1995年11月6日
The sensitivity of AMPA-selective glutamate receptor channels to pentobarbital is determined by a single amino acid residue of the α2 subunit
FEBS Letters
- ,
- ,
- ,
- 巻
- 374
- 号
- 3
- 開始ページ
- 412
- 終了ページ
- 414
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1016/0014-5793(95)01163-9
Clinical concentrations of pentobarbital inhibit the α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective glutamate receptor (GluR) channels. Recently, the AMPA-selective GluR channels that contained the α2 subunit were shown to be more sensitive to pentobarbital block than those without the α2 subunit. Here we demonstrated that replacement by glutamine of the arginine residue in putative transmembrane segment M2 of the α2 subunit (mutation α2-R586Q) drastically reduced the pentobarbital sensitivity of the α2 heteromeric channel to the level comparable to those of the α1 and α2-R586Q homomeric channels. These results suggest that the arginine residue in segment M2 of the α2 subunit is the critical determinant of the sensitivities of the AMPA-selective GluR channels to pentobarbital. © 1995.
- リンク情報
- ID情報
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- DOI : 10.1016/0014-5793(95)01163-9
- ISSN : 0014-5793
- CiNii Articles ID : 80008631052
- PubMed ID : 7589582
- SCOPUS ID : 0028858375