麩氨酸是脊椎動物中樞神經系統主要的興奮性神經衝動傳導物質之一。離子通道型麩氨酸受器依其藥理特性可分為AMPA、 kainate和NMDA受器等三大類。已經發現神經後突觸區內某些含有PDZ domain的蛋白質與 AMPA或NMDA受器次單元的C端間會產生蛋白質與蛋白質間作用，此作用可能與麩氨酸受器在神經後突觸細胞膜上的固定、聚集有關；或藉此把其他負責細胞內訊息傳遞的蛋白質募集至神經後突觸細胞區，並與麩氨酸受器發生結合，藉以調控麩氨酸受器離子通道的活性。目前哺乳動物GluR2基因具有兩種不同C端變異型式的產物，另外吳郭魚兩個GluR2基因同源體的( tfGluR2α及tfGluR2β )亦各具有兩種不同的C端變異型式產物，因此我們目前正研究這些不同的C端變異型式是否也保留於斑馬魚的GluR2同源基因。我們以RT-PCR和DNA自動定序分析了斑馬魚zfGluR2α和zfGluR2β所具有不同C端變異型式產物種類及核甘酸序列。結果顯示zfGluR2α和zfGluR2β皆具有兩種不同變異型式的C端產物。其中zfGluR2α和zfGluR2β次單元的short form C端皆具有PDZ-binding motif ( ESVKI序列 )，然而兩者之中只有zfGluR2β次單元的short form C端具有NSF binding motif ( VAKNAQ序列 )。此外，我們也研究吳郭魚兩個NR1同源基因體是否具有不同C端變異型式產物，我們以同源篩選含有tfNR1β次單元基因組DNA，並分析tfNR1β次單元的基因結構。 tfNR1β所具有兩種不同變異型式C端都包含另一種PDZ-binding motif ( STVV序列 )。而由分析tfNR1β的基因結構中推斷tfNR1β基因不具有與大鼠NMDA受器次單元rNR1基因第二十二個exon的5’端同源性的核甘酸序列，這些序列涵蓋了譯讀rNR1a及rNR1b蛋白質停止譯碼的區域，為不具有PDZ-binding motif ( STVV序列 )的區域。這些不同的變異型式C端的機制可能與調節麩氨酸受器離子通道活性有著密切的關係，值得進一步研究分析。

Ligand-gated ionotropic glutamate receptors mediate a majority of excitatory synaptic transmission in the CNS and are involved in neuronal development, excitatoxicity, and synaptic plasticity. Previous studies have revealed that protein-protein interactions with the C-terminal domains of glutamate receptor subunits are involved in the modulation and clustering of receptor function at excitatory synapse. So far, mammalian studies have shown that the AMPA receptor subunit GluR2 has two C-terminal splicing isoforms. Tilapia ( Oreochomis
mossambicus ) expresses eight AMPA receptor subunits

( tfGluR1-4α and tfGluR1-4β). C-terminal alternative splicing isoforms of tfGluR1α, tfGluR2α and tfGluR2β were found, whereas no C-terminal isoform of tfGluR1β was found. We

surveyed that C-terminal splicing isoforms of AMPA recptor subunits ( zfGluR2α and zfGluR2β) of zebrafish ( Danio rerio ) and NMDA receptor subunits ( tfNR1αand tfNR1β) of tilapia. In this study, homologous screening, automated DNA sequencing and reverse-transcriptase PCR were employed to examine the molecular constitutions and C-terminal splicing isoforms of AMPA and NMDA receptor subunits of teleost. We found two C-terminal alternative splicing isoforms of zebrafish zfGluR2α, zfGluR2β and tilapia tfNR1β. Both zfGluR2α and zfGluR2β possess the PDZ-binding motif ( ESVKI ) in the short C-terminal form, and the short form of zfGluR2β also contains NSF-binding motif ( VAKNAQ ). All tfNR1β C-terminal alternative splicing isoforms contain PDZ-binding motif ( STVV ). Data from analysis of gene structure of the tfNR1β subunit suggests that tfNR1β lacks some nucleotides with a homology to the 5’end of exon 22 of rat rNR1 gene.

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