The sensitivity of AMPA-selective glutamate receptor channels to pentobarbital is determined by a single amino acid residue of the alpha 2 subunit
| Autor: | Kenji Sakimura, Masayoshi Mishina, Tomohiro Yamakura, Koki Shimoji |
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| Rok vydání: | 1995 |
| Předmět: |
Pentobarbital
Arginine Protein subunit Glutamine Molecular Sequence Data Biophysics AMPA receptor Biochemistry Gamma-aminobutyric acid receptor subunit alpha-1 Ion Channels AMPA-selective glutamate receptor channel Structure-Activity Relationship Structural Biology Genetics medicine Homomeric Amino Acid Sequence Receptors AMPA Molecular Biology Site-directed mutagenesis Chemistry Anesthetic Electric Conductivity Cell Biology α2 Subunit Transmembrane domain Mutagenesis Site-Directed NMDA receptor medicine.drug |
| Zdroj: | FEBS letters. 374(3) |
| ISSN: | 0014-5793 |
| Popis: | Clinical concentrations of pentobarbital inhibit the alpha-amino-3-hydroxy-5- methyl-4-isoxazole propionic acid (AMPA)-selective glutamate receptor (GluR) channels. Recently, the AMPA-selective GluR channels that contained the alpha 2 subunit were shown to be more sensitive to pentobarbital block than those without the alpha 2 subunit. Here we demonstrated that replacement by glutamine of the arginine residue in putative transmembrane segment M2 of the alpha 2 subunit (mutation alpha 2-R586Q) drastically reduced the pentobarbital sensitivity of the alpha 2 heteromeric channel to the level comparable to those of the alpha 1 and alpha 2-R586Q homomeric channels. These results suggest that the arginine residue in segment M2 of the alpha 2 subunit is the critical determinant of the sensitivities of the AMPA-selective GluR channels to pentobarbital. |
| Databáze: | OpenAIRE |
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