메뉴 건너뛰기




Volumn 366, Issue 2-3, 1999, Pages 301-308

Gain of function mutation of the α7 nicotinic receptor: Distinct pharmacology of the human α7V274T variant

Author keywords

Dihydro erythroidine; Human; Mecamylamine; Methyllycaconitine; Nicotinic receptor; Oocyte, Xenopus laevis

Indexed keywords

2 METHYL 3 (2 PYRROLIDINYLMETHOXY)PYRIDINE; 3 (2,4 DIMETHOXYBENZYLIDENE)ANABASEINE; ACETYLCHOLINE; MECAMYLAMINE; METHYLLYCACONITINE; NICOTINIC AGENT; NICOTINIC RECEPTOR; NICOTINIC RECEPTOR BLOCKING AGENT;

EID: 0033030490     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(98)00909-1     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 0029979162 scopus 로고    scopus 로고
    • Pharmacology of nicotine: Addiction and therapeutics
    • Benowitz N.L. Pharmacology of nicotine: addiction and therapeutics. Annu. Rev. Pharmacol. Toxicol. 36:1996;597-613.
    • (1996) Annu. Rev. Pharmacol. Toxicol. , vol.36 , pp. 597-613
    • Benowitz, N.L.1
  • 2
    • 0029006150 scopus 로고
    • Nicotinic receptor: An allosteric protein specialized for intercellular communication
    • Bertrand D., Changeux J.-P. Nicotinic receptor: an allosteric protein specialized for intercellular communication. Sem. Neurosci. 7:1995;75-90.
    • (1995) Sem. Neurosci. , vol.7 , pp. 75-90
    • Bertrand, D.1    Changeux, J.-P.2
  • 5
    • 0031595748 scopus 로고    scopus 로고
    • Mutations at lipid-exposed residues of the acetylcholine-receptor affect its gating kinetics
    • Bouzat C., Roccamo A.M., Garbus I., Barrantes F.J. Mutations at lipid-exposed residues of the acetylcholine-receptor affect its gating kinetics. Mol. Pharmacol. 54:1998;146-153.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 146-153
    • Bouzat, C.1    Roccamo, A.M.2    Garbus, I.3    Barrantes, F.J.4
  • 6
    • 0029893705 scopus 로고    scopus 로고
    • Effect of MK-801 at the human α7 nicotinic acetylcholine receptor
    • Briggs C.A., McKenna D.G. Effect of MK-801 at the human α7 nicotinic acetylcholine receptor. Neuropharmacology. 35:1996;407-414.
    • (1996) Neuropharmacology , vol.35 , pp. 407-414
    • Briggs, C.A.1    McKenna, D.G.2
  • 7
    • 0032440954 scopus 로고    scopus 로고
    • Activation and inhibition of the human α7 nicotinic acetylcholine receptor by agonists
    • Briggs C.A., McKenna D.G. Activation and inhibition of the human α7 nicotinic acetylcholine receptor by agonists. Neuropharmacology. 37:1998;1095-1102.
    • (1998) Neuropharmacology , vol.37 , pp. 1095-1102
    • Briggs, C.A.1    McKenna, D.G.2
  • 8
    • 0028979585 scopus 로고
    • Human α7 nicotinic acetylcholine receptor responses to novel ligands
    • Briggs C.A., McKenna D.G., Piattoni-Kaplan M. Human α7 nicotinic acetylcholine receptor responses to novel ligands. Neuropharmacology. 34:1995;583-590.
    • (1995) Neuropharmacology , vol.34 , pp. 583-590
    • Briggs, C.A.1    McKenna, D.G.2    Piattoni-Kaplan, M.3
  • 9
    • 0030987817 scopus 로고    scopus 로고
    • Mutations in different functional domains of the human muscle acetylcholine receptor α-subunit in patients with the slow channel congenital myasthenic syndrome
    • Croxen R., Newland C., Beeson D., Oosterhuis H., Chauplannaz G., Vincent A., Newsom-Davis J. Mutations in different functional domains of the human muscle acetylcholine receptor α-subunit in patients with the slow channel congenital myasthenic syndrome. Hum. Mol. Genet. 6:1997;767-774.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 767-774
    • Croxen, R.1    Newland, C.2    Beeson, D.3    Oosterhuis, H.4    Chauplannaz, G.5    Vincent, A.6    Newsom-Davis, J.7
  • 10
    • 0019256904 scopus 로고
    • Types of muscarinic response in Xenopus oocytes
    • Dascal N., Landau E.M. Types of muscarinic response in Xenopus oocytes. Life Sci. 27:1980;1423-1428.
    • (1980) Life Sci. , vol.27 , pp. 1423-1428
    • Dascal, N.1    Landau, E.M.2
  • 14
    • 0030481333 scopus 로고    scopus 로고
    • Allosteric proteins after thirty years: The binding and state functions of the neuronal α7 nicotinic acetylcholine receptors
    • Edelstein S.J., Changeux J.P. Allosteric proteins after thirty years: the binding and state functions of the neuronal α7 nicotinic acetylcholine receptors. Experientia. 52:1996;1083-1090.
    • (1996) Experientia , vol.52 , pp. 1083-1090
    • Edelstein, S.J.1    Changeux, J.P.2
  • 16
    • 0031837418 scopus 로고    scopus 로고
    • Molecular basis of congenital myasthenic syndromes: Mutations in the acetylcholine receptor
    • Engel, A.G., Ohno, K., Wang, H.L., Milone, M., Sine, S.M., 1998. Molecular basis of congenital myasthenic syndromes: mutations in the acetylcholine receptor. Neuroscientist, 185-194.
    • (1998) Neuroscientist , pp. 185-194
    • Engel, A.G.1    Ohno, K.2    Wang, H.L.3    Milone, M.4    Sine, S.M.5
  • 17
    • 0029023597 scopus 로고
    • Inward rectification of neuronal nicotinic acetylcholine receptors investigated by using the homomeric α7 receptor
    • Forster I., Bertrand D. Inward rectification of neuronal nicotinic acetylcholine receptors investigated by using the homomeric α7 receptor. Proc. R. Soc. London. 260:1995;139-148.
    • (1995) Proc. R. Soc. London , vol.260 , pp. 139-148
    • Forster, I.1    Bertrand, D.2
  • 19
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • Galzi J.-L., Devillers-Thiéry A., Hussy N., Bertrand S., Changeux J.-P., Bertrand D. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature. 359:1992;500-505.
    • (1992) Nature , vol.359 , pp. 500-505
    • Galzi, J.-L.1    Devillers-Thiéry, A.2    Hussy, N.3    Bertrand, S.4    Changeux, J.-P.5    Bertrand, D.6
  • 20
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:1989;51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 22
    • 0029163027 scopus 로고
    • Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors
    • Labarca C., Nowak M.W., Zhang H.Y., Tang L.X., Deshpande P., Lester H.A. Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors. Nature. 376:1995;514-516.
    • (1995) Nature , vol.376 , pp. 514-516
    • Labarca, C.1    Nowak, M.W.2    Zhang, H.Y.3    Tang, L.X.4    Deshpande, P.5    Lester, H.A.6
  • 24
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • Lynch J.W., Rajendra S., Pierce K.D., Handford C.A., Barry P.H., Schofield P.R. Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel. EMBO J. 16:1997;110-120.
    • (1997) EMBO J. , vol.16 , pp. 110-120
    • Lynch, J.W.1    Rajendra, S.2    Pierce, K.D.3    Handford, C.A.4    Barry, P.H.5    Schofield, P.R.6
  • 26
    • 0030873046 scopus 로고    scopus 로고
    • Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing
    • Ortiz-Miranda S.I., Lasalde J.A., Pappone P.A., McNamee M.G. Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing. J. Membr. Biol. 158:1997;17-30.
    • (1997) J. Membr. Biol. , vol.158 , pp. 17-30
    • Ortiz-Miranda, S.I.1    Lasalde, J.A.2    Pappone, P.A.3    McNamee, M.G.4
  • 27
    • 0031033516 scopus 로고    scopus 로고
    • Coexpression of the neuronal α7 and L247T α7 mutant subunits yields hybrid nicotinic receptors with properties of both wild-type α7 and α7 mutant homomeric receptors
    • Palma E., Eusebi F., Miledi R. Coexpression of the neuronal α7 and L247T α7 mutant subunits yields hybrid nicotinic receptors with properties of both wild-type α7 and α7 mutant homomeric receptors. Proc. Natl. Acad. Sci. USA. 94:1997;1539-1543.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1539-1543
    • Palma, E.1    Eusebi, F.2    Miledi, R.3
  • 28
    • 0031008480 scopus 로고    scopus 로고
    • Agonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains
    • Pan Z.H., Zhang D.X., Zhang X.S., Lipton S.A. Agonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains. Proc. Natl. Acad. Sci. USA. 94:1997;6490-6495.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6490-6495
    • Pan, Z.H.1    Zhang, D.X.2    Zhang, X.S.3    Lipton, S.A.4
  • 29
    • 0030576581 scopus 로고    scopus 로고
    • An evaluation of neuronal nicotinic acetylcholine receptor activation by quaternary nitrogen compounds indicates that choline is selective for the α7 subtype
    • Papke R.L., Bencherif M., Lippiello P. An evaluation of neuronal nicotinic acetylcholine receptor activation by quaternary nitrogen compounds indicates that choline is selective for the α7 subtype. Neurosci. Lett. 213:1996;201-204.
    • (1996) Neurosci. Lett. , vol.213 , pp. 201-204
    • Papke, R.L.1    Bencherif, M.2    Lippiello, P.3
  • 30
    • 0028176058 scopus 로고
    • Human α7 acetylcholine receptor: Cloning of the α7 subunit from the SH-SY5Y cell line and determination of pharmacological properties of native receptors and function α7 homomers expressed in Xenopus oocytes
    • Peng X., Katz M., Gerzanich V., Anand R., Lindstrom J. Human α7 acetylcholine receptor: cloning of the α7 subunit from the SH-SY5Y cell line and determination of pharmacological properties of native receptors and function α7 homomers expressed in Xenopus oocytes. Mol. Pharmacol. 45:1994;546-554.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 546-554
    • Peng, X.1    Katz, M.2    Gerzanich, V.3    Anand, R.4    Lindstrom, J.5
  • 33
    • 0031876802 scopus 로고    scopus 로고
    • The nicotinic acetylcholine receptor of the Torpedo electric ray
    • Unwin N. The nicotinic acetylcholine receptor of the Torpedo electric ray. Journal of Structural Biology. 121:1998;181-190.
    • (1998) Journal of Structural Biology , vol.121 , pp. 181-190
    • Unwin, N.1
  • 34
    • 0031613616 scopus 로고    scopus 로고
    • A, and nicotinic acetylcholine receptors provide new insights into the ligand-gated ion channel receptor superfamily
    • A, and nicotinic acetylcholine receptors provide new insights into the ligand-gated ion channel receptor superfamily. Int. Rev. Neurobiol. 42:1998;285-332.
    • (1998) Int. Rev. Neurobiol. , vol.42 , pp. 285-332
    • Vafa, B.1    Schofield, P.R.2
  • 35
    • 0030906795 scopus 로고    scopus 로고
    • Mutation in the M1 domain of the acetylcholine receptor α subunit decreases the rate of agonist dissociation
    • Wang H.L., Auerbach A., Bren N., Ohno K., Engel A.G., Sine S.M. Mutation in the M1 domain of the acetylcholine receptor α subunit decreases the rate of agonist dissociation. J. Gen. Physiol. 109:1997;757-766.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 757-766
    • Wang, H.L.1    Auerbach, A.2    Bren, N.3    Ohno, K.4    Engel, A.G.5    Sine, S.M.6
  • 36
    • 0030602149 scopus 로고    scopus 로고
    • An amino acid exchange in the 2nd transmembrane segment of a neuronal nicotinic receptor causes partial epilepsy by altering its desensitization kinetics
    • Weiland S., Witzemann V., Villarroel A., Propping P., Steinlein O. An amino acid exchange in the 2nd transmembrane segment of a neuronal nicotinic receptor causes partial epilepsy by altering its desensitization kinetics. FEBS Lett. 398:1996;91-96.
    • (1996) FEBS Lett. , vol.398 , pp. 91-96
    • Weiland, S.1    Witzemann, V.2    Villarroel, A.3    Propping, P.4    Steinlein, O.5
  • 37
    • 0027194134 scopus 로고
    • Single amino acid substitution affects desensitization of the 5-hydroxytryptamine type 3 receptor expressed in Xenopus oocytes
    • Yakel J.L., Lagrutta A., Adelman J.P., North R.A. Single amino acid substitution affects desensitization of the 5-hydroxytryptamine type 3 receptor expressed in Xenopus oocytes. Proc. Natl. Acad. Sci. USA. 90:1993;5030-5033.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5030-5033
    • Yakel, J.L.1    Lagrutta, A.2    Adelman, J.P.3    North, R.A.4
  • 38
    • 0031456382 scopus 로고    scopus 로고
    • Identification of acetylcholine receptor channel lining residues in the M1 segment of the β-subunit
    • Zhang H., Karlin A. Identification of acetylcholine receptor channel lining residues in the M1 segment of the β-subunit. Biochemistry. 36:1997;15856-15864.
    • (1997) Biochemistry , vol.36 , pp. 15856-15864
    • Zhang, H.1    Karlin, A.2
  • 39
    • 0027956644 scopus 로고
    • A unique amino acid of the Drosophila GABA receptor with influence on drug sensitivity by two mechanisms
    • Zhang H.-G., Ffrench-Constant R.H., Jackson M.B. A unique amino acid of the Drosophila GABA receptor with influence on drug sensitivity by two mechanisms. J. Physiol. (London). 479:1994;65-75.
    • (1994) J. Physiol. (London) , vol.479 , pp. 65-75
    • Zhang, H.-G.1    Ffrench-Constant, R.H.2    Jackson, M.B.3
  • 40
    • 0002677769 scopus 로고
    • Long range transmission of polar effects in cholinergic 3-arylidene anabaseines. Conformations calculated by molecular modeling
    • Zoltewicz J.A., Prokai-Tatrai K., Bloom L.B., Kem W.R. Long range transmission of polar effects in cholinergic 3-arylidene anabaseines. Conformations calculated by molecular modeling. Heterocycles. 35:1993;171-179.
    • (1993) Heterocycles , vol.35 , pp. 171-179
    • Zoltewicz, J.A.1    Prokai-Tatrai, K.2    Bloom, L.B.3    Kem, W.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.