The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Identification and functional expression of a novel ligand binding subunit of the inhibitory glycine receptor.
Open accessAbstract
By homology screening of a rat brain cDNA library we have identified a novel alpha subunit variant of the inhibitory glycine receptor, alpha 3. The deduced protein exhibits 82-83% amino acid identity to the previously characterized rat and human alpha 1 and alpha 2 subunit sequences. Upon heterologous expression in Xenopus laevis oocytes, the alpha 3 subunit formed functional agonist-gated chloride channels which displayed a low affinity for glycine and only small responses to taurine. Amplification of alpha 3 transcripts by polymerase chain reaction revealed high levels in spinal cord at later postnatal stages of development. These data indicate alpha subunit heterogeneity of the inhibitory glycine receptor in adult rats that may result in pharmacologically distinct receptor subtypes.
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Cites
Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA Polymerase
Saiki, R. K., Gelfand, D. H., Stoffel, S., Scharf, S. J., Higuchi, R., Horn, G. T., Mullis, K. B., & Erlich, H. A. (1988) · Science · doi:10.1126/science.2448875 · Cited by 17,719
Cited by
Molecular Structure and Physiological Function of Chloride Channels
Jentsch, T. J., Stein, V., Weinreich, F., & Zdebik, A. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00029.2001 · Cited by 1,256
The 93-kDa glycine receptor-associated protein binds to tubulin.
Kirsch, J., Langosch, D., Prior, P., Littauer, U. Z., Schmitt, B., & Betz, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54560-9 · Cited by 273
Self-citationMilestone Review: Unlocking the Proteomics of Glycine Receptor Complexes
Fraser, S. D., Klaassen, R. V., Villmann, C., Smit, A. B., & Harvey, R. J. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70061 · Cited by 10
“The GlyR α1-α4 subunits exhibit a high degree of sequence identity ( ≥ 80%; Grenningloh, Schmieden, et al. 1990; Kuhse et al. 1990; Matzenbach et al. 1994) which hampered the design of subunit-specific antibodies for many years.”
Metadata
- Authors
- Kuhse, J., Schmieden, V, & Betz, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-12
- Volume
- 265
- Issue
- 36
- Pages
- 22317-22320
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1599587228
- Cited by
- 191
- References
- 1
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kuhse, J., Schmieden, V, & Betz, H. (1990). Identification and functional expression of a novel ligand binding subunit of the inhibitory glycine receptor. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)45707-9
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
