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Characterization of a presynaptic glutamate receptor
T Smirnova1, J Stinnakre, J Mallet
1Laboratoire de génétique moléculaire de la neurotransmission et des processus neurodégénératifs, Centre National de la Recherche Scientifique (CNRS), Gif sur Yvette, France.
Science (New York, N.Y.)
|October 15, 1993
Summary
This study identifies a presynaptic protein, GR33 (syntaxin), as a functional glutamate receptor. Expressed in oocytes, GR33 forms glutamate-activated ion channels, suggesting a role in neurotransmission.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Glutamate receptors are crucial for excitatory neurotransmission, memory formation, and neurodegenerative diseases.
- A novel 33-kilodalton protein (GR33) was identified using antibodies against glutamate binding proteins.
Purpose of the Study:
- To characterize the function of the GR33 protein.
- To determine if GR33 acts as a glutamate receptor.
Main Methods:
- Complementary DNA library screening using specific antibodies.
- Expression of GR33 in Xenopus oocytes.
- Pharmacological and electrophysiological characterization of ion channels.
Main Results:
- GR33 sequence is identical to the presynaptic protein syntaxin.
- Expressed GR33 forms glutamate-activated ion channels in oocytes.
- These channels exhibit pharmacological similarities to N-methyl-D-aspartate receptors but distinct electrophysiological properties.
- Mutation of leucine 278 in GR33 alters channel properties.
Conclusions:
- GR33 functions as a glutamate-activated ion channel.
- GR33 may act as a presynaptic glutamate receptor in vivo.
- The findings provide new insights into the molecular mechanisms of glutamatergic neurotransmission.