Homomeric and native alpha 7 acetylcholine receptors exhibit remarkably similar but non-identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex

FEBS Lett. 1993 Jul 26;327(2):241-6. doi: 10.1016/0014-5793(93)80177-v.


Sucrose gradient analysis of chick acetylcholine receptor (AChR) alpha 7 subunits expressed in oocytes indicates that they form pharmacologically active homomers of the same size as native alpha 7 AChRs, a size compatible with a complex of five alpha 7 subunits. By immunoisolating the [35S]methionine-labeled alpha 7 subunits we also demonstrate that they do not appear to assemble with endogenous Xenopus AChR subunits. Pharmacological characterization of detergent-solubilized brain alpha 7 AChRs and alpha 7 homomers reveals that they have similar but nonidentical properties. The pharmacological difference is most accentuated for cytisine (approximately 50-fold). Thus, at least in E18 chicken brain, most or all of the native alpha 7 AChRs do not appear to be homomeric.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Binding, Competitive
  • Brain / metabolism
  • Brain Chemistry
  • Bungarotoxins / metabolism
  • Centrifugation, Density Gradient
  • Chickens
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression
  • Oocytes / metabolism
  • Receptors, Cholinergic / chemistry*
  • Receptors, Cholinergic / genetics
  • Receptors, Cholinergic / metabolism
  • Xenopus


  • Antibodies, Monoclonal
  • Bungarotoxins
  • Receptors, Cholinergic