Pathological and biochemical study of dementia as a combined protein accumulation disease

TDP-43、FUS和tau蛋白是多种神经退行性疾病中神经元和神经胶质包涵体的主要成分。这些蛋白质的分布与大多数疾病的临床特征有关。这些蛋白的联合蓄积常发生在许多神经退行性疾病中，包括额颞叶变性、运动神经元疾病和弥漫性神经纤维缠结伴钙化。亚甲基蓝减少了tau蛋白基因突变小鼠中tau蛋白的积累，表明其抑制tau蛋白聚集可能具有作为治疗tau蛋白病的候选药物的潜力。本研究的结果表明，发展检测生物体液中每种蛋白质的方法可能对疾病的诊断和疾病改善治疗具有重要意义。

TDP-43, FUS and tau are the major components of the neuronal and glial inclusions in a variety of neurodegenerative disorders. The distributions of these proteins were related to the clinical features in most disorders. The combined accumulation of these proteins frequently occurred in many of neurodegenerative disorders, including frontotemporal lobar degeneration, motor neuron diseases and diffuse neurofibrillary tangles with calcification. Methylene blue reduced tau accumulation in mice harboring tau gene mutation, suggesting that inhibition of tau aggregation by it may have potential as a drug candidate for the treatment of tauopathy. The results of the present study suggest developing the methods to detect each protein in biological fluids may be important for the diagnosis and the disease modifying therapy for the diseases.