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目的:研究在咪唑啉Ⅰ型受体(imidazoline-1receptor,I1R)激动剂莫索尼定和利美尼定作用下,I1R抗体选择性蛋白(imidazolinereceptorantiseraselectedprotein,IRAS)的信号转导机制。方法:采用[35S]-GTPγS结合实验,确定IRAS是否与G蛋白相偶联;采用蛋白免疫印迹方法,研究IRAS的激活与ERK磷酸化之间的关系。结果:以稳定表达有IRAS的CHO细胞(CHO-IRAS)为实验对象研究发现,利美尼定、莫索尼定在多种实验条件下均不能提高[35S]-GTPγS结合量,表明IRAS不与G蛋白偶联,而利美尼定和莫索尼定在激活IRAS的同时,能够浓度依赖性地显著升高ERK磷酸水平,其刺激作用能被I1R拮抗剂依法克生完全拮抗。结论:IRAS不与G蛋白偶联,ERK可能是IRAS偶联的信号分子之一。
OBJECTIVE: To study the signal transduction mechanism of I1R antibody selective protein (IRAS) under the action of imidazoline and limpetidine, an imidazoline-1 receptor (I1R) agonist. METHODS: [35S] -GTPγS binding assay was used to determine whether IRAS was coupled to G protein. The relationship between IRAS activation and ERK phosphorylation was studied by Western blotting. Results: Using CHO-IRAS cells stably expressing CHO-IRAS as experimental subjects, we found that lemecini and moxonidine did not increase [35S] -GTPγS binding under various experimental conditions, indicating that IRAS is not associated with G protein-coupled, while the combination of leeminizumab and moxonidine could significantly increase the level of ERK phosphorylation in a concentration-dependent manner while activating IRAS. The stimulation of IRAS could be fully antagonized by Iridium antagonist Ilex. CONCLUSION: IRAS is not coupled to G protein, and ERK may be one of the IRAS-coupled signal molecules.