Homomeric and native α7 acetylcholine receptors exhibit remarkably similar but non‐identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex

FEBS Letters

Anand, René¹  Peng, Xiao¹  Lindstrom, Jon¹ 

[1] Department of Neuroscience, University of Pennsylvania, Philadelphia, PA 19104-607, USA

关键词: Acetylcholine receptor;    α-Bungarotoxin;    Pharmacology;    Xenopus oocyte;    Homomeric receptor;    α7 subunit;    αBgt;    α-bungarotoxin;    ACh;    acetylcholine;    AChR;    acetylcholine receptor;    Carb;    carbamylcholine;    Deca;    decamethonium;    EDTA;    [ethylenedinitrilo]tetraacetic acid;    EGTA;    [ethyl-ene-bis(oxyethylenenitrilo)]tetraacetic acid;    Hex;    hexamethonium;    mAb;    monoclonal antibody;    PBS;    phosphate-buffered saline;    RIA;    radioimmunoassay;    TEA;    tetraethylammonium;    TMA;    tetramethylammonium;   

DOI  :  10.1016/0014-5793(93)80177-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sucrose gradient analysis of chick acetylcholine receptor (AChR) α7 subunits expressed in oocytes indicates that they form pharmacologically active homomers of the same size as native α7 AChRs, a size compatible with a complex of five α7 subunits. By immunoisolating the [³⁵S]methionine-labeled α7 subunits we also demonstrate that they do not appear to assemble with endogenous Xenopus AChR subunits. Pharmacological characterization of detergent-solubilized brain α7 AChRs and α7 homomers reveals that they have similar but nonidentical properties. The pharmacological difference is most accentuated for cytisine (~50-fold). Thus, at least in E18 chicken brain, most or all of the native α7 AChRs do not appear to be homomeric.

【 授权许可】

Unknown