Karoline Pichlerová, Jakub Šinský, Matej Kotásek, Petra Majerová, Jozef Hanes
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引用次数: 0
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.
阿尔茨海默病目前无法治愈。几乎所有试图寻找改变疾病的药物的努力都失败了,而且人们对疾病的病因也不甚了解。由病理性 tau 蛋白组成的神经纤维缠结是这种疾病的主要特征。因此,我们通过酵母双杂交系统对大脑文库进行了筛选,以确定新的 tau 相互作用伙伴。通过这种方法,我们发现 CHORDC1(富含半胱氨酸和组氨酸结构域的蛋白 1)是一种新型 tau 相互作用伙伴。大鼠脑组织中的共免疫沉淀和表达全长人类 tau 蛋白的细胞模型中的体外共定位验证了 CHORDC1 与 tau 的相互作用。我们相信,我们的研究结果对研究健康和疾病中的 tau 蛋白的研究人员很有帮助。
期刊介绍:
General Physiology and Biophysics is devoted to the publication of original research papers concerned with general physiology, biophysics and biochemistry at the cellular and molecular level and is published quarterly by the Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences.