PT  - JOURNAL ARTICLE
AU  - V Gerzanich
AU  - R Anand
AU  - J Lindstrom
TI  - Homomers of alpha 8 and alpha 7 subunits of nicotinic receptors exhibit similar channel but contrasting binding site properties.
DP  - 1994 Feb 01
TA  - Molecular Pharmacology
PG  - 212--220
VI  - 45
IP  - 2
4099  - http://molpharm.aspetjournals.org/content/45/2/212.short
4100  - http://molpharm.aspetjournals.org/content/45/2/212.full
SO  - Mol Pharmacol1994 Feb 01; 45
AB  - alpha 8 subunits of alpha-bungarotoxin-sensitive chick neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes from cRNA are shown to form homomeric, acetylcholine-gated, rapidly desensitizing, inwardly rectifying, Ca(2+)-permeable cation channels similar to those of alpha 7 homomers. alpha 8 forms oligomers of several sizes, of which < 14% are expressed on the oocyte surface, which is less efficient than for alpha 7 homomers. alpha 8 homomers are more sensitive to agonists but less sensitive to antagonists than are alpha 7 homomers, and some agonists for alpha 8 homomers are partial agonists or antagonists for alpha 7 homomers. The pharmacological properties of homomers of alpha 8 and alpha 7 subunits generally reflect those of native alpha 8 and alpha 7 receptors.