Neurochem 83 1030 1042 12437574 10.1046/j.1471-4159.2002.01211.x 1:CAS:528:DC%2BD38XptlGksbw%3D Urushitani M, Kurisu J, Tsukita K, Takahashi R (2002) Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis. J Neurochem 83:1030–1042
    • (2002) J Neurochem , vol.83 , pp. 1030-1042
    • Urushitani, M1    Kurisu, J2    Tsukita, K3    Takahashi, R4
  • 13
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • 13. JD Rothstein M Kammen Van AI Levey LJ Martin RW Kuncl 1995 Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis Ann Neurol 38 73 84 7611729 10.1002/ana.410380114 1:CAS:528:DyaK2MXnt12lsbw%3D Rothstein JD, Van Kammen M, Levey AI, Martin LJ, Kuncl RW (1995) Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann Neurol 38:73–84
    • (1995) Ann Neurol , vol.38 , pp. 73-84
    • Rothstein, JD1    Kammen, M2    Levey, AI3    Martin, LJ4    Kuncl, RW5
  • 14
    • 0029991177 scopus 로고    scopus 로고
    • Pathogenic mechanisms in familial amyotrophic lateral sclerosis due to mutation of Cu, Zn superoxide dismutase
    • 14. ME Gurney FB Cutting P Zhai PK Andrus ED Hall 1996 Pathogenic mechanisms in familial amyotrophic lateral sclerosis due to mutation of Cu, Zn superoxide dismutase Pathol Biol (Paris) 44 51 56 1:CAS:528:DyaK28XitlGrtbs%3D Gurney ME, Cutting FB, Zhai P, Andrus PK, Hall ED (1996) Pathogenic mechanisms in familial amyotrophic lateral sclerosis due to mutation of Cu, Zn superoxide dismutase. Pathol Biol (Paris) 44:51–56
    • (1996) Pathol Biol (Paris) , vol.44 , pp. 51-56
    • Gurney, ME1    Cutting, FB2    Zhai, P3    Andrus, PK4    Hall, ED5
  • 15
    • 67651045775 scopus 로고    scopus 로고
    • Differential regulation of neuronal and inducible nitric oxide synthase (NOS) in the spinal cord of mutant SOD1 (G93A) ALS mice
    • 15. J Lee H Ryu NW Kowall 2009 Differential regulation of neuronal and inducible nitric oxide synthase (NOS) in the spinal cord of mutant SOD1 (G93A) ALS mice Biochem Biophys Res Commun 387 202 206 19580782 10.1016/j.bbrc.2009.07.007 1:CAS:528:DC%2BD1MXptValtrc%3D Lee J, Ryu H, Kowall NW (2009) Differential regulation of neuronal and inducible nitric oxide synthase (NOS) in the spinal cord of mutant SOD1 (G93A) ALS mice. Biochem Biophys Res Commun 387:202–206
    • (2009) Biochem Biophys Res Commun , vol.387 , pp. 202-206
    • Lee, J1    Ryu, H2    Kowall, NW3
  • 16
    • 65649104477 scopus 로고    scopus 로고
    • Motor neuronal protection by l-arginine prolongs survival of mutant SOD1 (G93A) ALS mice
    • 16. J Lee H Ryu NW Kowall 2009 Motor neuronal protection by l-arginine prolongs survival of mutant SOD1 (G93A) ALS mice Biochem Biophys Res Commun 384 524 529 19427829 10.1016/j.bbrc.2009.05.015 1:CAS:528:DC%2BD1MXmsVCgt78%3D Lee J, Ryu H, Kowall NW (2009) Motor neuronal protection by l-arginine prolongs survival of mutant SOD1 (G93A) ALS mice. Biochem Biophys Res Commun 384:524–529
    • (2009) Biochem Biophys Res Commun , vol.384 , pp. 524-529
    • Lee, J1    Ryu, H2    Kowall, NW3
  • 17
    • 0018386616 scopus 로고
    • Free amino acids in motor cortex of amyotrophic lateral sclerosis
    • 17. Y Yoshino H Koike K Akai 1979 Free amino acids in motor cortex of amyotrophic lateral sclerosis Experientia 35 219 220 421837 10.1007/BF01920627 1:CAS:528:DyaE1MXhtF2gsL0%3D Yoshino Y, Koike H, Akai K (1979) Free amino acids in motor cortex of amyotrophic lateral sclerosis. Experientia 35:219–220
    • (1979) Experientia , vol.35 , pp. 219-220
    • Yoshino, Y1    Koike, H2    Akai, K3
  • 18
    • 0016887303 scopus 로고
    • Free amino-acids in the human spinal cord—analysis of anterior, posterior columns and anterior, lateral and posterior funiculi
    • 18. Y Yoshino S Iwabuchi K Akai 1976 Free amino-acids in the human spinal cord—analysis of anterior, posterior columns and anterior, lateral and posterior funiculi Rinsho Shinkeigaku 16 74 81 943267 1:STN:280:DyaE287jvVOhug%3D%3D Yoshino Y, Iwabuchi S, Akai K (1976) Free amino-acids in the human spinal cord—analysis of anterior, posterior columns and anterior, lateral and posterior funiculi. Rinsho Shinkeigaku 16:74–81
    • (1976) Rinsho Shinkeigaku , vol.16 , pp. 74-81
    • Yoshino, Y1    Iwabuchi, S2    Akai, K3
  • 19
    • 18244417833 scopus 로고    scopus 로고
    • Plasma amino acids concentration in amyotrophic lateral sclerosis patients
    • 19. J Iłzecka Z Stelmasiak J Solski S Wawrzycki M Szpetnar 2003 Plasma amino acids concentration in amyotrophic lateral sclerosis patients Amino Acids 25 69 73 12836061 Iłzecka J, Stelmasiak Z, Solski J, Wawrzycki S, Szpetnar M (2003) Plasma amino acids concentration in amyotrophic lateral sclerosis patients. Amino Acids 25:69–73
    • (2003) Amino Acids , vol.25 , pp. 69-73
    • Iłzecka, J1    Stelmasiak, Z2    Solski, J3    Wawrzycki, S4    Szpetnar, M5
  • 20
    • 84934439009 scopus 로고    scopus 로고
    • Effects of dietary salt and fat on taurine excretion in healthy and diseased rats
    • 20. MS Mozaffari R Abdelsayed C Patel SW Schaffer 2006 Effects of dietary salt and fat on taurine excretion in healthy and diseased rats Adv Exp Med Biol 583 173 180 17153600 10.1007/978-0-387-33504-9_17 1:CAS:528:DC%2BD1MXhtFWjurs%3D Mozaffari MS, Abdelsayed R, Patel C, Schaffer SW (2006) Effects of dietary salt and fat on taurine excretion in healthy and diseased rats. Adv Exp Med Biol 583:173–180
    • (2006) Adv Exp Med Biol , vol.583 , pp. 173-180
    • Mozaffari, MS1    Abdelsayed, R2    Patel, C3    Schaffer, SW4
  • 21
    • 0026641662 scopus 로고
    • Bile salt- and lysophosphatidylcholine-induced membrane damage in human erythrocytes
    • 21. GP Martin LM el-Hariri C Marriott 1992 Bile salt-and lysophosphatidylcholine-induced membrane damage in human erythrocytes J Pharm Pharmacol 44 646 650 1359087 10.1111/j.2042-7158.1992.tb05486.x 1:CAS:528:DyaK38Xlslyhsbw%3D Martin GP, el-Hariri LM, Marriott C (1992) Bile salt-and lysophosphatidylcholine-induced membrane damage in human erythrocytes. J Pharm Pharmacol 44:646–650
    • (1992) J Pharm Pharmacol , vol.44 , pp. 646-650
    • Martin, GP1    el-Hariri, LM2    Marriott, C3
  • 22
    • 0034585074 scopus 로고    scopus 로고
    • Gene expression of taurine transporter and taurine biosynthetic enzymes in hyperosmotic states: a comparative study with the expression of the genes involved in the accumulation of other osmolytes
    • 22. M Bitoun M Tappaz 2000 Gene expression of taurine transporter and taurine biosynthetic enzymes in hyperosmotic states: a comparative study with the expression of the genes involved in the accumulation of other osmolytes Adv Exp Med Biol 483 239 248 11787603 10.1007/0-306-46838-7_26 1:CAS:528:DC%2BD3MXitFahtrw%3D Bitoun M, Tappaz M (2000) Gene expression of taurine transporter and taurine biosynthetic enzymes in hyperosmotic states: a comparative study with the expression of the genes involved in the accumulation of other osmolytes. Adv Exp Med Biol 483:239–248
    • (2000) Adv Exp Med Biol , vol.483 , pp. 239-248
    • Bitoun, M1    Tappaz, M2
  • 23
    • 0034646797 scopus 로고    scopus 로고
    • Gene expression of taurine transporter and taurine biosynthetic enzymes in brain of rats with acute or chronic hyperosmotic plasma. A comparative study with gene expression of myo-inositol transporter, betaine transporter and sorbitol biosynthetic enzyme
    • 23. M Bitoun M Tappaz 2000 Gene expression of taurine transporter and taurine biosynthetic enzymes in brain of rats with acute or chronic hyperosmotic plasma. A comparative study with gene expression of myo-inositol transporter, betaine transporter and sorbitol biosynthetic enzyme Brain Res Mol Brain Res 77 10 18 10814827 10.1016/S0169-328X(00)00034-6 1:CAS:528:DC%2BD3cXjt1aqt7k%3D Bitoun M, Tappaz M (2000) Gene expression of taurine transporter and taurine biosynthetic enzymes in brain of rats with acute or chronic hyperosmotic plasma. A comparative study with gene expression of myo-inositol transporter, betaine transporter and sorbitol biosynthetic enzyme. Brain Res Mol Brain Res 77:10–18
    • (2000) Brain Res Mol Brain Res , vol.77 , pp. 10-18
    • Bitoun, M1    Tappaz, M2
  • 24
    • 0028074718 scopus 로고
    • Potassium and taurine release are highly correlated with regulatory volume decrease in neonatal primary rat astrocyte cultures
    • 24. D Vitarella DJ DiRisio HK Kimelberg M Aschner 1994 Potassium and taurine release are highly correlated with regulatory volume decrease in neonatal primary rat astrocyte cultures J Neurochem 63 1143 1149 8051556 10.1046/j.1471-4159.1994.63031143.x 1:CAS:528:DyaK2cXmtVWntbw%3D Vitarella D, DiRisio DJ, Kimelberg HK, Aschner M (1994) Potassium and taurine release are highly correlated with regulatory volume decrease in neonatal primary rat astrocyte cultures. J Neurochem 63:1143–1149
    • (1994) J Neurochem , vol.63 , pp. 1143-1149
    • Vitarella, D1    DiRisio, DJ2    Kimelberg, HK3    Aschner, M4
  • 25
    • 0032572603 scopus 로고    scopus 로고
    • Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease
    • 25. IJ Benjamin DR McMillan 1998 Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease Circ Res 83 117 132 9686751 10.1161/01.RES.83.2.117 1:CAS:528:DyaK1cXkvFanu78%3D Benjamin IJ, McMillan DR (1998) Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease. Circ Res 83:117–132
    • (1998) Circ Res , vol.83 , pp. 117-132
    • Benjamin, IJ1    McMillan, DR2
  • 26
    • 80052783545 scopus 로고    scopus 로고
    • Astrocytes from familial and sporadic ALS patients are toxic to motor neurons
    • 26. AM Haidet-Phillips ME Hester CJ Miranda K Meyer L Braun A Frakes S Song S Likhite MJ Murtha KD Foust M Rao A Eagle A Kammesheidt A Christensen JR Mendell AH Burghes BK Kaspar 2011 Astrocytes from familial and sporadic ALS patients are toxic to motor neurons Nat Biotechnol 29 9 824 828 21832997 10.1038/nbt.1957 1:CAS:528:DC%2BC3MXpvF2isrw%3D Haidet-Phillips AM, Hester ME, Miranda CJ, Meyer K, Braun L, Frakes A, Song S, Likhite S, Murtha MJ, Foust KD, Rao M, Eagle A, Kammesheidt A, Christensen A, Mendell JR, Burghes AH, Kaspar BK (2011) Astrocytes from familial and sporadic ALS patients are toxic to motor neurons. Nat Biotechnol 29(9):824–828
    • (2011) Nat Biotechnol , vol.29 , Issue.9 , pp. 824-828
    • Haidet-Phillips, AM1    Hester, ME2    Miranda, CJ3    Meyer, K4    Braun, L5    Frakes, A6    Song, S7    Likhite, S8    Murtha, MJ9    Foust, KD10    Rao, M11    Eagle, A12    Kammesheidt, A13    Christensen, A14    Mendell, JR15    Burghes, AH16    Kaspar, BK17
  • 27
    • 0027048250 scopus 로고
    • Cloning and expression of a high affinity taurine transporter from rat brain
    • 27. KE Smith LA Borden CH Wang PR Hartig TA Branchek RL Weinshank 1992 Cloning and expression of a high affinity taurine transporter from rat brain Mol Pharmacol 42 563 569 1435737 1:CAS:528:DyaK3sXkvV2hsrk%3D Smith KE, Borden LA, Wang CH, Hartig PR, Branchek TA, Weinshank RL (1992) Cloning and expression of a high affinity taurine transporter from rat brain. Mol Pharmacol 42:563–569
    • (1992) Mol Pharmacol , vol.42 , pp. 563-569
    • Smith, KE1    Borden, LA2    Wang, CH3    Hartig, PR4    Branchek, TA5    Weinshank, RL6
  • 28
    • 0033787716 scopus 로고    scopus 로고
    • Gene expression of the transporters and biosynthetic enzymes of the osmolytes in astrocyte primary cultures exposed to hyperosmotic conditions
    • 28. M Bitoun M Tappaz 2000 Gene expression of the transporters and biosynthetic enzymes of the osmolytes in astrocyte primary cultures exposed to hyperosmotic conditions Glia 32 165 176 11008216 10.1002/1098-1136(200011)32:2<165::AID-GLIA60>3.0.CO;2-2 1:STN:280:DC%2BD3M%2FivFWntw%3D%3D Bitoun M, Tappaz M (2000) Gene expression of the transporters and biosynthetic enzymes of the osmolytes in astrocyte primary cultures exposed to hyperosmotic conditions. Glia 32:165–176
    • (2000) Glia , vol.32 , pp. 165-176
    • Bitoun, M1    Tappaz, M2
  • 29
    • 0022259736 scopus 로고
    • Is taurine a neurotransmitter in rabbit retina?
    • 29. CT Lin GX Song JY Wu 1985 Is taurine a neurotransmitter in rabbit retina? Brain Res 337 293 298 2992680 10.1016/0006-8993(85)90066-6 1:CAS:528:DyaL2MXkvVahtLY%3D Lin CT, Song GX, Wu JY (1985) Is taurine a neurotransmitter in rabbit retina? Brain Res 337:293–298
    • (1985) Brain Res , vol.337 , pp. 293-298
    • Lin, CT1    Song, GX2    Wu, JY3
  • 30
    • 0026595620 scopus 로고
    • Physiological actions of taurine
    • 30. RJ Huxtable 1992 Physiological actions of taurine Physiol Rev 72 101 163 1731369 1:CAS:528:DyaK38XhsVKhsLw%3D Huxtable RJ (1992) Physiological actions of taurine. Physiol Rev 72:101–163
    • (1992) Physiol Rev , vol.72 , pp. 101-163
    • Huxtable, RJ1
  • 31
    • 0023711703 scopus 로고
    • A possible role for taurine in osmoregulation within the brain
    • 31. JV Wade JP Olson FE Samson SR Nelson TL Pazdernik 1988 A possible role for taurine in osmoregulation within the brain J Neurochem 51 740 745 3411323 10.1111/j.1471-4159.1988.tb01807.x 1:CAS:528:DyaL1cXlsVOis70%3D Wade JV, Olson JP, Samson FE, Nelson SR, Pazdernik TL (1988) A possible role for taurine in osmoregulation within the brain. J Neurochem 51:740–745
    • (1988) J Neurochem , vol.51 , pp. 740-745
    • Wade, JV1    Olson, JP2    Samson, FE3    Nelson, SR4    Pazdernik, TL5
  • 32
    • 77956047414 scopus 로고    scopus 로고
    • Taurine protection of PC12 cells against endoplasmic reticulum stress induced by oxidative stress
    • 32. C Pan GS Giraldo H Prentice JY Wu 2010 Taurine protection of PC12 cells against endoplasmic reticulum stress induced by oxidative stress J Biomed Sci 17 Suppl 1 S17 20804591 10.1186/1423-0127-17-S1-S17 Pan C, Giraldo GS, Prentice H, Wu JY (2010) Taurine protection of PC12 cells against endoplasmic reticulum stress induced by oxidative stress. J Biomed Sci 17(Suppl 1):S17
    • (2010) J Biomed Sci , vol.17 , Issue.Suppl 1 , pp. S17
    • Pan, C1    Giraldo, GS2    Prentice, H3    Wu, JY4
  • 33
    • 0026465350 scopus 로고
    • Neuroblastoma x spinal cord (NSC) hybrid cell lines resemble developing motor neurons
    • 33. NR Cashman HD Durham JK Blusztajn K Oda T Tabira IT Shaw S Dahrouge JP Antel 1992 Neuroblastoma x spinal cord (NSC) hybrid cell lines resemble developing motor neurons Dev Dyn 194 209 221 1467557 10.1002/aja.1001940306 1:STN:280:DyaK3s7gsVGlsw%3D%3D Cashman NR, Durham HD, Blusztajn JK, Oda K, Tabira T, Shaw IT, Dahrouge S, Antel JP (1992) Neuroblastoma x spinal cord (NSC) hybrid cell lines resemble developing motor neurons. Dev Dyn 194:209–221
    • (1992) Dev Dyn , vol.194 , pp. 209-221
    • Cashman, NR1    Durham, HD2    Blusztajn, JK3    Oda, K4    Tabira, T5    Shaw, IT6    Dahrouge, S7    Antel, JP8
  • 34
    • 0027714989 scopus 로고
    • Evaluation of the spinal cord neuron X neuroblastoma hybrid cell line NSC-34 as a model for neurotoxicity testing
    • 34. HD Durham S Dahrouge NR Cashman 1993 Evaluation of the spinal cord neuron X neuroblastoma hybrid cell line NSC-34 as a model for neurotoxicity testing Neurotoxicology 14 387 395 7909362 1:CAS:528:DyaK2cXis1eitL0%3D Durham HD, Dahrouge S, Cashman NR (1993) Evaluation of the spinal cord neuron X neuroblastoma hybrid cell line NSC-34 as a model for neurotoxicity testing. Neurotoxicology 14:387–395
    • (1993) Neurotoxicology , vol.14 , pp. 387-395
    • Durham, HD1    Dahrouge, S2    Cashman, NR3
  • 35
    • 35448956015 scopus 로고    scopus 로고
    • Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis
    • 35. C Gomes S Keller P Altevogt J Costa 2007 Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis Neurosci Lett 428 43 46 17942226 10.1016/j.neulet.2007.09.024 1:CAS:528:DC%2BD2sXht1Kjs73O Gomes C, Keller S, Altevogt P, Costa J (2007) Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis. Neurosci Lett 428:43–46
    • (2007) Neurosci Lett , vol.428 , pp. 43-46
    • Gomes, C1    Keller, S2    Altevogt, P3    Costa, J4
  • 36
    • 43149109289 scopus 로고    scopus 로고
    • Establishment of a cell model of ALS disease: Golgi apparatus disruption occurs independently from apoptosis
    • 36. C Gomes AS Palma R Almeida M Regalla LF McCluskey JQ Trojanowski J Costa 2008 Establishment of a cell model of ALS disease: Golgi apparatus disruption occurs independently from apoptosis Biotechnol Lett 30 603 610 18004513 10.1007/s10529-007-9595-z 1:CAS:528:DC%2BD1cXitFKgtr8%3D Gomes C, Palma AS, Almeida R, Regalla M, McCluskey LF, Trojanowski JQ, Costa J (2008) Establishment of a cell model of ALS disease: Golgi apparatus disruption occurs independently from apoptosis. Biotechnol Lett 30:603–610
    • (2008) Biotechnol Lett , vol.30 , pp. 603-610
    • Gomes, C1    Palma, AS2    Almeida, R3    Regalla, M4    McCluskey, LF5    Trojanowski, JQ6    Costa, J7
  • 37
    • 25444515720 scopus 로고    scopus 로고
    • Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons
    • 37. H Ryu J Lee S Impey RR Ratan RJ Ferrante 2005 Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons Proc Natl Acad Sci U S A 102 13915 13920 16169904 10.1073/pnas.0502878102 1:CAS:528:DC%2BD2MXhtVOqsbjN Ryu H, Lee J, Impey S, Ratan RR, Ferrante RJ (2005) Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons. Proc Natl Acad Sci U S A 102:13915–13920
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13915-13920
    • Ryu, H1    Lee, J2    Impey, S3    Ratan, RR4    Ferrante, RJ5
  • 38
    • 0032533159 scopus 로고    scopus 로고
    • Arginine metabolism: nitric oxide and beyond
    • 38. G Wu SM Morris Jr 1998 Arginine metabolism: nitric oxide and beyond Biochem J 336 1 17 9806879 1:CAS:528:DyaK1cXotVGltrs%3D Wu G, Morris SM Jr (1998) Arginine metabolism: nitric oxide and beyond. Biochem J 336:1–17
    • (1998) Biochem J , vol.336 , pp. 1-17
    • Wu, G1    Morris, SM2
  • 39
    • 44849107154 scopus 로고    scopus 로고
    • Analysis of citrulline, arginine, and methylarginines using high-performance liquid chromatography
    • 39. G Wu CJ Meininger 2008 Analysis of citrulline, arginine, and methylarginines using high-performance liquid chromatography Methods Enzymol 440 177 189 18423217 10.1016/S0076-6879(07)00810-5 1:CAS:528:DC%2BD1cXntF2hs7g%3D Wu G, Meininger CJ (2008) Analysis of citrulline, arginine, and methylarginines using high-performance liquid chromatography. Methods Enzymol 440:177–189
    • (2008) Methods Enzymol , vol.440 , pp. 177-189
    • Wu, G1    Meininger, CJ2
  • 40
    • 0036892753 scopus 로고    scopus 로고
    • Regulation of taurine transport at the blood–brain barrier by tumor necrosis factor-alpha, taurine and hypertonicity
    • 40. YS Kang S Ohtsuki H Takanaga M Tomi K Hosoya T Terasaki 2002 Regulation of taurine transport at the blood–brain barrier by tumor necrosis factor-alpha, taurine and hypertonicity J Neurochem 83 1188 1195 12437590 10.1046/j.1471-4159.2002.01223.x 1:CAS:528:DC%2BD38XptlGktrY%3D Kang YS, Ohtsuki S, Takanaga H, Tomi M, Hosoya K, Terasaki T (2002) Regulation of taurine transport at the blood–brain barrier by tumor necrosis factor-alpha, taurine and hypertonicity. J Neurochem 83:1188–1195
    • (2002) J Neurochem , vol.83 , pp. 1188-1195
    • Kang, YS1    Ohtsuki, S2    Takanaga, H3    Tomi, M4    Hosoya, K5    Terasaki, T6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.