Molecular Characteristics of Membrane Glutamate Receptor-Ionophore Interaction.
Abstract
The objectives of the research project were those of defining the macromolecule or macromolecules that function as the glutamate receptor in synaptic membranes of brain neurons, of demonstrating that functional reconstitution of these sites in a membrane bilayer can be accomplished, and of studying the molecular topography of these sites in such membranes. The studies performed during the tenure of this contract have led to the isolation of a glutamate binding protein from bovine as well as rat brain synaptic membranes, and a complete biochemical characterization of both proteins. Furthermore, antibodies have been raised against these two proteins, and the antibodies against the bovine brain protein have been used in extensive immunochemical and immunocytochemical studies. The immunochemical studies have revealed a high degree of specificity of these antibodies that is associated with a selective inhibition by the antibodies of both glutamate binding to the isolated protein and glutamate-induced ion flux. Substantial progress has been made in the immunohistochemical labeling of neurons with these antibodies and in tracing the labeled sites at the light and electron microscopic level. Concurrently, a series of studies has been performed to develop the methodology for the reconstitution of a glutamate receptor-like function in liposomes and for the functional reconstitution of a partially or completely purified gultamate binding protein. Keywords: L-glutamic acid, Na fluxes, SCN(-) uptake, neuroexcitatory amino acids, antibodies, spider venom, receptor inhibitors.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 29, 1986
- Accession Number
- ADA173488
Entities
People
- Elias K. Michaelis
Organizations
- University of Kansas