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Immunohistochemistry analysis of Paraformaldehyde-fixed mouse brain section.
Strong immunoreactivity in the cerebellar molecular layer (cbm) and hippocampal formation (HF) characteristic of GluR1 distribution.
Western blot analysis of mouse cerebellar membrane protein with anti-GluR1 antibody .
Lane 1-5: Mouse cerebellar membrane protein (10 µg).
Western blot and IHC images provided courtesy of Dr. Christopher L. Thompson, Durham University.
Khatib, T., Whiting, A., Chisholm, D., Redfern, C., Müller, B. and McCaffery, P. (2019). A Bioluminescence Reporter Assay for Retinoic Acid Control of Translation of the GluR1 Subunit of the AMPA Glutamate Receptor. Mol Neurobiol. PMID: 30972628
Spaethling, J., Le, L. and Meaney, D. (2012). NMDA receptor mediated phosphorylation of GluR1 subunits contributes to the appearance of calcium-permeable AMPA receptors after mechanical stretch injury. Neurobiol Dis, 46(3), 646-654. PMID: 22426393
The α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) is an ionotropic transmembrane receptor for glutamate found throughout the central nervous system (CNS). AMPARs are composed of four types of subunits: GluR1/GluA1, GluR2/GluA2, GluR3/GluA3, and GluA4 (GluRA-D2), which combine to form heterotetramers. The function of AMPARs is determined by the composition of AMPAR subunits and GluR1 is found in the dorsal horn region of the spinal cord. GluR1-containing AMPARs are permeable to Ca2+ and the presence of GluR1-containing AMPARs in synapses contributes to the formation of long-term potential. GluR1 is involved in synaptic plasticity and the expression of the GluR1 gene is reduced with age.
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