Irie Y, Yamagata K, Gan Y, Miyamoto K, Do E, Kuo C H, Taira E, Miki N
Department of Pharmacology, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
J Biol Chem. 2000 Jan 28;275(4):2647-53. doi: 10.1074/jbc.275.4.2647.
Amida was isolated by the yeast two-hybrid system as a novel protein which associated with Arc, a non-transcriptional immediate early gene specific to the brain. Amida was confirmed to be associated with Arc in vitro and in vivo. Amida shows no homology to known proteins. Amida is ubiquitously expressed, although it is abundant in the brain. A transfection study revealed that Amida was localized in the nucleus and after 72 h the transfected cells underwent apoptosis. Furthermore, we found two nuclear localization signals and a domain needed for interacting with Arc was encompassed by two nuclear localization signals. Co-transfection experiment with Amida and Arc suggested that Amida transported Arc into the nucleus and negatively regulated Amida-induced cell death. These results indicate that Arc together with Amida may modulate cell death in the brain.
通过酵母双杂交系统分离出了阿米达（Amida），它是一种与Arc相关的新型蛋白质，Arc是一种大脑特异性的非转录即时早期基因。已证实在体外和体内阿米达均与Arc相关。阿米达与已知蛋白质无同源性。尽管在大脑中含量丰富，但阿米达在全身广泛表达。一项转染研究表明，阿米达定位于细胞核，转染72小时后转染细胞发生凋亡。此外，我们发现了两个核定位信号，与Arc相互作用所需的结构域被两个核定位信号所包围。阿米达与Arc的共转染实验表明，阿米达将Arc转运到细胞核中，并对阿米达诱导的细胞死亡起负调控作用。这些结果表明，Arc与阿米达一起可能调节大脑中的细胞死亡。
