2026-03-15T17:56:37Z https://niigata-u.repo.nii.ac.jp/oai

oai:niigata-u.repo.nii.ac.jp:00014657 2022-12-15T03:46:37Z 453:456 471:537:538:1070

The Lurcher Mutation Reveals Ca^2+ Permeability and PKC Modification of the GluRδ Channels Lurcher型変異を用いたグルタミン酸受容体 δサブユニットのチャネル特性解析 Lurcher型変異を用いたグルタミン酸受容体 δサブユニットのチャネル特性解析 池野, 観寿 94611 Lurcher PKC グルタミン酸受容体δサブユニット Ca ^2＋透過性 The physiological function of the GluRδ subfamily which is one of the glutamate receptor channel subunits has not yet been clarified, because no GluR channel activity was detected in heterologous expression systems. The Lurcher mutation, a point mutation of the GluRδ 2 subunit, converts it into a functional channel. We introduced this mutation into GluRδ, AMPA-and NMDA-type GluR channel subunits, and characterized their channel properties. It was shown that the Lurcher mutation exerts effects only on the AMPA-and NMDA-type channel gating, but not on their ionic channel permeabilities. These findings support the idea that the Lurcher mutant GluRδ 1 and GluRδ 2 channels are permeable to Ca^2+, reflecting their original channel properties. It was also found that the ionic permeability of the mutant GluRδ 1 channels was modulated by TPA. departmental bulletin paper 新潟医学会 2001-10 application/pdf 新潟医学会雑誌 10 115 506 517 新潟医学会雑誌 AN00182415 00290440 https://niigata-u.repo.nii.ac.jp/record/14657/files/115(10)_506-517.pdf http://hdl.handle.net/10191/48426 https://niigata-u.repo.nii.ac.jp/records/14657 jpn