The mGluR1 metabotropic glutamate receptor is a G-protein-coupled receptor that exists as different C-terminal splice variants. When expressed in mammalian cells, the mGluR1 splice variants exhibit diverse transduction mechanisms and also slightly differ in their apparent agonist affinities. In the
Immunocytochemical localization of the metabotropic glutamate receptor mGluR4a in the piriform cortex of the rat
✍ Scribed by Ben�tez, Roc�o; Fern�ndez-Capetillo, Oscar; L�zaro, Esther; Mar�a Mateos, Jos�; Osorio, Alexandra; Elezgarai, Izaskun; Bilbao, Aurora; Lingenhoehl, Kurt; Van Der Putten, Herman; Hampson, David R.; Kuhn, Rainer; Kn�pfel, Thomas; Grandes, Pedro
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 1019 KB
- Volume
- 417
- Category
- Article
- ISSN
- 0021-9967
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✦ Synopsis
This study evaluates the localization of the metabotropic glutamate receptor mGluR4a in the piriform cortex of rats using preembedding immunocytochemical methods. At the light microscopic level, punctate labeling was evident in layers Ia and Ib of the piriform cortex, and immunolabeled fibers were present in layers II and III. Following bilateral destruction of the olfactory bulb, the density of labeled puncta in layer Ia decreased. These results suggest that the receptor is present on the terminals of the lateral olfactory tract (LOT). Electron microscopic evaluation of layers Ia and Ib revealed that mGluR4a was localized in synaptic terminals in layers Ia and Ib. The terminals had clear, round synaptic vesicles and terminated on asymmetric synapses on dendritic spines and shafts. There was also immunolabeling of some dendritic profiles in layers Ia and Ib that were postsynaptic to unlabeled presynaptic terminals. These observations suggest that mGluR4a is present on presynaptic terminals in the layers of the piriform cortex that receive LOT and associational synapses. This is the same area in which previous studies have revealed the presence of mGluR7 and mGluR8, suggesting that all three receptors may be colocalized.
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