Cloning, expression and modulation of a mouse NMDA receptor subunit

Makoto Yamazaki; Hisashi Mori; Kazuaki Araki; Kazuhiro J. Mori; Masayoshi Mishina

doi:10.1016/0014-5793(92)80160-I

Cloning, expression and modulation of a mouse NMDA receptor subunit

Makoto Yamazaki, Hisashi Mori, Kazuaki Araki, Kazuhiro J. Mori, Masayoshi Mishina^*

^*Corresponding author for this work

Molecular Neuroscience

Research output: Contribution to journal › Article › peer-review

287 Scopus citations

Abstract

The primary structure and presence of two forms of the mouse N-methyl-d-aspartate (NMDA) receptor channel subunit ζl have been disclosed by cloning and sequencing the cDNAs. The ζl subunit shows -20% amino acid sequence identities with the rodent α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)- or kainate-selective GluR subunits and has structural features common to neurotransmitter-gated ion channels. Functional homomeric ζl channels expressed in Xenopus oocytes by injection of the subunit specific mRNA exhibit current responses characteristics for the NMDA receptor channel such as activation by glycine, Ca²⁺ permeability, blocking by Mg²⁺ and activation by polyamine. It has been found that the ζl channel activity is positively modulated by treatment with 12-O-tetradecanoylphorbol 13-acetate (TPA).

Original language	English
Pages (from-to)	39-45
Number of pages	7
Journal	FEBS Letters
Volume	300
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(92)80160-I
State	Published - 1992/03/23

Keywords

12-O-Tetradecanoylphorbol 13-acetate
Glutamate receptor
Glycine
Mg block
N-methyl-d-aspartate receptor channel

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(92)80160-I

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title = "Cloning, expression and modulation of a mouse NMDA receptor subunit",

abstract = "The primary structure and presence of two forms of the mouse N-methyl-d-aspartate (NMDA) receptor channel subunit ζl have been disclosed by cloning and sequencing the cDNAs. The ζl subunit shows -20% amino acid sequence identities with the rodent α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)- or kainate-selective GluR subunits and has structural features common to neurotransmitter-gated ion channels. Functional homomeric ζl channels expressed in Xenopus oocytes by injection of the subunit specific mRNA exhibit current responses characteristics for the NMDA receptor channel such as activation by glycine, Ca2+ permeability, blocking by Mg2+ and activation by polyamine. It has been found that the ζl channel activity is positively modulated by treatment with 12-O-tetradecanoylphorbol 13-acetate (TPA).",

keywords = "12-O-Tetradecanoylphorbol 13-acetate, Glutamate receptor, Glycine, Mg block, N-methyl-d-aspartate receptor channel",

author = "Makoto Yamazaki and Hisashi Mori and Kazuaki Araki and Mori, {Kazuhiro J.} and Masayoshi Mishina",

year = "1992",

month = mar,

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doi = "10.1016/0014-5793(92)80160-I",

language = "英語",

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T1 - Cloning, expression and modulation of a mouse NMDA receptor subunit

AU - Yamazaki, Makoto

AU - Mori, Hisashi

AU - Araki, Kazuaki

AU - Mori, Kazuhiro J.

AU - Mishina, Masayoshi

PY - 1992/3/23

Y1 - 1992/3/23

N2 - The primary structure and presence of two forms of the mouse N-methyl-d-aspartate (NMDA) receptor channel subunit ζl have been disclosed by cloning and sequencing the cDNAs. The ζl subunit shows -20% amino acid sequence identities with the rodent α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)- or kainate-selective GluR subunits and has structural features common to neurotransmitter-gated ion channels. Functional homomeric ζl channels expressed in Xenopus oocytes by injection of the subunit specific mRNA exhibit current responses characteristics for the NMDA receptor channel such as activation by glycine, Ca2+ permeability, blocking by Mg2+ and activation by polyamine. It has been found that the ζl channel activity is positively modulated by treatment with 12-O-tetradecanoylphorbol 13-acetate (TPA).

AB - The primary structure and presence of two forms of the mouse N-methyl-d-aspartate (NMDA) receptor channel subunit ζl have been disclosed by cloning and sequencing the cDNAs. The ζl subunit shows -20% amino acid sequence identities with the rodent α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)- or kainate-selective GluR subunits and has structural features common to neurotransmitter-gated ion channels. Functional homomeric ζl channels expressed in Xenopus oocytes by injection of the subunit specific mRNA exhibit current responses characteristics for the NMDA receptor channel such as activation by glycine, Ca2+ permeability, blocking by Mg2+ and activation by polyamine. It has been found that the ζl channel activity is positively modulated by treatment with 12-O-tetradecanoylphorbol 13-acetate (TPA).

KW - 12-O-Tetradecanoylphorbol 13-acetate

KW - Glutamate receptor

KW - Glycine

KW - Mg block

KW - N-methyl-d-aspartate receptor channel

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DO - 10.1016/0014-5793(92)80160-I

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AN - SCOPUS:0026560041

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VL - 300

SP - 39

EP - 45

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Cloning, expression and modulation of a mouse NMDA receptor subunit

Abstract

Keywords

ASJC Scopus subject areas

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