Neuronal nicotinic α-bungarotoxin receptors

  • M. Quik
  • R. Afar
  • T. Audhya
  • G. Goldstein
  • J.-M. Trifaró
Part of the Journal of Neural Transmission book series (NEURAL SUPPL, volume 29)


Recent evidence has indicated that the nicotinic acetylcholine receptor and the nicotinic α-bungarotoxin (α-BGT) site may be distinct in neuronal tissues. With regard to function, the former receptor appears to be involved in mediating synaptic events; however, the role of the nicotinic α-BGT site in nervous tissue is currently not known. Since the binding of α-BGT exhibits such high affinity and selectivity for a specific receptor, this may implicate an involvement of the toxin binding site in some aspect of neuronal activity with the receptor possibly mediating functions other than nicotinic cholinergic transmission. A further hypothesis to explain the nature of the toxin binding site may be that the natural ligand for the α-BGT site is one other than acetylcholine, with acetylcholine acting as a modulator of the site. Current studies in our laboratory are exploring these possibilities by determining whether specific peptides and/or polypeptides can interact at the nicotinic α-BGT site in nervous tissue. Studies using both in vivo and in vitro approaches suggest that thy-mopoietin may serve a role as a modulator of the nicotinic α-BGT site in neuronal tissues.


Chromaffin Cell Nicotinic Receptor Nicotinic Acetylcholine Receptor Neuronal Tissue Adrenal Chromaffin Cell 
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Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • M. Quik
    • 1
    • 4
  • R. Afar
    • 1
  • T. Audhya
    • 2
  • G. Goldstein
    • 2
  • J.-M. Trifaró
    • 3
  1. 1.Department of PharmacologyMcGill UniversityMontrealCanada
  2. 2.Immunobiology Research InstituteAnnandaleUSA
  3. 3.Secretory Process Research Program, Department of PharmacologyUniversity of OttawaOttawaCanada
  4. 4.Department of PharmacologyMcGill UniversityMontrealCanada

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