Cloning, expression and modulation of a mouse NMDA receptor subunit.
The primary structure and presence of two forms of the mouse N-methyl-D-aspartate (NMDA) receptor channel subunit zeta 1 have been disclosed by cloning and sequencing the cDNAs. The zeta 1 subunit shows approximately 20% amino acid sequence identities with the rodent alpha-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 zeta 1 channels expressed in Xenopus oocytes by injection of the subunit-specific mRNA exhibit current responses characteristic 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 zeta 1 channel activity is positively modulated by treatment with 12-O-tetradecanoylphorbol 13-acetate (TPA).
Yamazaki
M
M
Department of Neuropharmacology, Niigata University, Japan.
Mori
H
H
Araki
K
K
Mori
K J
KJ
Mishina
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D005786:Gene Expression Regulation; D051379:Mice; D008969:Molecular Sequence Data; D016194:Receptors, N-Methyl-D-Aspartate / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014982:Xenopus laevis / Q000235:genetics
D016194:Receptors, N-Methyl-D-Aspartate; D004247:DNA; D013755:Tetradecanoylphorbol Acetate