Identification of Purine Binding Sites on Torpedo Acetylcholine Receptor

References

• Dowdall M. J., Boyne A. F., Whittaker V. P. Adenosine triphosphate, a constituent of cholinergic synaptic vesicles. Biochem. J. 1974; 140: 1–12
   PubMedGoogle Scholar
• Burnstock G. The co‐transmitter hypothesis, with special reference to the storage and release of ATP with noradrenaline and acetylcholine. Co‐transmission, A. C. Cuello, 1982; 151–164
   Google Scholar
• Pintor J., Kowalewski H. J., Torres M., Miras‐Portugal M. Z., Zimmermann H. Synaptic vesicle storage of diadenosine polyphosphates in the Torpedo electric organ. Neurosci. Res. Comm. 1991; 10: 9–16
   Google Scholar
• Correia da Sà P., Sebastiao A. M., Ribeiro J. A. Inhibitory and exitatory effects of adenosine receptor agonists on evoked transmitter release from phrenic nerve endings of the rat. Br. J. Pharmacol. 1991; 103: 1614–1620
   PubMedGoogle Scholar
• Okada Y., Sakurai T., Mori M. Exitatory effect of adenosine on neurotransmission is due to an increase of transmitter release in the hippocampal slices. Neurosci. Lett. 1992; 142: 233–236
   PubMedGoogle Scholar
• Kolb H. A., Wankelam M. J.O. Transmitter‐like action of ATP on patched membranes of cultured myoblasts and myotubes. Nature 1982; 303: 621–623
   Google Scholar
• Igusa Y. Adenosine 5′‐triphosphate activates acetylcholine receptor channels in cultured Xenopus myotomal muscle cells. J. Physiol. (London) 1988; 405: 169–185
   Google Scholar
• Reis R. A. M., Rozental R., Albuquerque E. X. Extracellular ATP modulates the function of the peripheral nicotinic receptor. Soc. Neurosci. Abstr. 1990; 16: 205
   Google Scholar
• Mozrzymas J. W., Ruzzier F. ATP activates junctional and extrajunctional acetylcholine receptor channels in isolated adult rat muscle fibres. Neurosc. Lett. 1992; 139: 217–220
   PubMedGoogle Scholar
• Evans R. J., Derkach V., Surprenant A. ATP mediates fast synaptic transmission in mammalian neurons. Nature 1992; 357: 503–505
   PubMed Web of Science ®Google Scholar
• Eterovic V. A., Li L., Palma A., McNamee M. G. Regulation of nicotinic acetylcholine receptor function by adenine nucleotides. Cell. Mol. Neurobiol. 1990; 10: 423–433
   PubMedGoogle Scholar
• Lu Z., Smith D. O. Adenosine 5′‐triphosphat increases acetylcholine channel opening frequency in rat skeletal muscle. J. Physiol. (London) 1991; 436: 45–56
   Google Scholar
• Fu W., Poo M. ATP potentiates spontaneous transmitter release at developing neuromuscular synapses. Neuron 1991; 6: 837–843
   PubMedGoogle Scholar
• Bean B. P. Pharmacology and electrophysiology of ATP‐activated ion channels. Trends Pharmacol. Sci. 1992; 13: 87–90
   PubMed Web of Science ®Google Scholar
• Maelicke A., Coban T., Schrattenholz A., Schröder B., Reinhardt‐Maelicke S., Storch A., Godovac‐Zimmermann J., Methfessel C., Pereira E. F. R., Albuquerque E. Physostigmine and neuromuscular transmission. Myasthenia gravis and related disorders: experimental and clinical aspects, A. S. Penn, D. P. Richman, R. L. Ruff, V. A. Lennon. Ann. New York Acad. Sci. 1993; 681: 140–156
   Google Scholar
• Schrattenholz A., Coban T., Schröder B., Okonjo K. O., Kuhlmann J., Pereira E. F., Albuquerque E. X., Maelicke A. Biochemical characterization of a novel channel‐activating site on nicotinic acetylcholine receptors. J. Receptor Res. 1993; 13: 393–412
   PubMed Web of Science ®Google Scholar
• Pereira E. F. R., Alkondon M., Tano T., Castro N. G., Froes‐Ferrao M. M., Rozental R., Aronstam R. S., Schrattenholz A., Maelicke A., Albuquerque E. X. A novel agonist binding site on nicotinic acetylcholine receptors. J. Rec. Res. 1993; 13: 413–436
   PubMed Web of Science ®Google Scholar
• Pereira E. F. R., Reinhardt‐Maelicke S., Schrattenholz A., Maelicke A., Albuquerque E. X. Identification and functional characterization of a new agonist site on nicotinic acetylcholine receptors of cultured hippocampal neurons. J. Pharmacol. Experim. Therap. 1993; 265: 1474–1491
   PubMed Web of Science ®Google Scholar
• Schrattenholz A., Godovac‐Zimmermann J., Schäfer H. ‐J., Albuquerque E. X., Maelicke A. Photoaffinity labeling of Torpedo acetylcholine receptor by physostigmine. Eur. J. Biochem. 1993; 216: 671–677
   PubMedGoogle Scholar
• Sloothaak J. B., Berden J. A., Herweijer M. A., Kemp A. The use of 8‐azido‐ATP and 8‐azido‐ADP as photoaffinity labels of the ATP synthase in submitochondrial particles: evidence for a mechanism of ATP hydrolysis involving two independent catalytic sites? Biochim. Biophys. Acta 1985; 809: 27–38
   PubMedGoogle Scholar
• Schäfer H. ‐J., Scheurich P., Dose K. Eine einfache Darstellung von 8‐Azidoadenosin‐5′‐triphosphat; ein Agens zur Photoaffinitätsmarkierung von ATP‐bindenden Proteinen. Liebigs Ann. Chem. 1978; 1978: 1749–1753
   Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Laskey A., Mills A. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur. J. Biochem. 1975; 56: 335–341
   PubMedGoogle Scholar
• Oberthuer W., Muhn P., Baumann H., Lottspeich F., Wittmann‐Liebold B., Hucho F. The reaction site of a non‐competetive antagonist in the δ‐subunit of the nicotinic acetylcholine receptor. EMBO J. 1986; 5: 1815–1819
   PubMedGoogle Scholar
• Giraudat J., Dennis M., Heidmann T., Haumont P. T., Lederer F., Changeux J. P. Structure of the high‐affinity binding site for noncompetitive blockers of the acetylcholine receptor: 3H chlorpromazine labels homologous residues in the β‐ and δ‐chains. Biochemistry 1987; 26: 2410–2418
   PubMed Web of Science ®Google Scholar
• Revah F., Galzi J. ‐L., Giraudat J., Haumont P. ‐Y., Lederer F., Changeux J. P. The non‐competetive blocker 3H chlorpromazine labels three amino acids of the acetylcholine receptor γ‐subunit: implications for the α‐helical organization of regions M II and for the structure of the ion channel. Proc. Natl. Acad. Sci. USA 1990; 87: 4675–4679
   PubMed Web of Science ®Google Scholar
• Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Furutani Y., Hirose T., Takashima H., Inayama S., Miyata T., Numa S. Structural Homology of Torpedo californica Acetylcholine Receptor Subunits. Nature 1983; 302: 528–532
   PubMed Web of Science ®Google Scholar
• Carlson B. J., Raftery M. A. Specific binding of ATP to extracellular sites on Torpedo acetylcholine receptor. Biochemistry 1993; 32: 7329–7333
   PubMedGoogle Scholar