肿瘤转移是导致肿瘤患者死亡的首要因素，是当前国际医学研究重点。国际同行研究表明钠通道亚型Nav1.7在高转移前列腺癌PC3细胞上特异性高表达，并促进其转移活性，但分子机制尚不清楚。蛋白质相互作用复合物和磷酸化修饰是钠通道功能执行和调控的必要途径，阐明PC3细胞转移过程Nav1.7复合物和磷酸化修饰变化，是揭示钠通道在生理/病理过程的功能所必须的。本课题基于前期研究发现蜘蛛多肽毒素JZTX-I和HWTX-IV分别增强和减弱PC3转移活性，创新性提出利用JZTX-I与HWTX-IV作为分子探针，通过蛋白质组学技术包括BN/SDS-PAGE膜蛋白复合物分离、磷酸化修饰质谱鉴定，比较JZTX-I导致的转移增强组和HWTX-IV导致的转移减弱组Nav1.7互作蛋白和磷酸化修饰位点变化，为深入解释Nav1.7调节肿瘤转移的途径、发现新药物靶标提供依据，为探讨肿瘤相关离子通道在病理过程作用提供新思路新方法

Metastasis is the primary factors contributing to deaths in patients with cancer,and is the research focus in medical research in the present study. Voltage-gated sodium channel subtype Nav1.7 has been found to be highly expressed in the prostate canncer cell line PC3 and to modulate the metastasis of this cell line, but the mechanism underlying this process is not clarified so far. The research of sodium channel complex and phosphorylation has become a hot theme in the sodium channel related field, and some studies indicated that Nav1.7 complex and phosphorylation play important rols in its regulation of metastasis. Our previous work showed that two spider peptide toxins, JZTX-I and HWTX-IV, could inhibit the inactivation and activation of Nav1.7 and then promoted and supressed the metastasis of PC3 cells, respectively, which would provide us an novel probes for the investigation of PC3 metastasis regulated by Nav1.7. A combination of several proteomic techniques, including BN/SDS-PAGE， phosphorylation identification, will be used to identify Nav1.7-interacted proteins and phosphorylated sites in the PC3 cells treated with JZTX-I and HWTX-IV. Moreover, 2-3 proteins and phosphorylation sites will be further studied. This study might help to elucidate the mechanism of Nav1.7 regulated PC3 metastasis, to identify potential protein markers and novel mechanisms of metastasis of cancer cells, and to establish a novel stratedy for invastigating the regulation of ion channels on physiological and pathological processes.