Human glutamate receptor hGluR3 flip and flop isoforms: Cloning and sequencing of the cDNAs and primary structure of the proteins

doi:10.1016/0167-4781(94)90090-6

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression

Volume 1219, Issue 2, 18 October 1994, Pages 563-566

https://doi.org/10.1016/0167-4781(94)90090-6 Get rights and content

Abstract

Several cDNA clones encoding the human glutamate receptor subunit GluR3 flip and flop isoforms, were isolated from human hippocampus and fetal brain libraries. DNA sequence analysis revealed overlapping clones permitting the reconstruction of full-length GluR3-flip and GluR3-flop cDNAs. The GluR3 cDNAs demonstrated an 94.1–94.7% nucleotide (nt) identity with the corresponding rat cDNAs. The nt sequence of the GluR3 cDNAs would encode 894 amino acid proteins that have a 99.4% identity with the rat GluR3 isoforms. The human GluR3 cDNAs predict an additional 6 amino acid in the N-terminal signal peptide as compared to the rat GluR3.

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The compositions of the glutamate AMPA-type receptors influence the neural response and the subunits GluR2/3 has been referred to as essential for receptor trafficking and synapse consolidation. We investigate the GluR2/3 occurrence and expression in the hippocampal formation of newly born homing pigeons by a semi-quantitative approach, the Western-blotting technique and by immunohistochemistry. Immunoreactivity for GluR2/3 occurs before hatching has been evident in neuropil that was fully dispersed over the hippocampus proper (HP) and the area parahippocampalis (APH). Although many HP cells are NeuN-positives, a specific neuronal protein indicating that they are already differentiated as neurons while not one contains GluR2/3 at the hatching day (P0). Few neurons at the APH seem to express GluR2/3 at P0, but 3 days later (P3) the GluR2/3 labeling can be recognized in many HP neurons, showing a distribution pattern that resembles the adult, gradually increasing in intensity until P10. Also, the Western-blot shows an augment between P0 and P3, remaining stable after that. The enhancement of the neuronal label at P3 coincides with the retraction of the GluR2/3 label in neuropil, reducing their occurrence during the maturational period to become restricted to the dorsomedial portion as reported for adults. As the HP GluR2/3-containing cells are supposedly projecting neurons, taking together, the results signalize the relevance of the GluR2/3 in post-hatch formation of avian hippocampal circuitry in which the third day seems to be the critical period.
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By using the Xenopus oocyte as an expression system, we have performed a series of experiments in order to examine the divalent cation-permeability of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptors from the human epileptic temporal lobe. Xenopus oocytes, injected with total RNA from the epileptic temporal lobe, were tested for expression of receptors by a conventional two electrode voltage-clamp technique. Administration of glutamate and AMPA gave small or no clear current responses, whereas kainate produced large inward non-desensitizing currents. The current responses evoked by kainate were concentration dependent. Experimental data gave a Hill coefficient of 1.06 and an EC₅₀ value of 87 μ The current to voltage relationship showed an inward rectification and when the concentration of divalent cations were enhanced, there was a shift in the reversal potential from −11 mV (2 mM Ca²⁺) to 12 mV (60 mM Ba²⁺). This yielded a pBa²⁺/pK⁺ permeability ratio of 1.6 when the constant field equation was used. The amplitude of the currents evoked by 600 μM kainate in solutions containing higher Ba²⁺-ion concentrations was markedly diminished (46% in 10 mM Ba²⁺- and 75% in 60 mM Ba²⁺-solution), when compared to those obtained in normal Ringer's solution, suggesting interactions between different cation species and/or screening of surface charges.
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Short sequence-paperHuman glutamate receptor hGluR3 flip and flop isoforms: Cloning and sequencing of the cDNAs and primary structure of the proteins

Abstract

FEBS Lett.

Neuron

Neuron

Cell

Neuron

Cell

Mol. Brain. Res.

Neuron

Mol. Brain. Res.

Neuron

Trends Pharmacol. Sci.

Gene

Annu. Rev. Neurosci.

Nature

Science

Science

Science

Short sequence-paper
Human glutamate receptor hGluR3 flip and flop isoforms: Cloning and sequencing of the cDNAs and primary structure of the proteins