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Residues 1 to 80 of the N-terminal domain of the ? subunit confer neuronal bungarotoxin sensitivity and agonist selectivity on neuronal nicotinic receptors

Residues 1 to 80 of the N-terminal domain of the ? subunit confer neuronal bungarotoxin sensitivity and agonist selectivity on neuronal nicotinic receptors
Residues 1 to 80 of the N-terminal domain of the ? subunit confer neuronal bungarotoxin sensitivity and agonist selectivity on neuronal nicotinic receptors
Standard two electrode voltage clamp techniques were used to investigate the response of neuronal nicotinic acetylcholine receptors, expressed in Xenopus oocytes, to various agonists and neuronal bungarotoxin (NBT). The ? subunit is an important determinant of the receptor's pharmacological profile. Co-expression of ?4 and ?2 subunits produced a receptor that was relatively insensitive to cytisine and nicotine and inhibited by NBT, whilst the ?4?4 combination produced a receptor that was highly sensitive to cytisine and nicotine but resistant to toxin. The first 80 amino acids of the N-terminal domain of the ? subunit are implicated in these characteristics, since the combination of ?4 with a hybrid ? subunit comprising amino acids 1 ? 80 of ?2 and 81 ? 416 of ?4 became relatively insensitive to nicotine and cytisine and resistant to inhibition by neuronal bungarotoxin.
nicotinic receptor, chimeric subunit, xenopus oocyte, neuronal bungarotoxin
0014-5793
139-142
Wheeler, Susan V.
ae7687e4-20ad-4d48-9263-390797c2b0e3
Chad, John E.
d220e55e-3c13-4d1d-ae9a-1cfae8ccfbe1
Foreman, Richard
c3c1ed19-ec2a-431d-bb57-e3dfb86049a4
Wheeler, Susan V.
ae7687e4-20ad-4d48-9263-390797c2b0e3
Chad, John E.
d220e55e-3c13-4d1d-ae9a-1cfae8ccfbe1
Foreman, Richard
c3c1ed19-ec2a-431d-bb57-e3dfb86049a4

Wheeler, Susan V., Chad, John E. and Foreman, Richard (1993) Residues 1 to 80 of the N-terminal domain of the ? subunit confer neuronal bungarotoxin sensitivity and agonist selectivity on neuronal nicotinic receptors. FEBS Letters, 332 (1-2), 139-142. (doi:10.1016/0014-5793(93)80500-T).

Record type: Article

Abstract

Standard two electrode voltage clamp techniques were used to investigate the response of neuronal nicotinic acetylcholine receptors, expressed in Xenopus oocytes, to various agonists and neuronal bungarotoxin (NBT). The ? subunit is an important determinant of the receptor's pharmacological profile. Co-expression of ?4 and ?2 subunits produced a receptor that was relatively insensitive to cytisine and nicotine and inhibited by NBT, whilst the ?4?4 combination produced a receptor that was highly sensitive to cytisine and nicotine but resistant to toxin. The first 80 amino acids of the N-terminal domain of the ? subunit are implicated in these characteristics, since the combination of ?4 with a hybrid ? subunit comprising amino acids 1 ? 80 of ?2 and 81 ? 416 of ?4 became relatively insensitive to nicotine and cytisine and resistant to inhibition by neuronal bungarotoxin.

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More information

Published date: 11 October 1993
Keywords: nicotinic receptor, chimeric subunit, xenopus oocyte, neuronal bungarotoxin

Identifiers

Local EPrints ID: 56763
URI: http://eprints.soton.ac.uk/id/eprint/56763
ISSN: 0014-5793
PURE UUID: 2ce6f15d-15c6-4852-9d66-d8822ef034c1
ORCID for John E. Chad: ORCID iD orcid.org/0000-0001-6442-4281

Catalogue record

Date deposited: 22 Aug 2008
Last modified: 16 Mar 2024 02:35

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Contributors

Author: Susan V. Wheeler
Author: John E. Chad ORCID iD
Author: Richard Foreman

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