HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by McLane, K. E. Articles by Conti-Tronconi, B. M. Search for Related Content PubMed PubMed Citation Articles by McLane, K. E. Articles by Conti-Tronconi, B. M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 17, 9816-9824, Jun, 1990

Identification of a brain acetylcholine receptor alpha subunit able to bind alpha-bungarotoxin

KE McLane, XD Wu and BM Conti-Tronconi
Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul 55108.

Peptides corresponding to sequence segments homologous to an alpha- bungarotoxin (alpha-BGT) binding region on the alpha subunit of the Torpedo nicotinic cholinergic receptor (nAChR) were synthesized for each identified nAChR alpha subunit of the rat nervous system (alpha 1, which is expressed in muscle, and alpha 2, alpha 3, alpha 4, and alpha 5, which are expressed by neurons). The peptides were tested for their ability to directly bind 125I-alpha-BGT and to compete for 125I-alpha- BGT with Torpedo nAChR and with the alpha-BGT-binding component expressed by PC12, a sympathetic neuronal cell line. In addition to peptides of the muscle alpha 1 subunit, peptides corresponding to the sequence of a neuronal subunit, alpha 5, were able to bind 125I-alpha- BGT. Peptides containing the sequence segments 182-201 of the alpha 1 subunit and 180-199 of the alpha 5 subunit competed with Torpedo nAChR for 125I-alpha-BGT binding with IC50 values of 0.5 and 3.5 microM, respectively. Both of these peptides were also able to compete for 125I- alpha-BGT binding with native Torpedo nAChR and with the alpha-BGT- binding protein(s) expressed on PC12 cells. To determine if other sequence segments contribute to form the neuronal alpha-BGT-binding site, overlapping peptides corresponding to the putative extracellular domain of the alpha 5 subunit were synthesized and used both in direct binding assays and in competition experiments. Peptides corresponding to amino acids 16-35 and 180-199 of the alpha 5 subunit directly bound 125I-alpha-BGT and inhibited the binding of toxin to both Torpedo nAChR and PC12 cells. The results of these studies strongly support identification of the alpha 5 subunit as a component of a neuronal alpha-BGT-binding nAChR.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. R. Mahapatra Catestatin is a novel endogenous peptide that regulates cardiac function and blood pressure Cardiovasc Res, December 1, 2008; 80(3): 330 - 338. [Abstract] [Full Text] [PDF]

				S. K. Mahata, M. Mahata, G. Wen, W. B. Wong, N. R. Mahapatra, B. A. Hamilton, and D. T. O'Connor The Catecholamine Release-Inhibitory "Catestatin" Fragment of Chromogranin A: Naturally Occurring Human Variants with Different Potencies for Multiple Chromaffin Cell Nicotinic Cholinergic Responses Mol. Pharmacol., November 1, 2004; 66(5): 1180 - 1191. [Abstract] [Full Text] [PDF]

				J. A. Stitzel, J. M. Blanchette, and A. C. Collins Sensitivity to the Seizure-Inducing Effects of Nicotine is Associated with Strain-Specific Variants of the alpha 5 and alpha 7 Nicotinic Receptor Subunit Genes J. Pharmacol. Exp. Ther., March 1, 1998; 284(3): 1104 - 1111. [Abstract] [Full Text]