Increased calbindin-D28K immunoreactivity in rat cerebellar Purkinje cell with excitatory amino acids agonists is not dependent on protein synthesis.
2004
The calcium binding protein Calbindin-D28K (CaBP) is abundantly expressed in cerebellar Purkinje cells and show increased immunoreactivity (CaBP-IR) when challenged with glutamate or an analog agonist for the ionotropic glutamate receptor (iGluR). Here we report that t-ACPD, a metabotropic glutamate receptor (mGluR) agonist, produced small increases in CaBP-IR which was potentiated by a mGluR antagonist The increase in CaBPIR was not due to de novo protein synthesis because the translational inhibitors (cycloheximide and emetine) or transciptional inhibitors (actinomycine-D and a-amanitine), did not prevent the EAA enhanced CaBP-IR. The CaBP-IR in the PC appears to be coupled to the ionotropic rather than the metabotropic glutamate receptors, but the latter become effective in the presence of their blocker, L-AP3. The results suggest that CaBP may increase its IR through a conformational change of the protein itself.
Keywords:
- Metabotropic glutamate receptor 7
- Neuroscience
- Psychology
- Metabotropic glutamate receptor 3
- Metabotropic glutamate receptor 4
- Metabotropic glutamate receptor 5
- Metabotropic glutamate receptor 6
- Metabotropic glutamate receptor
- Endocrinology
- Metabotropic glutamate receptor 8
- Internal medicine
- Metabotropic glutamate receptor 1
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