Research Article
Differential patterns of expression of two novel invertebrate (Lymnaea stagnalis) ionotropic glutamate receptor genes
Article first published online: 12 MAR 2009
DOI: 10.1002/(SICI)1520-6769(199701)20:1<31::AID-NRC183>3.0.CO;2-6
Copyright © 1997 John Wiley & Sons, Ltd.
Additional Information
How to Cite
Harvey, R. J., Stühmer, T., van Minnen, J. and Darlison, M. G. (1997), Differential patterns of expression of two novel invertebrate (Lymnaea stagnalis) ionotropic glutamate receptor genes. Neurosci. Res. Comm., 20: 31–40. doi: 10.1002/(SICI)1520-6769(199701)20:1<31::AID-NRC183>3.0.CO;2-6
Publication History
- Issue published online: 12 MAR 2009
- Article first published online: 12 MAR 2009
- Manuscript Accepted: 25 OCT 1996
Funded by
- European Science Foundation
- European European Commission Biotechnology Programme 1992-1994. Grant Numbers: BIO2-CT93-0169, BIO2-CT93-0243
- Fonds der Chemischen Industrie
- Abstract
- Cited By
Keywords:
- complementary DNA cloning;
- gene family;
- glutamate-gated cation channel;
- glutamate receptor;
- in situ hybridisation;
- mollusc (Lymnaea stagnalis)
Abstract
We report the isolation of molluscan (Lymnaea stagnalis) partial complementary DNAs (cDNAs) that encode two new putative glutamate-gated cation-channel polypeptides. These proteins, which we have named Lym-eGluR4 and Lym-eGluR5, exhibit 56% identity to each other, and strong similarity (56% to 61%, and 56% to 68% identity, respectively) to the corresponding portions of vertebrate and invertebrate α-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA)-selective (or AMPA-like) glutamate receptor (GluR) subunits. Using in situ hybridisation, we have shown that the Lym-eGluR4 and Lym-eGluR5 genes are both transcribed in all 11 central ganglia of the molluscan nervous system; however, their patterns of expression are quite different. Interestingly, the Lym-eGluR5 mRNA is present in an identifiable neuron (RPeD1), within the right pedal ganglion, that has recently been shown to possess a GluR that can be readily activated by L-glutamate, quisqualic acid and kainic acid. © 1997 John Wiley & Sons, Ltd.

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