The excitatory, ionotropic glutamatergic AMPA receptor is the most common membrane-bound receptor in the central nervous system. AMPARs and the NMDA receptors are central to synaptic plasticity, memory, and mechanisms of neurodegeneration. The AMPAR is an obligate heterotetramer, composed of subunits GluA1-4. Subunit permutation determines ion conductance, trafficking and other functional characteristics. Few available antibodies are subunit-specific, disabling researchers from accurately visualizing differential AMPAR subunit distribution in the nervous system. This study sought to visualize a novel monoclonal GluA1/2/3 antibody with functional avidity for three of four receptor subunits and to characterize the ultrastructural localization of these receptors using confocal and electron microscopy.
| Identifer | oai:union.ndltd.org:CLAREMONT/oai:scholarship.claremont.edu:pitzer_theses-1085 |
| Date | 01 January 2014 |
| Creators | Aguiar, Sebastian |
| Publisher | Scholarship @ Claremont |
| Source Sets | Claremont Colleges |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Pitzer Senior Theses |
| Rights | © 2014 Sebastian Aguiar, http://creativecommons.org/licenses/by/4.0/ |
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