Methyllycaconitine and (+)‐anatoxin‐a differentiate between nicotinic receptors in vertebrate and invertebrate nervous systems

FEBS Letters

Rapoport, Henry²  Lunt, George G.¹  Swanson, Karen L.³  Wonnacott, Susan¹  Albuquerque, Edson X.³  Macallan, David R.E.¹ 

[1] Department of Biochemistry, University of Bath, Bath BA2 7AY, England;Department of Chemistry, University of California, Berkeley, CA 94720 USA;Department of Pharmacology and Experimental Therapeutics, University of Maryland, School of Medicine, Baltimore, MD 21201, USA

关键词: α-Bungarotoxin;    Nicotine;    Methyllycaconitine;    Anatoxin-a;    Nicotinic receptor;    (Rat brain;    Locust ganglion);    nAChR;    nicotinic acetylcholine receptor;    MLA;    methyllycaconitine;   

DOI  :  10.1016/0014-5793(88)81454-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Specific high-affinity binding sites for ¹²⁵I-α-bungarotoxin and (−)-[³H]nicotine have been measured in rat brain and locust (Schistocerca gregaria) ganglia. The binding sites for ¹²⁵I-α-bungarotoxin had similar K _d values of 1.5 × 10⁻⁹ and 0.8 × 10⁻⁹ M for rat and locust preparations, respectively; the corresponding values for the (−)-[³H]nicotine-binding site were 9.3 × 10⁻⁹ and 1.7 × 10⁻⁷ M. Methyllycaconitine (MLA) potently inhibited ¹²⁵I-α-bungarotoxin binding in both rat and locust. MLA was a less effective inhibitor of (−)-[³H]nicotine binding whereas (+)-anatoxin-a was a very potent inhibitor at this site in the rat but not in the locust. These data suggest that (+)-anatoxin-a is a useful probe for the high-affinity nicotine-binding receptor in vertebrate brain, whereas MLA is a preferential probe for the subclass of receptor that binds α-bungarotoxin.

【 授权许可】

Unknown