Abstract
Glutamate receptors mediate excitatory neurotransmission in the brain and are important in the formation of memory and in some neurodegenerative disorders. A complementary DNA clone that encoded a 33-kilodalton protein (GR33) was obtained by screening a library with an antibody generated against glutamate binding proteins. The sequence of GR33 is identical to that of the recently reported presynaptic protein syntaxin. When GR33 was expressed in Xenopus oocytes, it formed glutamate-activated ion channels that are pharmacologically similar to those of N-methyl-D-aspartate receptors but with different electrophysiological properties. Mutation of the leucine 278 residue in the single putative transmembrane segment of GR33 affects the properties of the channel. Thus, in vivo GR33 may be a presynaptic glutamate receptor.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Antigens, Surface / chemistry
-
Brain / embryology
-
Brain Chemistry
-
Calcium / metabolism
-
Cells, Cultured
-
Cloning, Molecular
-
Glutamates / pharmacology
-
Glutamic Acid
-
Humans
-
Membrane Potentials
-
Mutagenesis, Site-Directed
-
N-Methylaspartate / pharmacology
-
Nerve Tissue Proteins / chemistry
-
Neurons / chemistry
-
Oocytes
-
Rats
-
Rats, Wistar
-
Receptors, Glutamate / chemistry
-
Receptors, Glutamate / genetics
-
Receptors, Glutamate / metabolism*
-
Receptors, N-Methyl-D-Aspartate / metabolism
-
Receptors, Presynaptic / chemistry
-
Receptors, Presynaptic / genetics
-
Receptors, Presynaptic / metabolism*
-
Syntaxin 1
-
Xenopus
Substances
-
Antigens, Surface
-
Glutamates
-
Nerve Tissue Proteins
-
Receptors, Glutamate
-
Receptors, N-Methyl-D-Aspartate
-
Receptors, Presynaptic
-
Syntaxin 1
-
Glutamic Acid
-
N-Methylaspartate
-
Calcium