메뉴 건너뛰기




Volumn 50, Issue 4, 1996, Pages 701-708

Activation of N-methyl-D-aspartate receptors by glycine: Role of an aspartate residue in the M3-M4 loop of the NR1 subunit

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; GLYCINE; IFENPRODIL; MUTANT PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PARTIAL AGONIST; RECEPTOR SUBUNIT; SPERMINE;

EID: 0029921964     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (74)

References (36)
  • 1
    • 0024829451 scopus 로고
    • Excitatory amino acid receptors in the vertebrate central nervous system
    • Collingridge, G. L., and R. A. J. Lester. Excitatory amino acid receptors in the vertebrate central nervous system. Pharmacol. Rev. 41:143-210 (1989).
    • (1989) Pharmacol. Rev. , vol.41 , pp. 143-210
    • Collingridge, G.L.1    Lester, R.A.J.2
  • 2
    • 0024093449 scopus 로고
    • Glutamate neurotoxicity and diseases of the nervous system
    • Choi, D. W. Glutamate neurotoxicity and diseases of the nervous system. Neuron 1:623-634 (1988).
    • (1988) Neuron , vol.1 , pp. 623-634
    • Choi, D.W.1
  • 3
    • 0023091647 scopus 로고
    • Glycine potentiates the NMDA response in cultured mouse brain neurons
    • Johnson, J. W., and P. Ascher. Glycine potentiates the NMDA response in cultured mouse brain neurons. Nature (Lond.) 325:529-531 (1987).
    • (1987) Nature (Lond.) , vol.325 , pp. 529-531
    • Johnson, J.W.1    Ascher, P.2
  • 4
    • 0023754192 scopus 로고
    • Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes
    • Kleckner, N. W., and R. Dingledine. Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes. Science (Washington D. C.) 241:835-837 (1988).
    • (1988) Science (Washington D. C.) , vol.241 , pp. 835-837
    • Kleckner, N.W.1    Dingledine, R.2
  • 5
    • 0027469106 scopus 로고
    • The glycine site of the NMDA receptor: Five years on
    • Kemp, J. A., and P. D. Leeson. The glycine site of the NMDA receptor: five years on. Trends Pharmacol. Sci. 14:20-25 (1993).
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 20-25
    • Kemp, J.A.1    Leeson, P.D.2
  • 8
    • 0028340001 scopus 로고
    • Molecular diversity and functions of glutamate receptors
    • Nakanishi, S., and M. Masu. Molecular diversity and functions of glutamate receptors. Annu. Rev. Biophys. Biomol. Struct. 23:319-348 (1994).
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 319-348
    • Nakanishi, S.1    Masu, M.2
  • 13
    • 0028795941 scopus 로고
    • Recombinant human NMDA homomeric NR1 receptors expressed in mammalian cells form a high-affinity glycine antagonist binding site
    • Grimwood, S., B. L. Bourdellès, and P. J. Whiting. Recombinant human NMDA homomeric NR1 receptors expressed in mammalian cells form a high-affinity glycine antagonist binding site. J. Neurochem. 64:525-530 (1995).
    • (1995) J. Neurochem. , vol.64 , pp. 525-530
    • Grimwood, S.1    Bourdellès, B.L.2    Whiting, P.J.3
  • 14
    • 0028284469 scopus 로고
    • Mutational analysis of the glycine-binding site of the NMDA receptor: Structural similarity with bacterial amino acid-binding proteins
    • Kuryatov, A., B. Laube, H. Betz, and J. Kuhse. Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins. Neuron 12:1291-1300 (1994).
    • (1994) Neuron , vol.12 , pp. 1291-1300
    • Kuryatov, A.1    Laube, B.2    Betz, H.3    Kuhse, J.4
  • 15
    • 0028921951 scopus 로고
    • Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site
    • Wafford, K. A., M. Kathoria, C. J. Bain, G. Marshall, B. Le Bourdellès, J. A. Kemp, and P. J. Whiting. Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site. Mol. Pharmacol. 47:374-380 (1995).
    • (1995) Mol. Pharmacol. , vol.47 , pp. 374-380
    • Wafford, K.A.1    Kathoria, M.2    Bain, C.J.3    Marshall, G.4    Le Bourdellès, B.5    Kemp, J.A.6    Whiting, P.J.7
  • 16
    • 0029561009 scopus 로고
    • An acidic amino acid in the N-methyl-D-aspartate receptor that is important for spermine stimulation
    • Williams, K., K. Kashiwagi, J. Fukuchi, and K. Igarashi. An acidic amino acid in the N-methyl-D-aspartate receptor that is important for spermine stimulation. Mol. Pharmacol. 48:1087-1098 (1995).
    • (1995) Mol. Pharmacol. , vol.48 , pp. 1087-1098
    • Williams, K.1    Kashiwagi, K.2    Fukuchi, J.3    Igarashi, K.4
  • 17
    • 0029945013 scopus 로고    scopus 로고
    • An aspartate residue in the extracellular loop of the N-methyl-D-aspartate receptor controls sensitivity to spermine and protons
    • Kashiwagi, K., J. Fukuchi, J. Chao, K. Igarashi, and K. Williams. An aspartate residue in the extracellular loop of the N-methyl-D-aspartate receptor controls sensitivity to spermine and protons. Mol. Pharmacol. 49:1131-1141 (1996).
    • (1996) Mol. Pharmacol. , vol.49 , pp. 1131-1141
    • Kashiwagi, K.1    Fukuchi, J.2    Chao, J.3    Igarashi, K.4    Williams, K.5
  • 18
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119 (1985).
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 19
    • 0023613953 scopus 로고
    • Rapid and efficient sitespecific mutagenesis without phenotypic selection
    • Kunkel, T., J. D. Roberts, and R. A. Zakour. Rapid and efficient sitespecific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-382 (1987).
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.1    Roberts, J.D.2    Zakour, R.A.3
  • 20
    • 0026737236 scopus 로고
    • Rapid high-efficiency sitedirected mutagenesis by the phosphorothioate approach
    • Sayers, J. R., C. Krekel, and F. Eckstein. Rapid high-efficiency sitedirected mutagenesis by the phosphorothioate approach. Biotechniques 13:592-596 (1992).
    • (1992) Biotechniques , vol.13 , pp. 592-596
    • Sayers, J.R.1    Krekel, C.2    Eckstein, F.3
  • 22
    • 0028069856 scopus 로고
    • Mechanisms influencing stimulatory effects of spermine at recombinant N-methyl-D-aspartate receptors
    • Williams, K. Mechanisms influencing stimulatory effects of spermine at recombinant N-methyl-D-aspartate receptors. Mol. Pharmacol. 46:161-168 (1994).
    • (1994) Mol. Pharmacol. , vol.46 , pp. 161-168
    • Williams, K.1
  • 23
    • 0027405347 scopus 로고
    • Developmental switch in the expression of NMDA receptors occurs in vivo and in vitro
    • Williams, K., S. L. Russell, Y. M. Shen, and P. B. Molinoff. Developmental switch in the expression of NMDA receptors occurs in vivo and in vitro. Neuron 10:267-278 (1993).
    • (1993) Neuron , vol.10 , pp. 267-278
    • Williams, K.1    Russell, S.L.2    Shen, Y.M.3    Molinoff, P.B.4
  • 24
    • 0027525324 scopus 로고
    • Ifenprodil discriminates subtypes of the N-methyl-D-aspartate receptor: Selectivity and mechanisms at recombinant heteromeric receptors
    • Williams, K. Ifenprodil discriminates subtypes of the N-methyl-D-aspartate receptor: selectivity and mechanisms at recombinant heteromeric receptors. Mol. Pharmacol. 44:851-859 (1993).
    • (1993) Mol. Pharmacol. , vol.44 , pp. 851-859
    • Williams, K.1
  • 25
    • 0025343312 scopus 로고
    • Apparent desensitization of NMDA responses in Xenopus oocytes involves calcium-dependent chloride current
    • Leonard, J. P., and S. R. Kelso. Apparent desensitization of NMDA responses in Xenopus oocytes involves calcium-dependent chloride current. Neuron 2:53-60 (1990).
    • (1990) Neuron , vol.2 , pp. 53-60
    • Leonard, J.P.1    Kelso, S.R.2
  • 26
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 percent inhibition (I50) of an enzyme reaction
    • Cheng, Y.-C., and W. H. Prusoff. Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 percent inhibition (I50) of an enzyme reaction. Biochem. Pharmacol. 22:3099-3108 (1973).
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.-C.1    Prusoff, W.H.2
  • 27
    • 0026766877 scopus 로고
    • Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing
    • Sugihara, H., K. Moriyoshi, T. Ishii, M. Masu, and S. Nakanishi. Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing. Biochem. Biophys. Res. Commun. 185:826-832 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 826-832
    • Sugihara, H.1    Moriyoshi, K.2    Ishii, T.3    Masu, M.4    Nakanishi, S.5
  • 29
    • 0028034803 scopus 로고
    • Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor
    • Sullivan, J. M., S. F. Traynelis, H.-S. V. Chen, W. Escobar, S. F. Heinemann, and S. A. Lipton. Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor. Neuron 13:929-936 (1994).
    • (1994) Neuron , vol.13 , pp. 929-936
    • Sullivan, J.M.1    Traynelis, S.F.2    Chen, H.-S.V.3    Escobar, W.4    Heinemann, S.F.5    Lipton, S.A.6
  • 30
    • 0011762235 scopus 로고    scopus 로고
    • Modulation and block of ion channels: A new biology of polyamines
    • in press
    • Williams, K. Modulation and block of ion channels: a new biology of polyamines. Cell. Signalling 8:in press (1996).
    • (1996) Cell. Signalling , vol.8
    • Williams, K.1
  • 31
    • 0029021010 scopus 로고
    • Control of proton sensitivity of the NMDA receptor by RNA splicing and polyamines
    • Traynelis, S. F., M. Hartley, and S. F. Heinemann. Control of proton sensitivity of the NMDA receptor by RNA splicing and polyamines. Science (Washington D. C.) 268:873-876 (1995).
    • (1995) Science (Washington D. C.) , vol.268 , pp. 873-876
    • Traynelis, S.F.1    Hartley, M.2    Heinemann, S.F.3
  • 32
    • 0026758178 scopus 로고
    • Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor
    • O'Leary, M. E., and M. M. White. Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor. J. Biol. Chem. 267:8360-8365 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 8360-8365
    • O'Leary, M.E.1    White, M.M.2
  • 33
    • 0028831226 scopus 로고
    • Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists
    • Rajendra, S., J. W. Lynch, K. D. Pierce, C. R. French, P. H. Barry, and P. R. Schofield. Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists. Neuron 14:169-175 (1995).
    • (1995) Neuron , vol.14 , pp. 169-175
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 34
    • 0028361803 scopus 로고
    • Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor
    • Rajendra, S., J. W. Lynch, K. D. Pierce, C. R. French, P. H. Barry, and P. R. Schofield. Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor. J. Biol. Chem. 269:18739-18742 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18739-18742
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 35
    • 0028016521 scopus 로고
    • Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia
    • Langosch, D., B. Laube, N. Rundström, V. Schmieden, J. Bormann, and H. Betz. Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia. EMBO J. 13:4223-4228 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4223-4228
    • Langosch, D.1    Laube, B.2    Rundström, N.3    Schmieden, V.4    Bormann, J.5    Betz, H.6
  • 36
    • 0024521588 scopus 로고
    • Regulation of NMDA receptor desensitization in mouse hippocampal neurons by glycine
    • Mayer, M. L., L. Vyklicky, and J. Clements. Regulation of NMDA receptor desensitization in mouse hippocampal neurons by glycine. Nature (Lond.) 338:425-427 (1989).
    • (1989) Nature (Lond.) , vol.338 , pp. 425-427
    • Mayer, M.L.1    Vyklicky, L.2    Clements, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.