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The amino terminal half of the nicotinic beta-subunit extracellular domain regulates the kinetics of inhibition by neuronal bungarotoxin.
- Source :
-
Proceedings. Biological sciences [Proc Biol Sci] 1993 May 22; Vol. 252 (1334), pp. 141-8. - Publication Year :
- 1993
-
Abstract
- Subtypes of nicotinic receptors previously reported to be unaffected by neuronal bungarotoxin (NBT), including alpha 3 beta 4-containing and muscle type (alpha 1 beta 1 gamma delta) receptors, are shown to be inhibited by this toxin, but with rapid kinetics of onset and recovery. This inhibition is in contrast to the slow and prolonged inhibition of alpha 3 beta 2-containing receptors, suggesting that the beta subunits determine the kinetics of NBT inhibition of alpha 3 receptors. We have coexpressed chimeric beta subunits with alpha 3, and our results show that the first 121 amino acids of the beta subunit extracellular domain are sufficient to regulate the kinetics of NBT inhibition. This domain is also an important determinant of whether cytisine will act as a full agonist or a partial agonist of nicotinic receptors formed with alpha 3.
- Subjects :
- Acetylcholine pharmacology
Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
Female
Kinetics
Macromolecular Substances
Molecular Sequence Data
Nicotinic Antagonists
Oligodeoxyribonucleotides
Oligonucleotides, Antisense
Oocytes drug effects
Receptors, Nicotinic biosynthesis
Recombinant Fusion Proteins antagonists & inhibitors
Recombinant Fusion Proteins biosynthesis
Recombinant Fusion Proteins metabolism
Bungarotoxins pharmacology
Neurons physiology
Oocytes physiology
Receptors, Nicotinic physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0962-8452
- Volume :
- 252
- Issue :
- 1334
- Database :
- MEDLINE
- Journal :
- Proceedings. Biological sciences
- Publication Type :
- Academic Journal
- Accession number :
- 8391703
- Full Text :
- https://doi.org/10.1098/rspb.1993.0058