QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Whiting, P. Articles by Lindstrom, J. Search for Related Content PubMed PubMed Citation Articles by Whiting, P. Articles by Lindstrom, J.

 Previous Article  |  Next Article 

Journal of Neuroscience, Vol 6, 3061-3069, Copyright © 1986 by Society for Neuroscience

ARTICLE

Pharmacological properties of immuno-isolated neuronal nicotinic receptors

P Whiting and J Lindstrom

Recently we immunoaffinity-purified an ACh receptor from chicken brain using a monoclonal antibody raised against receptors from fish electric organ (Whiting and Lindstrom, 1986). This neuronal receptor could be affinity-labeled with 3H-bromoacetylcholine, and antisera to it specifically blocked ACh-induced depolarization of chicken ciliary ganglion cells. Here we show that this neuronal ACh receptor binds 3H- nicotine with high affinity (KD = 6.61 +/- 0.13 nM). 3H-Nicotine binding was blocked by various nicotinic cholinergic ligands but not by alpha-bungarotoxin or the muscarinic antagonist atropine. Binding was also blocked by affinity labeling the receptor with bromoacetylcholine (after reduction by dithiothreitol). Additionally, we were able to use rat antisera raised against the chicken brain receptor to isolate a component from detergent extracts of rat brain that also bound 3H- nicotine with high affinity (KD = 1.5 nM). The pharmacology of this putative ACh receptor from rat brain was almost identical to the receptor from chicken brain, and its regional distribution was in good agreement with that of 3H-nicotine binding to rodent brain membranes reported by other workers. Thus, by analogy to the receptor we have purified and characterized from chicken brain, this nicotine-binding component from rat brain is probably a functional mammalian neuronal nicotinic ACh receptor.

This article has been cited by other articles:

				K. Wang, J. T. Hackett, M. E. Cox, M. van Hoek, J. M. Lindstrom, and S. J. Parsons Regulation of the Neuronal Nicotinic Acetylcholine Receptor by Src Family Tyrosine Kinases J. Biol. Chem., March 5, 2004; 279(10): 8779 - 8786. [Abstract] [Full Text] [PDF]

				Y. Zhou, M. E. Nelson, A. Kuryatov, C. Choi, J. Cooper, and J. Lindstrom Human {alpha}4{beta}2 Acetylcholine Receptors Formed from Linked Subunits J. Neurosci., October 8, 2003; 23(27): 9004 - 9015. [Abstract] [Full Text] [PDF]

				M. Dourado and P. B. Sargent Properties of Nicotinic Receptors Underlying Renshaw Cell Excitation by alpha -Motor Neurons in Neonatal Rat Spinal Cord J Neurophysiol, June 1, 2002; 87(6): 3117 - 3125. [Abstract] [Full Text] [PDF]

				X. Peng, V. Gerzanich, R. Anand, F. Wang, and J. Lindstrom Chronic Nicotine Treatment Up-Regulates alpha 3 and alpha 7 Acetylcholine Receptor Subtypes Expressed by the Human Neuroblastoma Cell Line SH-SY5Y Mol. Pharmacol., May 1, 1997; 51(5): 776 - 784. [Abstract] [Full Text]

				C. M. Flores, R. M. DeCamp, S. Kilo, S. W. Rogers, and K. M. Hargreaves Neuronal Nicotinic Receptor Expression in Sensory Neurons of the Rat Trigeminal Ganglion: Demonstration of alpha 3beta 4, a Novel Subtype in the Mammalian Nervous System J. Neurosci., December 15, 1996; 16(24): 7892 - 7901. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help