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Volumn 49, Issue 6, 1996, Pages 1131-1141

An aspartate residue in the extracellular loop of the N-methyl-D-aspartate receptor controls sensitivity to spermine and protons

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; IFENPRODIL; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; SPERMINE;

EID: 0029945013     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (85)

References (50)
  • 3
    • 0027385330 scopus 로고
    • Multiple structural determinants of voltage-dependent magnesium block in recombinant NMDA receptors
    • Kawajiri, S., and R. Dingledine. Multiple structural determinants of voltage-dependent magnesium block in recombinant NMDA receptors. Neuropharmacology 32:1203-1211 (1993).
    • (1993) Neuropharmacology , vol.32 , pp. 1203-1211
    • Kawajiri, S.1    Dingledine, R.2
  • 4
    • 0027339551 scopus 로고
    • 2+ and channel blockers by a single amino acid substitution in the N-methyl-D-aspartate receptor
    • 2+ and channel blockers by a single amino acid substitution in the N-methyl-D-aspartate receptor. J. Biol. Chem. 268:410-415 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 410-415
    • Sakurada, K.1    Masu, M.2    Nakanishi, S.3
  • 5
    • 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
  • 6
    • 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
  • 8
    • 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
  • 9
    • 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. LeBourdellès, 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    LeBourdellès, B.5    Kemp, J.A.6    Whiting, P.J.7
  • 10
    • 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
  • 14
    • 0028559605 scopus 로고
    • Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid binding proteins
    • Stern-Bach, Y., B. Bettler, M. Hartley, P. O. Sheppard, P. J. O'Hara, and S. F. Heinemann. Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid binding proteins. Neuron 13:1345-1357 (1994).
    • (1994) Neuron , vol.13 , pp. 1345-1357
    • Stern-Bach, Y.1    Bettler, B.2    Hartley, M.3    Sheppard, P.O.4    O'Hara, P.J.5    Heinemann, S.F.6
  • 15
    • 0027323130 scopus 로고
    • Splice variants of the N-methyl-D-aspartate receptor NR1 identify domains involved in regulation by polyamines and protein kinase C
    • Durand, G. M., M. V. L. Bennett, and R. S. Zukin. Splice variants of the N-methyl-D-aspartate receptor NR1 identify domains involved in regulation by polyamines and protein kinase C. Proc. Natl. Acad. Sci. USA 90:6731-6736 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6731-6736
    • Durand, G.M.1    Bennett, M.V.L.2    Zukin, R.S.3
  • 16
    • 0028340993 scopus 로고
    • Sensitivity of the N-methyl-D-aspartate receptor to polyamines is controlled by NR2 subunits
    • Williams, K., A. M. Zappia, D. B. Pritchett, Y. M. Shen, and P. B. Molinoff. Sensitivity of the N-methyl-D-aspartate receptor to polyamines is controlled by NR2 subunits. Mol. Pharmacol. 45:803-809 (1994).
    • (1994) Mol. Pharmacol. , vol.45 , pp. 803-809
    • Williams, K.1    Zappia, A.M.2    Pritchett, D.B.3    Shen, Y.M.4    Molinoff, P.B.5
  • 17
    • 0002949270 scopus 로고
    • Modulation of NMDA receptors by polyamines
    • (R. A. Casero, ed.). R. G. Landes Co., Austin, TX
    • Williams, K. Modulation of NMDA receptors by polyamines, in Polyamines: Regulation and Molecular Interaction (R. A. Casero, ed.). R. G. Landes Co., Austin, TX, 129-170 (1995).
    • (1995) Polyamines: Regulation and Molecular Interaction , pp. 129-170
    • Williams, K.1
  • 18
    • 0025838225 scopus 로고
    • Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome
    • Furuchi, T., K. Kashiwagi, H. Kobayashi, and K. Igarashi. Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome. J. Biol. Chem. 266:20928-20933 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 20928-20933
    • Furuchi, T.1    Kashiwagi, K.2    Kobayashi, H.3    Igarashi, K.4
  • 19
    • 0027250513 scopus 로고
    • Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli
    • Kashiwagi, K., S. Miyamoto, E. Nukui, H. Kobayashi, and K. Igarashi. Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli. J. Biol. Chem. 268:19358-19363 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 19358-19363
    • Kashiwagi, K.1    Miyamoto, S.2    Nukui, E.3    Kobayashi, H.4    Igarashi, K.5
  • 20
    • 0028070407 scopus 로고
    • Properties and structure of spermidine acetyltransferase in Escherichia coli
    • Fukuchi, J., K. Kashiwagi, K. Takio, and K. Igarashi. Properties and structure of spermidine acetyltransferase in Escherichia coli. J. Biol. Chem. 269:22581-22585 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 22581-22585
    • Fukuchi, J.1    Kashiwagi, K.2    Takio, K.3    Igarashi, K.4
  • 21
    • 0028596211 scopus 로고
    • N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann, M., C. Maron, and S. Heinemann. N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron 13:1331-1343 (1994).
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 22
    • 0028364252 scopus 로고
    • Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation
    • Wo, Z. G., and R. E. Oswald. Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation. Proc. Natl. Acad. Sci. USA 91:7154-7158 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7154-7158
    • Wo, Z.G.1    Oswald, R.E.2
  • 23
    • 0028819612 scopus 로고
    • Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining reentrant membrane loop
    • Bennett, J. A., and R. Dingledine. Topology profile for a glutamate receptor: three transmembrane domains and a channel-lining reentrant membrane loop. Neuron 14:373-384 (1995).
    • (1995) Neuron , vol.14 , pp. 373-384
    • Bennett, J.A.1    Dingledine, R.2
  • 24
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo, Z. G., and R. E. Oswald. Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci. 18:161-168 (1995).
    • (1995) Trends Neurosci. , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2
  • 25
    • 0029933361 scopus 로고    scopus 로고
    • Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli
    • 24a. Sugiyama, S., D. G. Vassylyev, M. Matsushima, K. Kashiwagi, K. Igarashi, and K. Morikawa. Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. J. Biol. Chem. 271:9519-9525 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 9519-9525
    • Sugiyama, S.1    Vassylyev, D.G.2    Matsushima, M.3    Kashiwagi, K.4    Igarashi, K.5    Morikawa, K.6
  • 26
    • 0029083678 scopus 로고
    • Direct identification of a polyamine binding domain on the regulatory subunit of the protein casein kinase 2 by photoaffinity labeling
    • Leroy, D., N. Schmid, J-P. Behr, O. Filhol, S. Pares, J. Garin, J.-J. Bourgarit, E. M. Chambaz, and C. Cochet. Direct identification of a polyamine binding domain on the regulatory subunit of the protein casein kinase 2 by photoaffinity labeling. J. Biol. Chem. 270:17400-17406 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17400-17406
    • Leroy, D.1    Schmid, N.2    Behr, J.-P.3    Filhol, O.4    Pares, S.5    Garin, J.6    Bourgarit, J.-J.7    Chambaz, E.M.8    Cochet, C.9
  • 27
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S. B., and C. D. Wunsch. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:443-453 (1970).
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 28
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13 mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13 mp18 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
  • 29
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T., J. D. Roberts, and R. A. Zakour. Rapid and efficient site-specific 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
  • 30
    • 0026737236 scopus 로고
    • Rapid high-efficiency site-directed mutagenesis by the phosphorothioate approach
    • Sayers, J. R., C. Krekel, and F Eckstein. Rapid high-efficiency site-directed 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
  • 32
    • 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
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 37
    • 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
  • 39
    • 0028821024 scopus 로고
    • Pharmacological properties of recombinant N-methyl-D-aspartate (NMDA) receptors containing the ∈f (NR2D) subunit
    • Williams, K. Pharmacological properties of recombinant N-methyl-D-aspartate (NMDA) receptors containing the ∈f (NR2D) subunit. Neurosci. Lett. 184:181-184 (1995).
    • (1995) Neurosci. Lett. , vol.184 , pp. 181-184
    • Williams, K.1
  • 40
    • 0025315206 scopus 로고
    • Ifenprodil and SL 82.0715 as cerebral anti-ischemic agents. III. Evidence for antagonistic effects at the polyamine modulatory site within the N-methyl-D-aspartate receptor complex
    • Carter, C. J., K. G. Lloyd, B. Zivkovic, and B. Scatton. Ifenprodil and SL 82.0715 as cerebral anti-ischemic agents. III. Evidence for antagonistic effects at the polyamine modulatory site within the N-methyl-D-aspartate receptor complex. J. Pharmacol. Exp. Ther. 253:475-482 (1990).
    • (1990) J. Pharmacol. Exp. Ther. , vol.253 , pp. 475-482
    • Carter, C.J.1    Lloyd, K.G.2    Zivkovic, B.3    Scatton, B.4
  • 41
    • 0024316832 scopus 로고
    • Ifenprodil is a novel type of N-methyl-D-aspartate receptor antagonist: Interaction with polyamines
    • Reynolds, I. J., and R. J. Miller. Ifenprodil is a novel type of N-methyl-D-aspartate receptor antagonist: interaction with polyamines. Mol. Pharmacol. 36:758-765 (1989).
    • (1989) Mol. Pharmacol. , vol.36 , pp. 758-765
    • Reynolds, I.J.1    Miller, R.J.2
  • 42
    • 0025951641 scopus 로고
    • Ifenprodil blocks N-methyl-D-aspartate receptors by a two-component mechanism
    • Legendre, P., and G. L. Westbrook. Ifenprodil blocks N-methyl-D-aspartate receptors by a two-component mechanism. Mol. Pharmacol. 40:289-298 (1991).
    • (1991) Mol. Pharmacol. , vol.40 , pp. 289-298
    • Legendre, P.1    Westbrook, G.L.2
  • 43
    • 0027197230 scopus 로고
    • Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor
    • Hollmann, M., J. Boulter, C. Maron, L. Beasley, J. Sullivan, G. Pecht, and S. Heinemann. Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor. Neuron 10:943-954 (1993).
    • (1993) Neuron , vol.10 , pp. 943-954
    • Hollmann, M.1    Boulter, J.2    Maron, C.3    Beasley, L.4    Sullivan, J.5    Pecht, G.6    Heinemann, S.7
  • 44
    • 0024854473 scopus 로고
    • Spermine enhances binding to the glycine site associated with the N-methyl-D-aspartate receptor complex
    • Sacaan, A. I., and K. M. Johnson. Spermine enhances binding to the glycine site associated with the N-methyl-D-aspartate receptor complex. Mol. Pharmacol. 36:836-839 (1989).
    • (1989) Mol. Pharmacol. , vol.36 , pp. 836-839
    • Sacaan, A.I.1    Johnson, K.M.2
  • 45
    • 0027174665 scopus 로고
    • Multiple effects of spermine on N-methyl-D-aspartic acid receptor responses of rat cultured hippocampal neurones
    • Benveniste, M., and M. L. Mayer. Multiple effects of spermine on N-methyl-D-aspartic acid receptor responses of rat cultured hippocampal neurones. J. Physiol. (Lond.) 464:131-163 (1993).
    • (1993) J. Physiol. (Lond.) , vol.464 , pp. 131-163
    • Benveniste, M.1    Mayer, M.L.2
  • 46
    • 0026597543 scopus 로고
    • The polyamine spermine has multiple actions on N-methyl-D-aspartate receptor single-channel currents in cultured cortical neurons
    • Rock, D. M., and R. L. Macdonald. The polyamine spermine has multiple actions on N-methyl-D-aspartate receptor single-channel currents in cultured cortical neurons. Mol. Pharmacol. 41:83-88 (1992).
    • (1992) Mol. Pharmacol. , vol.41 , pp. 83-88
    • Rock, D.M.1    Macdonald, R.L.2
  • 47
    • 0027076784 scopus 로고
    • Spermine and related polyamines produce a voltage-dependent reduction of N-methyl-D-aspartate receptor single-channel conductance
    • Rock, D. M., and R. L. Macdonald. Spermine and related polyamines produce a voltage-dependent reduction of N-methyl-D-aspartate receptor single-channel conductance Mol. Pharmacol 42:157-164 (1992).
    • (1992) Mol. Pharmacol , vol.42 , pp. 157-164
    • Rock, D.M.1    Macdonald, R.L.2
  • 48
    • 0027245998 scopus 로고
    • Effects of polyamines on NMDA-induced currents in rat hippocampal neurons: A whole-cell and single-channel study
    • Araneda, R. C., R. S. Zukin, and M. V. L. Bennett. Effects of polyamines on NMDA-induced currents in rat hippocampal neurons: a whole-cell and single-channel study. Neurosci. Lett. 152:107-112 (1993).
    • (1993) Neurosci. Lett. , vol.152 , pp. 107-112
    • Araneda, R.C.1    Zukin, R.S.2    Bennett, M.V.L.3
  • 49
    • 0028926671 scopus 로고
    • Antagonist properties of polyamines and bis(ethyl)polyamines at N-methyl-D-aspartate receptors
    • Igarashi, K., and K. Williams. Antagonist properties of polyamines and bis(ethyl)polyamines at N-methyl-D-aspartate receptors. J. Pharmacol. Exp. Ther. 272:1101-1109 (1995).
    • (1995) J. Pharmacol. Exp. Ther. , vol.272 , pp. 1101-1109
    • Igarashi, K.1    Williams, K.2


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