Journal
CHANNELS
Volume 5, Issue 4, Pages 299-303Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/chan.5.4.16206
Keywords
Hb9-eGFP; mutant SOD1; motoneuron culture; patch clamp; mIPSC; gamma motoneuron; alpha motoneuron
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Funding
- [NIH-NS034100]
- [NIH-NS065895]
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A myotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease characterized by selective loss of motoneurons. Recently we studied glycine receptors (GlyRs) in motoneurons in an ALS mouse model expressing a mutant form of human superoxide dismutase-1 with a Gly93. Ala substitution (G93A-SOD1). Living motoneurons in dissociated spinal cord cultures were identified by using transgenic mice expressing eGFP driven by the Hb9 promoter. We showed that GlyR-mediated currents were reduced in large-sized (diameter >28 mu m) Hb9-eGFP(+) motoneurons from G93A-SOD1 embryonic mice. Here we analyze GlyR currents in a morphologically distinct subgroup of medium-sized (diameter 10-28 mu m) Hb9-eGFP(+) motoneurons, presumably gamma or slow-type alpha motoneurons. We find that glycine-induced current densities were not altered in medium-sized G93A-SOD1 motoneurons. No significant differences in glycinergic mIPSCs were observed between G93A-SOD1 and control medium-sized motoneurons. These results indicate that GlyR deficiency early in the disease process of ALS is specific for large alpha motoneurons.
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