Abstract：
Alzheimer\'s disease is currently not curable. Almost all attempts to identify disease-modifying drugs failed and the causes of disease etiology are not well understood. Neurofibrillary tangles composed of pathological tau protein belong to the main hallmarks of this disease. Identification of novel physiological and pathological tau interacting proteins may lead to a better understanding of Alzheimer\'s disease pathology and tau physiology and therefore we performed a screening of the brain library by a yeast two-hybrid system intending to identify new tau interaction partners. We identified CHORDC1 (cysteine and histidine-rich domain-containing protein 1) as a novel tau interaction partner by this approach. The CHORDC1-tau interaction was validated by co-immunoprecipitation from rat brain tissues and by in vitro co-localization in the cellular model expressing full-length human tau protein. We believe that our results can be useful for researchers studying tau protein in health and disease.
摘要：
阿尔茨海默病目前无法治愈。几乎所有确定改善疾病的药物的尝试都失败了，疾病病因的原因也没有得到很好的理解。由病理性tau蛋白组成的神经原纤维缠结属于该疾病的主要标志。新的生理和病理tau相互作用蛋白的鉴定可能导致对阿尔茨海默病病理学和tau生理学的更好理解，因此我们通过酵母双杂交系统对脑库进行了筛选，旨在鉴定新的tau相互作用伙伴。我们通过这种方法将CHORDC1（富含半胱氨酸和组氨酸结构域的蛋白质1）鉴定为新型tau相互作用伴侣。通过大鼠脑组织的共免疫沉淀和在表达全长人tau蛋白的细胞模型中的体外共定位来验证CHORDC1-tau相互作用。我们相信我们的结果对于研究tau蛋白在健康和疾病中的研究人员很有用。
