Abstract
A splice variant of the metabotropic glutamate receptor (mGluR) 1a, named mGluR1c, was isolated. Compared to mGluR1a, the predicted mGluR1c protein is 302 amino acids shorter at its C-terminal end. Despite this difference, mGluR1c activates phospholipase C in Xenopus oocytes with a pharmacological profile identical to that of mGluR1a. However, in contrast to the large fast transient responses induced by mGluR1a, mGluR1c receptors elicit a small more slowly generated long-lasting oscillatory current, suggesting that these two receptors do not generate the same pattern of Ca2+ release in Xenopus oocytes. In situ hybridization data show that mGluR1c mRNA is expressed at a lower level than the other splice variants of mGluR1. Some differences in the regional distribution of these transcripts were observed in the cerebellum, the olfactory bulb, and the striatum.
| Original language | English |
|---|---|
| Pages (from-to) | 10331-10335 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 89 |
| Issue number | 21 |
| DOIs | |
| Publication status | Published - 1992 |
| Externally published | Yes |
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