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Volume 17, Number 21, Issue of November 1, 1997 pp. 8201-8212
Copyright ©1997 Society for Neuroscience

Neuronal -Bungarotoxin Receptors Differ Structurally from Other Nicotinic Acetylcholine Receptors

Received May 30, 1997; revised Aug. 13, 1997; accepted Aug. 21, 1997.

Fatima Rangwala, Renaldo C. Drisdel, Sergey Rakhilin, Elizabeth Ko, Pramod Atluri, Amy B. Harkins, Aaron P. Fox, and Suleiman B. Salman, and William N. Green

Department of Pharmacological and Physiological Sciences, University of Chicago, Chicago, IL 60637

We have characterized the -bungarotoxin receptors (BgtRs) found on the cell surface of undifferentiated pheochromocytoma (PC12) cells. The PC12 cells express a homogeneous population of 7-containing receptors that bind -Bgt with high affinity (K_d = 94 pM). The BgtRs mediate most of the response elicited by nicotine, because the BgtR-specific antagonists methyllycaconitine and -Bgt block ~90% of the whole-cell current. The binding of nicotinic agonists to cell-surface BgtRs was highly cooperative with four different agonists showing Hill coefficients in the range of 2.3-2.4. A similar agonist binding cooperativity was observed for BgtR homomers formed from chimeric 7/5HT3 subunits expressed in tsA 201 cells. Two classes of agonist binding sites, in the ratio of 4:1 for PC12 cell BgtRs and 3:1 for 7/5HT3 BgtRs, were revealed by bromoacetylcholine alkylation of the reduced sites on both PC12 BgtRs and 7/5HT3 BgtRs. We conclude from this data that PC12 BgtRs and 7/5HT3 homomers contain at least three distinguishable agonist binding sites and thus are different from other nicotinic receptors.

Key words: nicotine; -bungarotoxin; pheochromocytoma; nicotinic receptors; electrophysiology; pharmacology

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