Cloning, expression and modulation of a mouse NMDA receptor subunit

FEBS Letters

Araki, Kazuaki²  Mishina, Masayoshi²  Yamazaki, Makoto²  Mori, Hisashi²  Mori, Kazuhiro J.¹ 

[1] Department of Biology, Faculty of Science, Niigata University, Niigata 951 Japan;Department of Neuropharmacology, Brain Research Institute Niigata University, Niigata 951 Japan

关键词: Glutamate receptor;    Glycine;    N-methyl-d-aspartate receptor channel;    Mg2+ block;    12-O-Tetradecanoylphorbol 13-acetate;    AMPA;    α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid;    APV;    d-2-amino-5-phosphonovalerate;    GluR;    glutamate receptor;    nAChR;    nicotinic acetylcholine;    receptor NMDA;    N-methyl-d-aspartate;    TPA;    12-O-tetradecanoylphorbol 13-acetate;   

DOI  :  10.1016/0014-5793(92)80160-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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).

【 授权许可】

Unknown