메뉴 건너뛰기




Volumn 19, Issue 6, 1999, Pages 745-757

Determinants of phencyclidine potency on the nicotinic acetylcholine receptors from muscle and electric organ

Author keywords

Cembranoids; Electric organ; Eupalmerin acetate; Nicotinic acetylcholine receptor; Phencyclidine; Voltage clamp; Xenopus oocytes

Indexed keywords

NICOTINIC RECEPTOR; NICOTINIC RECEPTOR BLOCKING AGENT; PHENCYCLIDINE;

EID: 0032776666     PISSN: 02724340     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006905106834     Document Type: Article
Times cited : (14)

References (40)
  • 2
    • 0030785389 scopus 로고    scopus 로고
    • Topology of ligand binding sites on the nicotinic acetylcholine receptor
    • Arias, H. R. (1997). Topology of ligand binding sites on the nicotinic acetylcholine receptor. Brain Res. Rev. 25:133-191.
    • (1997) Brain Res. Rev. , vol.25 , pp. 133-191
    • Arias, H.R.1
  • 4
    • 0022558294 scopus 로고
    • Effects of chlorpromazine and phencyclidine on mouse C2 acetylcholine receptor kinetics
    • Changeux, J.-P., Pinset, C., and Ribera, A. B. (1986). Effects of chlorpromazine and phencyclidine on mouse C2 acetylcholine receptor kinetics. J. Physiol. 378:497-513.
    • (1986) J. Physiol. , vol.378 , pp. 497-513
    • Changeux, J.-P.1    Pinset, C.2    Ribera, A.B.3
  • 5
    • 0025355129 scopus 로고
    • An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetylcholine receptor
    • Charnet, P., Labarca, C., Leonard, R. J., Vogelaar, N. J., Czyzyk, L., Gouin, A, Davidson, N., and Lester, H. A. (1990). An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetylcholine receptor. Neuron 2:87-95.
    • (1990) Neuron , vol.2 , pp. 87-95
    • Charnet, P.1    Labarca, C.2    Leonard, R.J.3    Vogelaar, N.J.4    Czyzyk, L.5    Gouin, A.6    Davidson, N.7    Lester, H.A.8
  • 6
    • 0025291849 scopus 로고
    • 3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor
    • 3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor. J. Biol. Chem. 265:11017-11029.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11017-11029
    • DiPaola, M.1    Kao, P.N.2    Karlin, A.3
  • 7
    • 0025720089 scopus 로고
    • Binding sites of α-bungarotoxin and the noncompetitive inhibitor phencyclidine on a synthetic peptide comprising residues 172-227 of the α-subunit of the nicotinic acetylcholine receptor
    • Donnelly-Roberts, D. L., and Lentz, T. L. (1991). Binding sites of α-bungarotoxin and the noncompetitive inhibitor phencyclidine on a synthetic peptide comprising residues 172-227 of the α-subunit of the nicotinic acetylcholine receptor. Biochemistry 30:7484-7491.
    • (1991) Biochemistry , vol.30 , pp. 7484-7491
    • Donnelly-Roberts, D.L.1    Lentz, T.L.2
  • 8
    • 0030791139 scopus 로고    scopus 로고
    • Differential effects of dimethyl sulfoxide on nicotinic acetylcholine receptor from mouse muscle and Torpedo electrocytes
    • Eaton, M. J., Pagán, O. R., Hann, R. M., and Eterović, V. A. (1997). Differential effects of dimethyl sulfoxide on nicotinic acetylcholine receptor from mouse muscle and Torpedo electrocytes. Neurosci. Lett. 230:163-166.
    • (1997) Neurosci. Lett. , vol.230 , pp. 163-166
    • Eaton, M.J.1    Pagán, O.R.2    Hann, R.M.3    Eterović, V.A.4
  • 9
    • 0008936589 scopus 로고    scopus 로고
    • Differential effect of mutations in the M2 membrane spanning region of the nicotinic acetylcholine receptor on the action of phencyclidine at its high and low affinity sites
    • Eaton, M. J., Labarca C. G., and Eterović, V. A. (1998). Differential effect of mutations in the M2 membrane spanning region of the nicotinic acetylcholine receptor on the action of phencyclidine at its high and low affinity sites. Biophys. J. 74:A91.
    • (1998) Biophys. J. , vol.74
    • Eaton, M.J.1    Labarca, C.G.2    Eterović, V.A.3
  • 10
    • 0029363473 scopus 로고
    • Noncompetitive inhibitors of the acetylcholine receptor help paint a picture of its ion channel
    • Eterović, V. A., and Hann, R. M. (1995). Noncompetitive inhibitors of the acetylcholine receptor help paint a picture of its ion channel. Puerto Rico Health Sci. J. 14:199-209.
    • (1995) Puerto Rico Health Sci. J. , vol.14 , pp. 199-209
    • Eterović, V.A.1    Hann, R.M.2
  • 11
    • 0027215671 scopus 로고
    • Diterpenoids from Caribbean Gorgonians act as noncompetitive inhibitors of the nicotinic acetylcholine receptor
    • Eterović, V. A., Hann, R. M., Ferchmin, P. A., Rodríguez, A. D., Li, L., Lee, Y. H., and McNamee, M. G. (1993a). Diterpenoids from Caribbean Gorgonians act as noncompetitive inhibitors of the nicotinic acetylcholine receptor. Cell. Mol. Neurobiol. 13:99-110.
    • (1993) Cell. Mol. Neurobiol. , vol.13 , pp. 99-110
    • Eterović, V.A.1    Hann, R.M.2    Ferchmin, P.A.3    Rodríguez, A.D.4    Li, L.5    Lee, Y.H.6    McNamee, M.G.7
  • 12
    • 0027276473 scopus 로고
    • The ion channel of mouse and electric organ acetylcholine receptors: Differing affinities for noncompetitive inhibitors
    • Eterović, V. A., Li, L., Ferchmin, P. A., Lee, Y. H., Hann, R. M., Rodríguez, A. D., and McNamee, M. G. (1993b). The ion channel of mouse and electric organ acetylcholine receptors: Differing affinities for noncompetitive inhibitors. Cell. Mol. Neurobiol. 13:111-121.
    • (1993) Cell. Mol. Neurobiol. , vol.13 , pp. 111-121
    • Eterović, V.A.1    Li, L.2    Ferchmin, P.A.3    Lee, Y.H.4    Hann, R.M.5    Rodríguez, A.D.6    McNamee, M.G.7
  • 16
    • 0344701102 scopus 로고    scopus 로고
    • Sensitivity to voltage-independent inhibition determined by pore-lining region of the acetylcholine receptor
    • Francis, M. M., Choi, K., II, Horenstein, B. A., and Papke, R. L. (1998). Sensitivity to voltage-independent inhibition determined by pore-lining region of the acetylcholine receptor. Biophys. J. 74:2306-2317.
    • (1998) Biophys. J. , vol.74 , pp. 2306-2317
    • Francis, M.M.1    Choi K. II2    Horenstein, B.A.3    Papke, R.L.4
  • 21
    • 0020571248 scopus 로고
    • Species differences determine azido phencyclidine labeling pattern in desensitized nicotinic acetylcholine receptors
    • Haring, R., Kloog, Y., Kalir, A., and Sokolovsky, M. (1983). Species differences determine azido phencyclidine labeling pattern in desensitized nicotinic acetylcholine receptors. Biochem. Biophys. Res. Commun. 113:723-729.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 723-729
    • Haring, R.1    Kloog, Y.2    Kalir, A.3    Sokolovsky, M.4
  • 22
    • 0021248404 scopus 로고
    • Localization of phencyclidine binding sites on α and β subunits of the nicotinic acetylcholine receptor from Torpedo ocellata electric organ using azido phencyclidine
    • Haring, R., Kloog, Y., and Sokolovsky, M. (1984). Localization of phencyclidine binding sites on α and β subunits of the nicotinic acetylcholine receptor from Torpedo ocellata electric organ using azido phencyclidine. J. Neurosci. 4:627-637.
    • (1984) J. Neurosci. , vol.4 , pp. 627-637
    • Haring, R.1    Kloog, Y.2    Sokolovsky, M.3
  • 23
    • 0020621092 scopus 로고
    • Multiple sites of action for noncompetitive blockers on acetylcholine receptor rich membrane fragments from Torpedo marmorata
    • Heidmann, T., Oswald, R. E., and Changeux, J.-P. (1983). Multiple sites of action for noncompetitive blockers on acetylcholine receptor rich membrane fragments from Torpedo marmorata. Biochemistry 22:3112-3127.
    • (1983) Biochemistry , vol.22 , pp. 3112-3127
    • Heidmann, T.1    Oswald, R.E.2    Changeux, J.-P.3
  • 24
    • 0022458822 scopus 로고
    • The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices MII of the receptor subunits
    • Hucho, F., Oberthür, W., and Lottspeich, F. (1986). The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices MII of the receptor subunits. FEBS Lett. 205:137-142.
    • (1986) FEBS Lett. , vol.205 , pp. 137-142
    • Hucho, F.1    Oberthür, W.2    Lottspeich, F.3
  • 25
    • 0024918350 scopus 로고
    • Explorations of the nicotinic acetylcholine receptor
    • Wiley-Liss, New York
    • Karlin, A. (1991). Explorations of the nicotinic acetylcholine receptor. The Harvey Lectures, Series 85, Wiley-Liss, New York, pp. 71-107.
    • (1991) The Harvey Lectures, Series 85 , pp. 71-107
    • Karlin, A.1
  • 26
    • 0022477119 scopus 로고
    • Cocaine, phencyclidine, and procaine inhibition of the acetylcholine receptor: Characterization of the binding site by stopped-flow measurements of receptor-controlled ion flux in membrane vesicles
    • Karpen, J. W., and Hess, G. P. (1986). Cocaine, phencyclidine, and procaine inhibition of the acetylcholine receptor: characterization of the binding site by stopped-flow measurements of receptor-controlled ion flux in membrane vesicles. Biochemistry 25:1777-1785.
    • (1986) Biochemistry , vol.25 , pp. 1777-1785
    • Karpen, J.W.1    Hess, G.P.2
  • 27
    • 0021828535 scopus 로고
    • Aryldiazonium salts as photoaffinity labels of the nicotinic acetylcholine receptor PCP binding site
    • Kotzyba-Hibert, F., Langembuch-Cachat, J., Jaganathen, J., Goeldner, M., and Hirth, C. (1985). Aryldiazonium salts as photoaffinity labels of the nicotinic acetylcholine receptor PCP binding site. FEBS Lett. 182:297-301.
    • (1985) FEBS Lett. , vol.182 , pp. 297-301
    • Kotzyba-Hibert, F.1    Langembuch-Cachat, J.2    Jaganathen, J.3    Goeldner, M.4    Hirth, C.5
  • 28
    • 0031059313 scopus 로고    scopus 로고
    • Quinacrine and ethidium bromide bind the same locus on the nicotinic acetylcholine receptor from Torpedo californica
    • Lurtz, M. M., Hareland, M. L., and Pedersen, S. E. (1997). Quinacrine and ethidium bromide bind the same locus on the nicotinic acetylcholine receptor from Torpedo californica. Biochemistry 36:2068-2075.
    • (1997) Biochemistry , vol.36 , pp. 2068-2075
    • Lurtz, M.M.1    Hareland, M.L.2    Pedersen, S.E.3
  • 29
    • 0023186820 scopus 로고
    • Localization of azidophencyclidine-binding site on the nicotinic acetylcholine receptor alpha-subunit
    • Mosckovitz, R., Haring, R., Gershoni, J. M., Kloog, Y., and Sokolovsky, M. (1987). Localization of azidophencyclidine-binding site on the nicotinic acetylcholine receptor alpha-subunit, Biochem. Biophys. Res. Commun. 145:810-816.
    • (1987) Biochem. Biophys. Res. Commun. , vol.145 , pp. 810-816
    • Mosckovitz, R.1    Haring, R.2    Gershoni, J.M.3    Kloog, Y.4    Sokolovsky, M.5
  • 30
    • 0022758905 scopus 로고
    • The reaction site of a non-competitive antagonist in the δ subunit of the nicotinic acetylcholine receptor
    • Oberthür, W., Muhn, P., Baumann, H., Lottspeich, F., Wittmann-Liebold, B., and Hucho, F. (1986). The reaction site of a non-competitive antagonist in the δ subunit of the nicotinic acetylcholine receptor. EMBO J. 5:1815-1819.
    • (1986) EMBO J. , vol.5 , pp. 1815-1819
    • Oberthür, W.1    Muhn, P.2    Baumann, H.3    Lottspeich, F.4    Wittmann-Liebold, B.5    Hucho, F.6
  • 31
    • 0020560273 scopus 로고
    • 3H]phencyclidine binding to acetylcholine receptor rich membrane fragments from Torpedo marmorata
    • 3H]phencyclidine binding to acetylcholine receptor rich membrane fragments from Torpedo marmorata. Biochemistry 22:3128-3136.
    • (1983) Biochemistry , vol.22 , pp. 3128-3136
    • Oswald, R.E.1    Heidmann, T.2    Changeux, J.-P.3
  • 32
    • 0021185325 scopus 로고
    • Mechanism of phencyclidine binding to the acetylcholine receptor from Torpedo electroplaque
    • Oswald, R. E., Bamberger, M. J., and McLaughlin, J. T. (1984). Mechanism of phencyclidine binding to the acetylcholine receptor from Torpedo electroplaque. Mol. Pharmacol. 25:360-368.
    • (1984) Mol. Pharmacol. , vol.25 , pp. 360-368
    • Oswald, R.E.1    Bamberger, M.J.2    McLaughlin, J.T.3
  • 33
    • 0024399875 scopus 로고
    • Mechanisms of noncompetitive inhibition of acetylcholine-induced single-channel currents
    • Papke, R. L., and Oswald, R. E. (1989). Mechanisms of noncompetitive inhibition of acetylcholine-induced single-channel currents. J. Gen. Physiol. 93:785-811.
    • (1989) J. Gen. Physiol. , vol.93 , pp. 785-811
    • Papke, R.L.1    Oswald, R.E.2
  • 35
    • 0025195179 scopus 로고
    • 3H]chlorpromazine labels three amino acids of the acetylcholine receptor γ subunit: Implications for the α-helical organization of regions MII and for the structure of the ion channel
    • 3H]chlorpromazine labels three amino acids of the acetylcholine receptor γ subunit: implications for the α-helical organization of regions MII and for the structure of the ion channel. Proc. Natl. Acad. Sci. USA 87:4675-4679.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4675-4679
    • Revah, F.1    Galzi, J.L.2    Giraudat, J.3    Haumont, P.-Y.4    Lederer, F.5    Changeux, J.-P.6
  • 36
    • 0028839461 scopus 로고
    • Mutations in the M1 region of the nicotinic acetylcholine receptor alter the sensitivity to inhibition by quinacrine
    • Tamamizu, S., Todd, A. P., and McNamee, M. G. (1995). Mutations in the M1 region of the nicotinic acetylcholine receptor alter the sensitivity to inhibition by quinacrine. Cell. Mol. Neurobiol. 15:427-438.
    • (1995) Cell. Mol. Neurobiol. , vol.15 , pp. 427-438
    • Tamamizu, S.1    Todd, A.P.2    McNamee, M.G.3
  • 37
    • 0026625673 scopus 로고
    • Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist
    • White, B. H., and Cohen, J. B. (1992). Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist. J. Biol. Chem. 267:15770-15783.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15770-15783
    • White, B.H.1    Cohen, J.B.2
  • 38
    • 0025786180 scopus 로고
    • 125I]iodophenyl)diazirine is a novel noncompetitive antagonist of the nicotinic acetylcholine receptor
    • 125I]iodophenyl)diazirine is a novel noncompetitive antagonist of the nicotinic acetylcholine receptor. J. Biol. Chem. 266:21595-21607.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21595-21607
    • White, B.H.1    Howard, S.2    Cohen, S.G.3    Cohen, J.B.4
  • 39
    • 0023470651 scopus 로고
    • Equilibrium properties of mouse-Torpedo acetylcholine receptor hybrids expressed in Xenopus oocytes
    • Yoshii, K., Yu, L., Mixter Mayne, K., Davidson N., and Lester, H. A. (1987). Equilibrium properties of mouse-Torpedo acetylcholine receptor hybrids expressed in Xenopus oocytes. J. Gen. Physiol. 90:553-573.
    • (1987) J. Gen. Physiol. , vol.90 , pp. 553-573
    • Yoshii, K.1    Yu, L.2    Mixter Mayne, K.3    Davidson, N.4    Lester, H.A.5
  • 40
    • 0025829404 scopus 로고
    • Single-channel properties of mouse-Torpedo acetylcholine receptor hybrids expressed in Xenopus oocytes
    • Yu, L., Leonard, R. J., Davidson, N., and Lester, H. A. (1991). Single-channel properties of mouse-Torpedo acetylcholine receptor hybrids expressed in Xenopus oocytes. Mol. Brain Res. 10:203-211.
    • (1991) Mol. Brain Res. , vol.10 , pp. 203-211
    • Yu, L.1    Leonard, R.J.2    Davidson, N.3    Lester, H.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.