血管生成素相互作用蛋白质的筛选与鉴定

血管生成素（angiogenin, ANG）在肿瘤、神经退行性疾病和先天免疫过程中均发挥作用，但对其具体生理病理功能和作用机制的了解并不深入全面.蛋白质 蛋白质相互作用调控着细胞内的各个生物学过程，可以为目标蛋白质功能和机制的探索提供信息.本文利用酵母双杂交技术，分别从人心肌和肝cDNA文库中筛选了ANG的可能相互作用蛋白质.对筛选获得的20个候选蛋白质进行生物信息学分析，显示10个蛋白质含有EGF结构域；有5个蛋白质在KEGG 数据库已有记录，主要参与细胞黏附、通讯和迁移等过程.在以往的研究中，我们已经验证α 辅肌动蛋白2（α-actinin 2）、卵泡抑素（follistatin）、磷脂混杂酶1（phospholipid scramblase 1）和腓骨蛋白1（fibulin1）与ANG作用的真实性.本文的蛋白质沉降实验显示，ANG与腓骨蛋白2、3、4之间也存在相互作用.

Screen and Identification of Angiogenin interacting Proteins

Angiogenin (ANG) has been reported to play important roles in tumorigenesis, neurodegenerative diseases, and innate immunity. So far, the exact physiological and pathological functions and underlying mechanisms of ANG action are unknown. The protein-protein interaction is believed to regulate almost every biological process in the cell, and presumably provide useful information for exploring the function and mechanism of a target protein. In this study, we identified 20 potential ANG-interacting proteins using yeast two hybrid technique. Structure analysis showed that 10 proteins have EGF like domains. Function annotation predicted that ANG-interacting proteins are involved in cell adhesion, communication, migration etc. Our previous works have documented the authenticity of the interaction between ANG and α-actinin 2, follistatin, phospholipid scramblase 1, or fibulin1. Here our pull down assay confirmed the interaction between ANG and fibulin2, fibulin3, or fibulin4. Altogether, our findings might provide insights into the mechanism of action of angiogenin.