메뉴 건너뛰기




Volumn 479, Issue 1-3, 2003, Pages 237-247

The glutamate and neutral amino acid transporter family: Physiological and pharmacological implications

Author keywords

ASC; Glutamate; Neutral amino acid transporter

Indexed keywords

ALANINE; ASPARTIC ACID; CARRIER PROTEIN; COTRANSPORTER; CYSTEINE; GLUTAMATE TRANSPORTER; GLUTAMIC ACID; GLUTAMINE; ISOPROTEIN; POTASSIUM ION; PROTEIN ASCT 1; PROTEIN ASCT 2; PROTEIN EAAC 1; PROTEIN EAAT4; PROTEIN EAAT5; PROTEIN GLAST; PROTEIN GLT 1; PROTON; SERINE; SODIUM ION; THREONINE; UNCLASSIFIED DRUG;

EID: 0242469279     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejphar.2003.08.073     Document Type: Article
Times cited : (184)

References (92)
  • 1
  • 2
    • 0027327563 scopus 로고
    • Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family
    • Arriza J.L., Kavanaugh M.P., Fairman W.A., Wu Y.N., Murdoch G.H., North R.A., Amara S.G. Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J. Biol. Chem. 268:1993;15329-15332.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15329-15332
    • Arriza, J.L.1    Kavanaugh, M.P.2    Fairman, W.A.3    Wu, Y.N.4    Murdoch, G.H.5    North, R.A.6    Amara, S.G.7
  • 4
    • 0030932152 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance
    • Arriza J.L., Eliasof S., Kavanaugh M.P., Amara S.G. Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance. Proc. Natl. Acad. Sci. U. S. A. 94:1997;4155-4160.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 4155-4160
    • Arriza, J.L.1    Eliasof, S.2    Kavanaugh, M.P.3    Amara, S.G.4
  • 5
    • 0033636982 scopus 로고    scopus 로고
    • Fast removal of synaptic glutamate by postsynaptic transporters
    • Auger C., Attwell D. Fast removal of synaptic glutamate by postsynaptic transporters. Neuron. 28:2000;547-558.
    • (2000) Neuron , vol.28 , pp. 547-558
    • Auger, C.1    Attwell, D.2
  • 6
    • 0034836595 scopus 로고    scopus 로고
    • Na(+)-dependent neutral amino acid transporter ATB(0) is a rabbit epithelial cell brush-border protein
    • Avissar N.E., Ryan C.K., Ganapathy V., Sax H.C. Na(+)-dependent neutral amino acid transporter ATB(0) is a rabbit epithelial cell brush-border protein. Am. J. Physiol., Cell Physiol. 281:2001;C963-C971.
    • (2001) Am. J. Physiol., Cell Physiol. , vol.281
    • Avissar, N.E.1    Ryan, C.K.2    Ganapathy, V.3    Sax, H.C.4
  • 7
    • 0031853290 scopus 로고    scopus 로고
    • Comparative analysis of glutamate transporter expression in rat brain using differential double in situ hybridization
    • Berger U.V., Hediger M.A. Comparative analysis of glutamate transporter expression in rat brain using differential double in situ hybridization. Anat. Embryol. (Berl.). 198:1998;13-30.
    • (1998) Anat. Embryol. (Berl.) , vol.198 , pp. 13-30
    • Berger, U.V.1    Hediger, M.A.2
  • 8
    • 0034653526 scopus 로고    scopus 로고
    • Neutral amino acid transporter ASCT2 displays substrate-induced Na+ exchange and a substrate-gated anion conductance
    • Broer A., Wagner C., Lang F., Broer S. Neutral amino acid transporter ASCT2 displays substrate-induced Na+ exchange and a substrate-gated anion conductance. Biochem. J. 346(Pt 3):2000;705-710.
    • (2000) Biochem. J. , vol.346 , Issue.3 PART , pp. 705-710
    • Broer, A.1    Wagner, C.2    Lang, F.3    Broer, S.4
  • 9
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice
    • Brown R.H. Jr. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell. 80:1995;687-692.
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown Jr., R.H.1
  • 11
    • 0031017893 scopus 로고    scopus 로고
    • Inhibition of the high-affinity brain glutamate transporter GLAST-1 via direct phosphorylation
    • Conradt M., Stoffel W. Inhibition of the high-affinity brain glutamate transporter GLAST-1 via direct phosphorylation. J. Neurochem. 68:1997;1244-1251.
    • (1997) J. Neurochem. , vol.68 , pp. 1244-1251
    • Conradt, M.1    Stoffel, W.2
  • 12
    • 0026539793 scopus 로고
    • +]coupled L-glutamate transporter purified from rat brain is located in glial cell processes
    • +]coupled L-glutamate transporter purified from rat brain is located in glial cell processes. Neuroscience. 51:1992;295-310.
    • (1992) Neuroscience , vol.51 , pp. 295-310
    • Danbolt, N.C.1    Storm-Mathisen, J.2    Kanner, B.I.3
  • 13
    • 0032053985 scopus 로고    scopus 로고
    • Multiple signaling pathways regulate cell surface expression and activity of the excitatory amino acid carrier 1 subtype of Glu transporter in C6 glioma
    • Davis K.E., Straff D.J., Weinstein E.A., Bannerman P.G., Correale D.M., Rothstein J.D., Robinson M.B. Multiple signaling pathways regulate cell surface expression and activity of the excitatory amino acid carrier 1 subtype of Glu transporter in C6 glioma. J. Neurosci. 18:1998;2475-2485.
    • (1998) J. Neurosci. , vol.18 , pp. 2475-2485
    • Davis, K.E.1    Straff, D.J.2    Weinstein, E.A.3    Bannerman, P.G.4    Correale, D.M.5    Rothstein, J.D.6    Robinson, M.B.7
  • 14
    • 0030036982 scopus 로고    scopus 로고
    • Rapid stimulation of EAAC1-mediated Na+-dependent L-glutamate transport activity in C6 glioma cells by phorbol ester
    • Dowd L.A., Robinson M.B. Rapid stimulation of EAAC1-mediated Na+-dependent L-glutamate transport activity in C6 glioma cells by phorbol ester. J. Neurochem. 67:1996;508-516.
    • (1996) J. Neurochem. , vol.67 , pp. 508-516
    • Dowd, L.A.1    Robinson, M.B.2
  • 15
    • 0020574199 scopus 로고
    • Novel neuron-related regulatory mechanisms for astrocytic glutamate and GABA high affinity uptake
    • Drejer J., Meier E., Schousboe A. Novel neuron-related regulatory mechanisms for astrocytic glutamate and GABA high affinity uptake. Neurosci. Lett. 37:1983;301-306.
    • (1983) Neurosci. Lett. , vol.37 , pp. 301-306
    • Drejer, J.1    Meier, E.2    Schousboe, A.3
  • 16
    • 0033612892 scopus 로고    scopus 로고
    • Properties of excitatory amino acid transport in the human U373 astrocytoma cell line
    • Dunlop J., Lou Z., McIlvain H.B. Properties of excitatory amino acid transport in the human U373 astrocytoma cell line. Brain Res. 839:1999;235-242.
    • (1999) Brain Res. , vol.839 , pp. 235-242
    • Dunlop, J.1    Lou, Z.2    McIlvain, H.B.3
  • 18
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • Fairman W.A., Vandenberg R.J., Arriza J.L., Kavanaugh M.P., Amara S.G. An excitatory amino-acid transporter with properties of a ligand-gated chloride channel. Nature. 375:1995;599-603.
    • (1995) Nature , vol.375 , pp. 599-603
    • Fairman, W.A.1    Vandenberg, R.J.2    Arriza, J.L.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 19
    • 0034657768 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide (PACAP), a neuron-derived peptide regulating glial glutamate transport and metabolism
    • Figiel M., Engele J. Pituitary adenylate cyclase-activating polypeptide (PACAP), a neuron-derived peptide regulating glial glutamate transport and metabolism. J. Neurosci. 20:2000;3596-3605.
    • (2000) J. Neurosci. , vol.20 , pp. 3596-3605
    • Figiel, M.1    Engele, J.2
  • 20
    • 0030840881 scopus 로고    scopus 로고
    • High affinity glutamate transporters: Regulation of expression and activity
    • Gegelashvili G., Schousboe A. High affinity glutamate transporters: regulation of expression and activity. Mol. Pharmacol. 52:1997;6-15.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 6-15
    • Gegelashvili, G.1    Schousboe, A.2
  • 21
    • 0034257164 scopus 로고    scopus 로고
    • The high-affinity glutamate transporters GLT1, GLAST, and EAAT4 are regulated via different signalling mechanisms
    • Gegelashvili G., Dehnes Y., Danbolt N.C., Schousboe A. The high-affinity glutamate transporters GLT1, GLAST, and EAAT4 are regulated via different signalling mechanisms. Neurochem. Int. 37:2000;163-170.
    • (2000) Neurochem. Int. , vol.37 , pp. 163-170
    • Gegelashvili, G.1    Dehnes, Y.2    Danbolt, N.C.3    Schousboe, A.4
  • 22
    • 17644432338 scopus 로고    scopus 로고
    • Phorbol myristate acetate-dependent interaction of protein kinase C{alpha} and the neuronal glutamate transporter EAAC1
    • Gonzalez M.I., Bannerman P.G., Robinson M.B. Phorbol myristate acetate-dependent interaction of protein kinase C{alpha} and the neuronal glutamate transporter EAAC1. J. Neurosci. 23:2003;5589-5593.
    • (2003) J. Neurosci. , vol.23 , pp. 5589-5593
    • Gonzalez, M.I.1    Bannerman, P.G.2    Robinson, M.B.3
  • 23
    • 0034662861 scopus 로고    scopus 로고
    • Glutamate translocation of the neuronal glutamate transporter EAAC1 occurs within milliseconds
    • Grewer C., Watzke N., Wiessner M., Rauen T. Glutamate translocation of the neuronal glutamate transporter EAAC1 occurs within milliseconds. Proc. Natl. Acad. Sci. U. S. A. 97:2000;9706-9711.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9706-9711
    • Grewer, C.1    Watzke, N.2    Wiessner, M.3    Rauen, T.4
  • 24
    • 0034737622 scopus 로고    scopus 로고
    • The accessibility of a novel reentrant loop of the glutamate transporter GLT-1 is restricted by its substrate
    • Grunewald M., Kanner B.I. The accessibility of a novel reentrant loop of the glutamate transporter GLT-1 is restricted by its substrate. J. Biol. Chem. 275:2000;9684-9689.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9684-9689
    • Grunewald, M.1    Kanner, B.I.2
  • 25
    • 0032169137 scopus 로고    scopus 로고
    • Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology
    • Grunewald M., Bendahan A., Kanner B.I. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Neuron. 21:1998;623-632.
    • (1998) Neuron , vol.21 , pp. 623-632
    • Grunewald, M.1    Bendahan, A.2    Kanner, B.I.3
  • 26
    • 0002639306 scopus 로고    scopus 로고
    • Neurotrophic factors protect cortical synaptic terminals against amyloid and oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function
    • Guo Z.H., Mattson M.P. Neurotrophic factors protect cortical synaptic terminals against amyloid and oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function. Cereb. Cortex. 10:2000;50-57.
    • (2000) Cereb. Cortex , vol.10 , pp. 50-57
    • Guo, Z.H.1    Mattson, M.P.2
  • 27
    • 0036939520 scopus 로고    scopus 로고
    • Human glioma cells and undifferentiated primary astrocytes that express aberrant EAAT2 mRNA inhibit normal EAAT2 protein expression and prevent cell death
    • Guo H., Lai L., Butchbach M.E., Lin C.L. Human glioma cells and undifferentiated primary astrocytes that express aberrant EAAT2 mRNA inhibit normal EAAT2 protein expression and prevent cell death. Mol. Cell. Neurosci. 21:2002;546-560.
    • (2002) Mol. Cell. Neurosci. , vol.21 , pp. 546-560
    • Guo, H.1    Lai, L.2    Butchbach, M.E.3    Lin, C.L.4
  • 28
    • 0034554777 scopus 로고    scopus 로고
    • Exacerbation of noise-induced hearing loss in mice lacking the glutamate transporter GLAST
    • Hakuba N., Koga K., Gyo K., Usami S.I., Tanaka K. Exacerbation of noise-induced hearing loss in mice lacking the glutamate transporter GLAST. J. Neurosci. 20:2000;8750-8753.
    • (2000) J. Neurosci. , vol.20 , pp. 8750-8753
    • Hakuba, N.1    Koga, K.2    Gyo, K.3    Usami, S.I.4    Tanaka, K.5
  • 30
    • 0032749353 scopus 로고    scopus 로고
    • Glutamate transporters in kidney and brain
    • Hediger M.A. Glutamate transporters in kidney and brain. Am. J. Physiol. 277:1999;F487-F492.
    • (1999) Am. J. Physiol. , vol.277
    • Hediger, M.A.1
  • 31
    • 0032741947 scopus 로고    scopus 로고
    • Introduction: Glutamate transport, metabolism, and physiological responses
    • Hediger M.A., Welbourne T.C. Introduction: glutamate transport, metabolism, and physiological responses. Am. J. Physiol. 277:1999;F477-F480.
    • (1999) Am. J. Physiol. , vol.277
    • Hediger, M.A.1    Welbourne, T.C.2
  • 32
    • 0024294163 scopus 로고
    • Electrogenicity of sodium/L-glutamate cotransport in rabbit renal brush-border membranes: A reevaluation
    • Heinz E., Sommerfeld D.L., Kinne R.K. Electrogenicity of sodium/L-glutamate cotransport in rabbit renal brush-border membranes: a reevaluation. Biochim. Biophys. Acta. 937:1988;300-308.
    • (1988) Biochim. Biophys. Acta , vol.937 , pp. 300-308
    • Heinz, E.1    Sommerfeld, D.L.2    Kinne, R.K.3
  • 33
    • 0034711151 scopus 로고    scopus 로고
    • Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls
    • Honig L.S., Chambliss D.D., Bigio E.H., Carroll S.L., Elliott J.L. Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls. Neurology. 55:2000;1082-1088.
    • (2000) Neurology , vol.55 , pp. 1082-1088
    • Honig, L.S.1    Chambliss, D.D.2    Bigio, E.H.3    Carroll, S.L.4    Elliott, J.L.5
  • 34
    • 0027369524 scopus 로고
    • The uptake inhibitor L-trans-PDC enhances responses to glutamate but fails to alter the kinetics of excitatory synaptic currents in the hippocampus
    • Isaacson J.S., Nicoll R.A. The uptake inhibitor L-trans-PDC enhances responses to glutamate but fails to alter the kinetics of excitatory synaptic currents in the hippocampus. J. Neurophysiol. 70:1993;2187-2191.
    • (1993) J. Neurophysiol. , vol.70 , pp. 2187-2191
    • Isaacson, J.S.1    Nicoll, R.A.2
  • 36
    • 0030858918 scopus 로고    scopus 로고
    • Family of neutral and acidic amino acid transporters: Molecular biology, physiology and medical implications
    • Kanai Y. Family of neutral and acidic amino acid transporters: molecular biology, physiology and medical implications. Curr. Opin. Cell Biol. 9:1997;565-572.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 565-572
    • Kanai, Y.1
  • 37
    • 0026458124 scopus 로고
    • Primary structure and functional characterization of a high-affinity glutamate transporter
    • Kanai Y., Hediger M.A. Primary structure and functional characterization of a high-affinity glutamate transporter. Nature. 360:1992;467-471.
    • (1992) Nature , vol.360 , pp. 467-471
    • Kanai, Y.1    Hediger, M.A.2
  • 38
    • 0003256875 scopus 로고    scopus 로고
    • High-affinity glutamate transporters: Physiological and pathophysiological relevance in the central nervous system
    • D.W. Brann, Mahesh V.B. Boca Raton: CRC Press
    • Kanai Y., Hediger M.A. High-affinity glutamate transporters: physiological and pathophysiological relevance in the central nervous system. Brann D.W., Mahesh V.B. Excitatory Amino Acids: Their Role in Neuroendocrine Function. vol. 1995:2001;103-131 CRC Press, Boca Raton.
    • (2001) Excitatory Amino Acids: Their Role in Neuroendocrine Function , vol.1995 , pp. 103-131
    • Kanai, Y.1    Hediger, M.A.2
  • 39
    • 0028124811 scopus 로고
    • The neuronal and epithelial human high affinity glutamate transporter. Insights into structure and mechanism of transport
    • Kanai Y., Stelzner M., Nussberger S., Khawaja S., Hebert S.C., Smith C.P., Hediger M.A. The neuronal and epithelial human high affinity glutamate transporter. Insights into structure and mechanism of transport. J. Biol. Chem. 269:1994;20599-20606.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20599-20606
    • Kanai, Y.1    Stelzner, M.2    Nussberger, S.3    Khawaja, S.4    Hebert, S.C.5    Smith, C.P.6    Hediger, M.A.7
  • 40
    • 0029586025 scopus 로고
    • Neuronal high-affinity glutamate transport in the rat central nervous system
    • Kanai Y., Bhide P.G., DiFiglia M., Hediger M.A. Neuronal high-affinity glutamate transport in the rat central nervous system. NeuroReport. 6:1995;2357-2362.
    • (1995) NeuroReport , vol.6 , pp. 2357-2362
    • Kanai, Y.1    Bhide, P.G.2    DiFiglia, M.3    Hediger, M.A.4
  • 41
    • 0029035583 scopus 로고
    • Electrogenic properties of the epithelial and neuronal high affinity glutamate transporter
    • Kanai Y., Nussberger S., Romero M.F., Boron W.F., Hebert S.C., Hediger M.A. Electrogenic properties of the epithelial and neuronal high affinity glutamate transporter. J. Biol. Chem. 270:1995;16561-16568.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16561-16568
    • Kanai, Y.1    Nussberger, S.2    Romero, M.F.3    Boron, W.F.4    Hebert, S.C.5    Hediger, M.A.6
  • 42
    • 0031028206 scopus 로고    scopus 로고
    • Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange
    • Kavanaugh M.P., Bendahan A., Zerangue N., Zhang Y., Kanner B.I. Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange. J. Biol. Chem. 272:1997;1703-1708.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1703-1708
    • Kavanaugh, M.P.1    Bendahan, A.2    Zerangue, N.3    Zhang, Y.4    Kanner, B.I.5
  • 43
    • 0029744420 scopus 로고    scopus 로고
    • Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line
    • Kekuda R., Prasad P.D., Fei Y.J., Torres-Zamorano V., Sinha S., Yang-Feng T.L., Leibach F.H., Ganapathy V. Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line. J. Biol. Chem. 271:1996;18657-18661.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18657-18661
    • Kekuda, R.1    Prasad, P.D.2    Fei, Y.J.3    Torres-Zamorano, V.4    Sinha, S.5    Yang-Feng, T.L.6    Leibach, F.H.7    Ganapathy, V.8
  • 44
    • 0027165152 scopus 로고
    • Electrogenic L-glutamate uptake in Xenopus laevis oocytes expressing a cloned rat brain L-glutamate/L-aspartate transporter (GLAST-1)
    • Klockner U., Storck T., Conradt M., Stoffel W. Electrogenic L-glutamate uptake in Xenopus laevis oocytes expressing a cloned rat brain L-glutamate/L-aspartate transporter (GLAST-1). J. Biol. Chem. 268:1993;14594-14596.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14594-14596
    • Klockner, U.1    Storck, T.2    Conradt, M.3    Stoffel, W.4
  • 45
    • 0032400828 scopus 로고    scopus 로고
    • Stoichiometry of the glial glutamate transporter GLT-1 expressed inducibly in a Chinese hamster ovary cell line selected for low endogenous Na+-dependent glutamate uptake
    • Levy L.M., Warr O., Attwell D. Stoichiometry of the glial glutamate transporter GLT-1 expressed inducibly in a Chinese hamster ovary cell line selected for low endogenous Na+-dependent glutamate uptake. J. Neurosci. 18:1998;9620-9628.
    • (1998) J. Neurosci. , vol.18 , pp. 9620-9628
    • Levy, L.M.1    Warr, O.2    Attwell, D.3
  • 46
    • 0032032013 scopus 로고    scopus 로고
    • Aberrant RNA processing in a neurodegenerative disease: The cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis
    • Lin C.L., Bristol L.A., Jin L., Dykes-Hoberg M., Crawford T., Clawson L., Rothstein J.D. Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. Neuron. 20:1998;589-602.
    • (1998) Neuron , vol.20 , pp. 589-602
    • Lin, C.L.1    Bristol, L.A.2    Jin, L.3    Dykes-Hoberg, M.4    Crawford, T.5    Clawson, L.6    Rothstein, J.D.7
  • 48
    • 0032869056 scopus 로고    scopus 로고
    • Placental anionic and cationic amino acid transporter expression in growth hormone overexpressing and null IGF-II or null IGF-I receptor mice
    • Matthews J.C., Beveridge M.J., Dialynas E., Bartke A., Kilberg M.S., Novak D.A. Placental anionic and cationic amino acid transporter expression in growth hormone overexpressing and null IGF-II or null IGF-I receptor mice. Placenta. 20:1999;639-650.
    • (1999) Placenta , vol.20 , pp. 639-650
    • Matthews, J.C.1    Beveridge, M.J.2    Dialynas, E.3    Bartke, A.4    Kilberg, M.S.5    Novak, D.A.6
  • 49
    • 0028349645 scopus 로고
    • Glial contributions to excitatory neurotransmission in cultured hippocampal cells
    • Mennerick S., Zorumski C.F. Glial contributions to excitatory neurotransmission in cultured hippocampal cells. Nature. 368:1994;59-62.
    • (1994) Nature , vol.368 , pp. 59-62
    • Mennerick, S.1    Zorumski, C.F.2
  • 51
    • 0030993144 scopus 로고    scopus 로고
    • EAAT4, a glutamate transporter with properties of a chloride channel, is predominantly localized in Purkinje cell dendrites, and forms parasagittal compartments in rat cerebellum
    • Nagao S., Kwak S., Kanazawa I. EAAT4, a glutamate transporter with properties of a chloride channel, is predominantly localized in Purkinje cell dendrites, and forms parasagittal compartments in rat cerebellum. Neuroscience. 78:1997;929-933.
    • (1997) Neuroscience , vol.78 , pp. 929-933
    • Nagao, S.1    Kwak, S.2    Kanazawa, I.3
  • 52
    • 0034655871 scopus 로고    scopus 로고
    • Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2
    • Otis T.S., Kavanaugh M.P. Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2. J. Neurosci. 20:2000;2749-2757.
    • (2000) J. Neurosci. , vol.20 , pp. 2749-2757
    • Otis, T.S.1    Kavanaugh, M.P.2
  • 53
    • 0032818544 scopus 로고    scopus 로고
    • Wnt signaling induces GLT-1 expression in rat C6 glioma cells
    • Palos T.P., Zheng S., Howard B.D. Wnt signaling induces GLT-1 expression in rat C6 glioma cells. J. Neurochem. 73:1999;1012-1023.
    • (1999) J. Neurochem. , vol.73 , pp. 1012-1023
    • Palos, T.P.1    Zheng, S.2    Howard, B.D.3
  • 54
    • 0031768026 scopus 로고    scopus 로고
    • Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients
    • Pedersen W.A., Fu W., Keller J.N., Markesbery W.R., Appel S., Smith R.G., Kasarskis E., Mattson M.P. Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients. Ann. Neurol. 44:1998;819-824.
    • (1998) Ann. Neurol. , vol.44 , pp. 819-824
    • Pedersen, W.A.1    Fu, W.2    Keller, J.N.3    Markesbery, W.R.4    Appel, S.5    Smith, R.G.6    Kasarskis, E.7    Mattson, M.P.8
  • 55
    • 0030976929 scopus 로고    scopus 로고
    • Glutamate transporter EAAC-1-deficient mice develop dicarboxylic aminoaciduria and behavioral abnormalities but no neurodegeneration
    • Peghini P., Janzen J., Stoffel W. Glutamate transporter EAAC-1-deficient mice develop dicarboxylic aminoaciduria and behavioral abnormalities but no neurodegeneration. EMBO J. 16:1997;3822-3832.
    • (1997) EMBO J. , vol.16 , pp. 3822-3832
    • Peghini, P.1    Janzen, J.2    Stoffel, W.3
  • 57
    • 0033979558 scopus 로고    scopus 로고
    • Developmental expression of excitatory amino acid transporter 5: A photoreceptor and bipolar cell glutamate transporter in rat retina
    • Pow D.V., Barnett N.L. Developmental expression of excitatory amino acid transporter 5: a photoreceptor and bipolar cell glutamate transporter in rat retina. Neurosci. Lett. 280:2000;21-24.
    • (2000) Neurosci. Lett. , vol.280 , pp. 21-24
    • Pow, D.V.1    Barnett, N.L.2
  • 58
    • 0034257045 scopus 로고    scopus 로고
    • Are neuronal transporters relevant in retinal glutamate homeostasis?
    • Pow D.V., Barnett N.L., Penfold P. Are neuronal transporters relevant in retinal glutamate homeostasis? Neurochem. Int. 37:2000;191-198.
    • (2000) Neurochem. Int. , vol.37 , pp. 191-198
    • Pow, D.V.1    Barnett, N.L.2    Penfold, P.3
  • 62
    • 0034688312 scopus 로고    scopus 로고
    • Glutamate release in severe brain ischaemia is mainly by reversed uptake
    • Rossi D.J., Oshima T., Attwell D. Glutamate release in severe brain ischaemia is mainly by reversed uptake. Nature. 403:2000;316-321.
    • (2000) Nature , vol.403 , pp. 316-321
    • Rossi, D.J.1    Oshima, T.2    Attwell, D.3
  • 65
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein J.D., Van Kammen M., Levey A.I., Martin L.J., Kuncl R.W. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann. Neurol. 38:1995;73-84.
    • (1995) Ann. Neurol. , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3    Martin, L.J.4    Kuncl, R.W.5
  • 67
    • 0037439780 scopus 로고    scopus 로고
    • Neutral amino acid transporter ASCT1 is preferentially expressed in L-Ser-synthetic/storing glial cells in the mouse brain with transient expression in developing capillaries
    • Sakai K., Shimizu H., Koike T., Furuya S., Watanabe M. Neutral amino acid transporter ASCT1 is preferentially expressed in L-Ser-synthetic/storing glial cells in the mouse brain with transient expression in developing capillaries. J. Neurosci. 23:2003;550-560.
    • (2003) J. Neurosci. , vol.23 , pp. 550-560
    • Sakai, K.1    Shimizu, H.2    Koike, T.3    Furuya, S.4    Watanabe, M.5
  • 68
    • 0027375540 scopus 로고
    • Glutamate uptake from the synaptic cleft does not shape the decay of the non-NMDA component of the synaptic current
    • Sarantis M., Ballerini L., Miller B., Silver R.A., Edwards M., Attwell D. Glutamate uptake from the synaptic cleft does not shape the decay of the non-NMDA component of the synaptic current. Neuron. 11:1993;541-549.
    • (1993) Neuron , vol.11 , pp. 541-549
    • Sarantis, M.1    Ballerini, L.2    Miller, B.3    Silver, R.A.4    Edwards, M.5    Attwell, D.6
  • 70
    • 0033681163 scopus 로고    scopus 로고
    • A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines
    • Seal R.P., Leighton B.H., Amara S.G. A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines. Neuron. 25:2000;695-706.
    • (2000) Neuron , vol.25 , pp. 695-706
    • Seal, R.P.1    Leighton, B.H.2    Amara, S.G.3
  • 73
    • 0034681452 scopus 로고    scopus 로고
    • Platelet-derived growth factor rapidly increases activity and cell surface expression of the EAAC1 subtype of glutamate transporter through activation of phosphatidylinositol 3-kinase
    • Sims K.D., Straff D.J., Robinson M.B. Platelet-derived growth factor rapidly increases activity and cell surface expression of the EAAC1 subtype of glutamate transporter through activation of phosphatidylinositol 3-kinase. J. Biol. Chem. 275:2000;5228-5237.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5228-5237
    • Sims, K.D.1    Straff, D.J.2    Robinson, M.B.3
  • 74
    • 0026489330 scopus 로고
    • Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain
    • Storck T., Schulte S., Hofmann K., Stoffel W. Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain. Proc. Natl. Acad. Sci. U. S. A. 89:1992;10955-10959.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10955-10959
    • Storck, T.1    Schulte, S.2    Hofmann, K.3    Stoffel, W.4
  • 76
    • 0030001740 scopus 로고    scopus 로고
    • Expressed human hippocampal ASCT1 amino acid transporter exhibits a pH-dependent change in substrate specificity
    • Tamarappoo B.K., McDonald K.K., Kilberg M.S. Expressed human hippocampal ASCT1 amino acid transporter exhibits a pH-dependent change in substrate specificity. Biochim. Biophys. Acta. 1279:1996;131-136.
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 131-136
    • Tamarappoo, B.K.1    McDonald, K.K.2    Kilberg, M.S.3
  • 78
    • 0028061339 scopus 로고
    • Block of glutamate transporters potentiates postsynaptic excitation
    • Tong G., Jahr C.E. Block of glutamate transporters potentiates postsynaptic excitation. Neuron. 13:1994;1195-1203.
    • (1994) Neuron , vol.13 , pp. 1195-1203
    • Tong, G.1    Jahr, C.E.2
  • 79
    • 0033366461 scopus 로고    scopus 로고
    • SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter
    • Trotti D., Rolfs A., Danbolt N.C., Brown R.H. Jr., Hediger M.A. SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. Nat. Neurosci. 2:1999;848.
    • (1999) Nat. Neurosci. , vol.2 , pp. 848
    • Trotti, D.1    Rolfs, A.2    Danbolt, N.C.3    Brown Jr., R.H.4    Hediger, M.A.5
  • 80
    • 0035964851 scopus 로고    scopus 로고
    • Inhibition of the glutamate transporter EAAC1 expressed in Xenopus oocytes by phorbol esters
    • Trotti D., Peng J.B., Dunlop J., Hediger M.A. Inhibition of the glutamate transporter EAAC1 expressed in Xenopus oocytes by phorbol esters. Brain Res. 914:2001;196-203.
    • (2001) Brain Res. , vol.914 , pp. 196-203
    • Trotti, D.1    Peng, J.B.2    Dunlop, J.3    Hediger, M.A.4
  • 82
    • 0030716859 scopus 로고    scopus 로고
    • Tissue specific variants of glutamate transporter GLT-1
    • Utsunomiya-Tate N., Endou H., Kanai Y. Tissue specific variants of glutamate transporter GLT-1. FEBS Lett. 416:1997;312-316.
    • (1997) FEBS Lett. , vol.416 , pp. 312-316
    • Utsunomiya-Tate, N.1    Endou, H.2    Kanai, Y.3
  • 83
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport
    • Wadiche J.I., Amara S.G., Kavanaugh M.P. Ion fluxes associated with excitatory amino acid transport. Neuron. 15:1995;721-728.
    • (1995) Neuron , vol.15 , pp. 721-728
    • Wadiche, J.I.1    Amara, S.G.2    Kavanaugh, M.P.3
  • 85
    • 0032873812 scopus 로고    scopus 로고
    • Amygdala-kindled and pentylenetetrazole-induced seizures in glutamate transporter GLAST-deficient mice
    • Watanabe T., Morimoto K., Hirao T., Suwaki H., Watase K., Tanaka K. Amygdala-kindled and pentylenetetrazole-induced seizures in glutamate transporter GLAST-deficient mice. Brain Res. 845:1999;92-96.
    • (1999) Brain Res. , vol.845 , pp. 92-96
    • Watanabe, T.1    Morimoto, K.2    Hirao, T.3    Suwaki, H.4    Watase, K.5    Tanaka, K.6
  • 87
    • 0034038270 scopus 로고    scopus 로고
    • Epidermal growth factor receptor agonists increase expression of glutamate transporter GLT-1 in astrocytes through pathways dependent on phosphatidylinositol 3-kinase and transcription factor NF-kappaB
    • Zelenaia O., Schlag B.D., Gochenauer G.E., Ganel R., Song W., Beesley J.S., Grinspan J.B., Rothstein J.D., Robinson M.B. Epidermal growth factor receptor agonists increase expression of glutamate transporter GLT-1 in astrocytes through pathways dependent on phosphatidylinositol 3-kinase and transcription factor NF-kappaB. Mol. Pharmacol. 57:2000;667-678.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 667-678
    • Zelenaia, O.1    Schlag, B.D.2    Gochenauer, G.E.3    Ganel, R.4    Song, W.5    Beesley, J.S.6    Grinspan, J.B.7    Rothstein, J.D.8    Robinson, M.B.9
  • 88
    • 0029903720 scopus 로고    scopus 로고
    • ASCT-1 is a neutral amino acid exchanger with chloride channel activity
    • Zerangue N., Kavanaugh M.P. ASCT-1 is a neutral amino acid exchanger with chloride channel activity. J. Biol. Chem. 271:1996;27991-27994.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27991-27994
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 89
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue N., Kavanaugh M.P. Flux coupling in a neuronal glutamate transporter. Nature. 383:1996;634-637.
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 90
    • 0029891464 scopus 로고    scopus 로고
    • Interaction of L-cysteine with a human excitatory amino acid transporter
    • Zerangue N., Kavanaugh M.P. Interaction of L-cysteine with a human excitatory amino acid transporter. J. Physiol. 493(Pt 2):1996;419-423.
    • (1996) J. Physiol , vol.493 , Issue.2 PART , pp. 419-423
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 91
    • 0033573907 scopus 로고    scopus 로고
    • Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitter
    • Zhang Y., Kanner B.I. Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitter. Proc. Natl. Acad. Sci. U. S. A. 96:1999;1710-1715.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1710-1715
    • Zhang, Y.1    Kanner, B.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.