PUBLICATION
A novel glycine receptor alphaZ1 subunit variant in the zebrafish brain
- Authors
- Devignot, V., Prado de Carvalho, L., Bregestovski, P., and Goblet, C.
- ID
- ZDB-PUB-031119-9
- Date
- 2003
- Source
- Neuroscience 122(2): 449-457 (Journal)
- Registered Authors
- Bregestovski, Piotz, Devignot, Véronique, Goblet, Christiane
- Keywords
- alternative splicing; heterologous expression; ionic currents; zinc modulation; developmental profile; hybridization in situ
- MeSH Terms
-
- Alternative Splicing
- Amino Acid Sequence
- Animals
- Base Sequence
- Brain/drug effects
- Brain/embryology
- Brain/metabolism*
- Cell Line
- Dose-Response Relationship, Drug
- Glycine/metabolism*
- Glycine/pharmacology
- Humans
- Membrane Potentials/drug effects
- Membrane Potentials/physiology
- Molecular Sequence Data
- Nerve Tissue Proteins/biosynthesis
- Nerve Tissue Proteins/chemistry*
- Nerve Tissue Proteins/genetics*
- Nerve Tissue Proteins/physiology
- Organ Specificity/genetics
- Protein Subunits/biosynthesis
- Protein Subunits/chemistry
- Protein Subunits/genetics
- Protein Subunits/physiology
- Receptors, Glycine/biosynthesis
- Receptors, Glycine/chemistry*
- Receptors, Glycine/genetics*
- Receptors, Glycine/physiology
- Transfection
- Zebrafish Proteins/biosynthesis
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/genetics*
- Zebrafish Proteins/physiology
- PubMed
- 14614909 Full text @ Neuroscience
Citation
Devignot, V., Prado de Carvalho, L., Bregestovski, P., and Goblet, C. (2003) A novel glycine receptor alphaZ1 subunit variant in the zebrafish brain. Neuroscience. 122(2):449-457.
Abstract
alpha subunits of the inhibitory glycine receptor (GlyR) display genetic heterogeneity in mammals and zebrafish. This diversity is increased in mammals by the alternative splicing mechanism. We report here in zebrafish, the characterization of a new alphaZ1 subunit likely arising from alphaZ1 gene by an alternative splice process (alphaZ1L). This novel cDNA possesses 45 supplementary nucleotides at the putative exon2/exon3 boundary. The corresponding protein contains 15 additional amino acids in the NH2-terminal domain. Heterologous expression of homomeric GlyRalphaZ1L in human embryonic kidney-293 cells generates glycine-gated strychnine-sensitive chloride channels with no obvious discrepancy with pharmacological properties of GlyRalphaZ1. Moreover, zinc modulation of glycine-induced currents is identical in alphaZ1 and alphaZ1L glycine receptors. During ontogenesis, simultaneous alphaZ1 and alphaZ1L mRNA synthesis have been observed. Embryonic and adult alphaZ1 and alphaZ1L mRNA expressions are restricted to the CNS. Embryonic alphaZ1L mRNA anatomical pattern of expression is, however, highly restrained and strictly limited to the rostral part of the brain revealing a highly regionalized function of alphaZ1L in the CNS. This report contributes to the characterization of the diversity of glycine receptor isoforms in zebrafish and emphasizes the common mechanism used among vertebrates for creating GlyR variety and specificity.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping