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  Differentiation of glycine antagonist sites of N-methyl-D-aspartate receptor subtypes

Honer, M., Benke, D., Laube, B., Kuhse, J., Heckendorn, R., Allgeier, H., et al. (1998). Differentiation of glycine antagonist sites of N-methyl-D-aspartate receptor subtypes. The Journal of Biological Chemistry, 273(18), 11158-11163. doi:10.1074/jbc.273.18.11158.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-7A21-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-7A22-7
Genre: Journal Article
Alternative Title : Differentiation of glycine antagonist sites of N-methyl-D-aspartate receptor subtypes

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JBiolChem_273_1998_11158.pdf (Any fulltext), 247KB
 
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 Creators:
Honer, Michael, Author
Benke, Dietmar, Author
Laube, Bodo, Author
Kuhse, Jochen, Author
Heckendorn, Roland, Author
Allgeier, Hans, Author
Angst, Christof, Author
Monyer, Hannah1, Author              
Seeburg, Peter H.1, Author              
Betz, Heinrich2, Author              
Mohler, Hanns, Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              

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 Abstract: The binding site for the co-agonist glycine onN-methyl-d-aspartate (NMDA) receptors has been mapped to the NR1 subunit whereas binding of the principal agonist glutamate is mediated by the NR2 subunits. Using the novel glycine site antagonist and photoaffinity label CGP 61594, distinct contributions of the NR2 subunit variants to the glycine antagonist binding domains of NMDA receptor subtypes are demonstrated. High affinity sites for CGP 61594 were exclusively displayed by NR1/2B receptors, as shown by their co-distribution with the NR2B subunit, by subunit-selective immunoprecipitation and by functional analysis of NR1/2B receptors expressed in Xenopus oocytes (inhibitory potency, IC50 = 45 ± 11 nm). Other NMDA receptor subtypes are clearly distinguished by reduced inhibitory potencies for CGP 61594, being low for NR1/2A and NR1/2D receptors (IC50 = 430 ± 105 nm and 340 ± 61 nm, respectively) and intermediate for NR1/2C receptors (IC50 = 164 ± 27 nm). Glycine antagonist sites with low and intermediate affinity for [3H]CGP 61594 were detected also in situ by radioligand binding in brain areas predominantly expressing the NR2A and NR2C subunits, respectively. Thus, [3H]CGP 61594 is the first antagonist radioligand that reliably distinguishes the glycine site of NMDA receptor subtypes. [3H]CGP 61594 is a promising tool to identify the NR2 subunit domains that contribute to differential glycine antagonist sites of NMDA receptor subtypes.

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Language(s): eng - English
 Dates: 1998-01-091998-05-01
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 273 (18) Sequence Number: - Start / End Page: 11158 - 11163 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1