RNA Editing of the Glutamate Receptor Subunits GluR2 and GluR6 in Human Brain Tissue

  title={RNA Editing of the Glutamate Receptor Subunits GluR2 and GluR6 in Human Brain Tissue},
  author={W. C. Paschen and John C. Hedreen and Christopher A. Ross},
  journal={Journal of Neurochemistry},
Abstract: Editing of mRNA in the coding region of the second transmembrane domain of glutamate receptor subunits GluR2, GluR5, and GluR6 involves a change of the base A in genomic DNA to the base G in mRNA as described in rat brain. To determine whether this reaction occurs in humans as well as rats, we studied RNA editing of GluR2 and GluR6 in human brain. We compared the extent of editing in controls and cases with Huntington's disease. To assay the extent of editing in brain RNA, first… 
RNA Editing at the Q/R Site for the Glutamate Receptor Subunits GLUR2, GLUR5, and GLUR6 in Hippocampus and Temporal Cortex from Epileptic Patients
It is found that the editing efficiency for the kainate receptor subunits GluR5 and GLUR6 was significantly higher in temporal cortex than in normal controls, which may reflect an adaptive reaction of ongoing seizure activity to prevent excessive Ca(2+) influx.
Low editing efficiency of GluR2 mRNA is associated with a low relative abundance of ADAR2 mRNA in white matter of normal human brain
The results suggest that Q/R site of GluRs editing is regulated in a regional, and hence presumably cell‐specific, manner and that the GluR2 Q/ R site editing is critically regulated by ADAR2 in human brain.
Editing of glutamate receptor subunit B pre-mRNA in vitro by site-specific deamination of adenosine
It is shown that the GluR-B pre-mRNA is efficiently and accurately edited in vitro, and that base-pair interactions between the editing site and a sequence in the downstream intron8 are required for substrate recognition.
Structural Requirements for RNA Editing in Glutamate Receptor Pre-mRNAs by Recombinant Double-stranded RNA Adenosine Deaminase (*)
It is shown here that DRADA indeed edits GluR pre-mRNAs, but that it displays selectivity for certain editing sites, and that this substrate selectivity correlated with the base pairing status and sequence environment of the editing-targeted adenosines.
Editing of the GLuR‐B ion channel RNA in vitro by recombinant double‐stranded RNA adenosine deaminase.
It is demonstrated in vitro that DRADA is indeed involved in editing of the GLuR‐B RNA and the Q/R site‐selective editing by DRADA requires a cofactor protein(s) commonly present even in non‐neuronal cells.
Underediting of glutamate receptor GluR-B mRNA in malignant gliomas
It is reported that in tissues from malignant human brain tumors, this editing position of glutamate receptor subunit B is substantially underedited compared with control tissues, suggesting a role for RNA editing in tumor progression and providing a molecular model explaining the occurrence of epileptic seizures in association with malignant gliomas.


Human GluR6 kainate receptor (GRIK2): molecular cloning, expression, polymorphism, and chromosomal assignment.
A cDNA clone for the human GluR6 kainate-preferring glutamate receptors shows a very high sequence similarity with that of the rat, except for a part of the 3' untranslated region in which there is a TAA triplet repeat.
Molecular cloning and chromosomal localization of one of the human glutamate receptor genes.
The extreme conservation between the human and rat kainate receptor subunits suggests that a similar gene family will encode human kainates receptors, and the GluHI mRNA is widely expressed in human brain.
Molecular cloning and functional expression of glutamate receptor subunit genes.
Three closely related genes, GluR1, GluR2, and GluR3, encode receptor subunits for the excitatory neurotransmitter glutamate. The proteins encoded by the individual genes form homomeric ion channels
Differential expression of three glutamate receptor genes in developing rat brain: an in situ hybridization study.
The finding of differential developmental regulation of the GluR-1, -2, and -3 genes indicates that the receptors they encode may have different influences on synaptic plasticity, neuronal survival, and susceptibility to excitatory amino acid toxicity.
Structural determinants of ion flow through recombinant glutamate receptor channels
The properties of heteromeric wild-type and mutant GluRs revealed that the dominance of GluR-B is due to the arginine residue in the TM2 region, and the steady-state current-voltage relations of glutamate- and kainate-induced currents through homomeric channels fell into two classes.
Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA
The cloning and expression of a functional rat glutamate receptor subunit cDNA, GluR6, which has a very different pharmacology from that of the GluLl–GluR4 class and exhibits an outwardly rectifying current–voltage relationship.