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| 题名: | Effects of sarcosine and N, N-dimethylglycine on NMDA receptor-mediated excitatory field potentials |
| 作者: | Chan, Ming-Huan
詹銘煥
Chen, Hwei-Hsien
Tseng, Yufeng Jane
Lee, Mei-Yi
Lin, Yi-Ruu
Tu, Yi-Shu |
| 贡献者: | 神經科學研究所;心智、大腦與學習研究中心 |
| 关键词: | dimethylglycine;n methyl dextro aspartic acid receptor;sarcosine;agonists;analogs and derivatives;animal;drug effects;Institute for Cancer Research mouse;male;membrane potential;metabolism;mouse;Animals;Male;Membrane Potentials;Mice;Mice, Inbred ICR;Receptors, N-Methyl-D-Aspartate;Sarcosine |
| 日期: | 2017 |
| 上传时间: | 2017-07-27 12:50:57 (UTC+8) |
| 摘要: | Background: Sarcosine, a glycine transporter type 1 inhibitor and an N-methyl-D-aspartate (NMDA) receptor co-agonist at the glycine binding site, potentiates NMDA receptor function. Structurally similar to sarcosine, N,N-dimethylglycine (DMG) is also N-methyl glycine-derivative amino acid and commonly used as a dietary supplement. The present study compared the effects of sarcosine and DMG on NMDA receptor-mediated excitatory field potentials (EFPs) in mouse medial prefrontal cortex brain slices using a multi-electrode array system. Results: Glycine, sarcosine and DMG alone did not alter the NMDA receptor-mediated EFPs, but in combination with glutamate, glycine and its N-methyl derivatives significantly increased the frequency and amplitude of EFPs. The enhancing effects of glycine analogs in combination with glutamate on EFPs were remarkably reduced by the glycine binding site antagonist 7-chlorokynurenate (7-CK). However, DMG, but not sarcosine, reduced the frequency and amplitude of EFPs elicited by co-application of glutamate plus glycine. D-cycloserine, a partial agonist at the glycine binding site on NMDA receptors, affected EFPs in a similar manner to DMG. Furthermore, DMG, but not sarcosine, reduced the frequencies and amplitudes of EFPs elicited by glutamate plus D-serine, another endogenous ligand for glycine binding site. Conclusions: These findings suggest that sarcosine acts as a full agonist, yet DMG is a partial agonist at glycine binding site of NMDA receptors. The molecular docking analysis indicated that the interactions of glycine, sarcosine, and DMG to NMDA receptors are highly similar, supporting that the glycine binding site of NMDA receptors is a critical target site for sarcosine and DMG. © 2017 The Author(s). |
| 關聯: | Journal of Biomedical Science, 24(1), 論文編號 18 |
| 数据类型: | article |
| DOI 連結: | http://dx.doi.org/10.1186/s12929-016-0314-8 |
| DOI: | 10.1186/s12929-016-0314-8 |
| 显示于类别: | [神經科學研究所] 期刊論文
[心智‧大腦與學習研究中心 ] 期刊論文
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