Biochemical Characterization of a Novel Channel-Activating Site on Nicotinic Acetylcholine Receptors

References

• Maelicke A. Structural similarities between ion channel proteins. Trends Biochem. Sc. 1988; 13: 199–202
   PubMed Web of Science ®Google Scholar
• Galzi J.-L., Revah F., Bessis A., Changeux J.-P. Functional architecture of the nicotinic acetylcholine receptor: From electric organ tto brain. Ann. Rev. Pharmacol. 1991; 31: 37–72
   Google Scholar
• Albuquerque E. X., Daly J. W., Warnick J. E. Macromolecular sites for specific neurotoxins and drugs on chemosensitive synapses and electrical excitation in biological membranes. Ion Channels, T. Narahashi. Plenum Publishing Corporation. 1988; Vol. 1: 95–162
   Google Scholar
• Barnard E. A. Subunits of signal-transducing receptors: types, analysis and reconstitution. Receptor Subunits and Complexes, A. Burgen, E. A. Barnard. Cambridge University Press. 1992; 97–117
   Google Scholar
• Maelicke A. The nicotinic acetylcholine receptor: towards the structure-function relationship. Receptor Subunits and Complexes, A. Burgen, E. A. Barnard. Cambridge University Press. 1992; 119–162
   Google Scholar
• Bernardi H., Fosset M., Lazdunski M. Characterization, purification and affinity labelling of the brain [3H]glibenclamide binding protein, a putative neuronal ATP-regulated K+channel. Proc. Natl. Acad. Sc. USA 1988; 85: 9816–9820
   PubMed Web of Science ®Google Scholar
• Dunne M. J., Bullett M. J., Li G., Wollheim C. B., Peterson O. H. Galanin activates nucleotide-dependent K+ channels in insulin-secreting cells via a pertussis toxin sensitive G-protein. EMBO J. 1989; 8: 413–420
   PubMed Web of Science ®Google Scholar
• Huganir R. L., Miles K. Protein phosphorylation of nicotinic acetylcholine receptors. CRC Critical Rev. Biochem. Mol. Biol. 1989; 24: 183–215
   PubMed Web of Science ®Google Scholar
• Colquhoun D. On the principles of postsynaptic action of neuromuscular blocking agents. Handbook of Experimental Pharmacology, D. A. Kharkevich. Springer Verlag, Berlin-Heidelberg 1986; Vol. 79: 59–113
   Google Scholar
• Auerbach A., Sachs F. Flickering of a nicotinic ion channel to a subconductance state. Biophys. J. 1983; 42: 1–10
   PubMedGoogle Scholar
• Colquhoun D., Ogden D. C. States of the nicotinic acetylcholine receptor: enumeration, characteristics and structure. Structure and Function of the Nicotinic Acetylcholine Receptor. NATO ASI Series H: Cell Biology, A. Maelicke. Springer Press, Berlin 1986; Vol. 3: 197–218
   Google Scholar
• Steinbach J. H. Structural and functional diversity in vertebrate skeletal muscle nicotinic acetylcholine receptors. Ann. Rev. Physiol. 1989; 51: 353–365
   PubMedGoogle Scholar
• Swanson K. L., Aracava Y., Sardina F. J., Rapoport H., Aronstam R. S., Albuquerque E. X. N-methylanatoxinol isomers: Derivatives of the agonist (+)-anatoxin-a block the nicotinic acetylcholine receptor ion channel. Mol. Pharmacol. 1989; 35: 223–231
   PubMedGoogle Scholar
• Kofuji P., Aracava Y., Swanson K. L., Aronstam R. S., Rapoport H., Albuquerque E. X. Activation and blockade of the acetylcholine receptor-ion channel by the agonists (+)-anatoxina, the N-methyl derivative and the enantiomer. J. Pharmacol. Exp. Ther. 1990; 252: 517–525
   PubMedGoogle Scholar
• Shaw K. P., Aracava Y., Akaike A., Daly J. W., Rickett D. L., Albuquerque E. X. The reversible cholinesterase inhibitor physostigmine has channel-blocking and agonist effects on the acetylcholine receptor-ion channel complex. Mol. Pharmacol. 1985; 28: 527–538
   PubMed Web of Science ®Google Scholar
• Albuquerque E. X., Deshpande S. S., Kawabuchi M., Aracava Y., Idriss M., Rickett D. L., Boyne A. F. Multiple actions of anticholinesterase agents on chemosensitive synapses: Molecular basis for prophylaxis and treatment of organophosphate poisoning. Fund. Appl. Toxicol. 1985; 5: S182–S203
   Google Scholar
• Albuquerque E. X., Aracava Y., Cintra W. M., Brossi A., Schonenberger B., Deshpande S. S. Structure-activity relationship of reversible of reversible cholinesterase inhibitors: activation, channel blockade and stereospecificity of the nicotinic acetylcholine receptor-ion channel. Braz. J. Med. Biol. Res. 1988; 21: 1173–1196
   PubMed Web of Science ®Google Scholar
• Akaike A., Ikeda S. R., Brookes N., Pascuzzo G. J., Rickett D. L., Albuquerque E. X. The nature of the interactions of pyridostigmine with the nicotinic acetylcholine-receptor ion channel complex II. Patch clamp studies. Mol. Pharmacol. 1984; 25: 102–112
   PubMed Web of Science ®Google Scholar
• McHugh E. M., McGee R. Direct anesthetic-like effects of forskolin on the nicotinic acetylcholine receptors of PC12 cells. J. Biol. Chem. 1986; 261: 3103–3106
   PubMedGoogle Scholar
• Eriksson H., Salmonsson R., Liljeqvist G., Helbronn E. Studies on a cAMP-dependent protein kinase obtained from nicotinic receptorbearing microsacs. Dynamics of Cholinergic Function, I. Hamin. Plenum Press, New York 1986; 933–937
   Google Scholar
• Henderson F., Prior C., Dempster J., Marshall I. G. The effects of chloramphenicol isomers on the motor end-plate nicotinic receptor-ion channel complex. Mol. Pharmacol. 1986; 29: 52–64
   PubMedGoogle Scholar
• Deana A., Scuka M. Time course of neostigmine action on the endplate response. Neurosci. Lett. 1990; 114: 272–276
   PubMedGoogle Scholar
• Rozental R., Scoble G. T., Albuquerque E. X., Idriss M., Sherby S., Sattelle D. B., Nakanishi K., Konno K., Eldefrawi T., Eldefrawi M. W. Allosteric inhibition of nicotinic acetylcholine receptors of vertebrates and insects by philanthotoxin. J. Pharmacol. Exp. Ther. 1989; 249: 123–130
   PubMedGoogle Scholar
• Adam L. P., Henderson E. G. Calcium channel effectors are potent non-competitive blockers of acetylcholine receptors. Pflugers Arch. 1990; 416: 586–593
   PubMedGoogle Scholar
• Costa A. C. S., Swanson K. L., Aracava Y., Aronstam R. S., Albuquerque E. X. Molecular effects of dimethylanatoxin on the peripheral nicotinic acetylcholine receptor. J. Pharmacol. Exp. Ther. 1990; 252: 507–516
   PubMedGoogle Scholar
• Oswald R. E., Michel L., Bigelow J. Mechanism of binding of a benzomorphan opiate to the acetylcholine receptor from Torpedo electroplaque. Mol. Pharmacol. 1986; 29: 179–187
   PubMedGoogle Scholar
• Okonjo K. O., Kuhlmann J., Maelicke A. A second pathway of activation of the Torpedo acetylcholine receptor channel. Eur. J. Biochem. 1991; 200: 671–677
   PubMedGoogle Scholar
• Kuhlmann J., Okonjo K. O., Maelicke A. Desensitization is a property of the cholinergic binding region of the nicotinic acetylcholine receptor, not of the receptor-integral ion channel. FEBS Lett. 1991; 279(1)216–218
   PubMedGoogle Scholar
• Schrattenholz A., Godovac-Zimmermann J., Schäfer H.-J., Albuquerque E. X., Maelicke A. Photoaffinity labeling of Torpedo acetylcholine receptor by the reversible cholinesterase inhibitor physostigmine. Proc. Natl. Acad. Sci. USA 1992, in press
   Google Scholar
• Sarter M. Taking stock of cognition enhancers. Trends Pharmacol. Sci. 1991; Vol. 12: 456–461
   Google Scholar
• Thal L. J., Fuld P. A., Masur D. M., Sharpless N. S. Oral physostigmine and lecithin improve membory in Alzheimer's disease. Ann. Neurol. 1983; 13: 491–496
   PubMed Web of Science ®Google Scholar
• Duguid J. R., Raftery M. A. Fractionation and partial characterization of membrane particles from Torpedo californica electroplax. Biochemistry 1973; 12: 3593–3597
   PubMedGoogle Scholar
• Reinhardt S., Schmiady H., Tesche B., Hucho F. Functional and structural analysis of acetylcholine receptor-rich membranes after negative staining. FEBS Lett. 1984; 173: 217–221
   PubMed Web of Science ®Google Scholar
• Neubig R. R., Cohen J. B. Conformations of Torpedo acetylcholine receptor associated with ion transport and desensitization. Biochemistry 1982; 21: 3460–3467
   PubMed Web of Science ®Google Scholar
• Conti-Tronconi B. M., Tang F., Diethelm B. M., Spencer R., Reinhardt-Maelicke S., Maelicke A. Mapping of a cholinergic binding site by means of synthetic peptides, monoclonal antibodies, and α-bungarotoxin. Biochemistry 1990; 29: 6221–6230
   PubMed Web of Science ®Google Scholar
• Moore H. P., Raftery M. A. Direct spectroscopic studies of cation translocation by Torpedo acetylcholine receptor on a time scale of physiological relevance. Proc. Natl. Acad. Sci. USA 1980; 77: 4509–4513
   PubMed Web of Science ®Google Scholar
• Covarrubias M., Prinz H., Meyers H.-W., Maelicke A. Equilibrium binding of cholinergic ligands to the membrane-bound acetylcholine receptor. J. Biol. Chem. 1986; 261: 14955–14961
   PubMed Web of Science ®Google Scholar
• Gonzalez-Ros J. M., Ferragut J. A., Martinez-Carrion M. Ligand-induced effects at regions of acetylcholine receptor accessible to membrane lipids. Biochem. Biophys. Res. Commun. 1984; 120: 268–375
   Google Scholar
• Karpen J. W., Sachs A. B., Cash D. J., Pasquale E. B., Hess G. P. Direct spectrophotometric detection of cation flux in membrane vesicles: stopped-flow measurements of acetylcholine-receptor-mediated ion flux. Anal. Biochem. 1983; 135: 83–94
   PubMedGoogle Scholar
• Covarrubias M., Prinz H., Maelicke A. Ligand-specific state transitions of the membranebound acetylcholine receptor. FEBS Lett. 1984; 169: 229–233
   PubMedGoogle Scholar
• Prinz H., Maelicke A. Ligand binding to the membrane bound acetylcholine receptor from Torpedo marmorata: A complete mathematical analysis. Biochemistry 1992; 31: 6728–6738
   PubMed Web of Science ®Google Scholar
• Galzi J.-L., Revah F., Black D., Goeldner M., Hirth C., Changeux J.-P. Identification of a novel amino acid Alpha-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-binding sites. J. Biol. Chem. 1990; 265: 10430–10437
   PubMed Web of Science ®Google Scholar
• Giraudat J., Dennis M., Heidmann T., Haumont P.-Y., Lederer F., Changeux J.-P. Structure of the high-affinity binding-site for noncompetitive blockers of the acetylcholine-re-ceptor: Serine-262 of the d-subunit is labeled by [3H]-Chlorpromazine. Proc. Natl. Acad. Sci. USA 1986; 83: 2719–2723
   PubMedGoogle Scholar
• Oberthür W., Muhn P., Baumann H., Lottspeich F., Wittmann-Liebold B., Hucho F. The reaction site of a non-competitive antagonist in the 8–subunit of the nicotinic acetylcholine receptor. EMBO J. 1986; 5: 1815–1818
   PubMedGoogle Scholar
• Plümer R., Fels G., Maelicke A. Antibodies against preselected peptides to map functional sites on the acetycholine receptor. FEBS Lett. 1984; 178: 204–208
   PubMedGoogle Scholar
• Puia G., Santi M. R., Vicini S., Pritchett D. B., Purdy R. H., Paul S. M., Seeburg P., Costa E. Neurosteroids act on recombinant human GABA receptors. Neuron 1990; 4: 759–765
   PubMed Web of Science ®Google Scholar
• Wood P. L., Rao T. S., Iyengar S., Lanthor T., Monahan J., Cordi A., Sun E., Vazques M., Gray N., Contreras P. A review of the in vitro and in vivo neurochemical characterization of the NMDA/PCP/glycine/ion channel receptor macrocomplex. Neurochem. Res. 1990; 15: 217–230
   PubMed Web of Science ®Google Scholar
• Bakshi R., Faden A. I. Blockade of the glycine modulatory site of NMDA receptors modifies dynorphin-induced behavioral effects. Neurosci. Lett. 1990; 110: 113–117
   PubMedGoogle Scholar
• Marvizon J.-C., Skolnick P. An endogenous modulator of N-methyl-D-aspartate receptor-coupled glycine receptors. Eur. J. Pharmacol. 1990; 188: 23–32
   PubMedGoogle Scholar