Effects of different anti‐tau antibodies on tau fibrillogenesis: RTA‐1 and RTA‐2 counteract tau aggregation
Effects of different anti‐tau antibodies on tau fibrillogenesis: RTA‐1 and RTA‐2 counteract tau aggregation
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DOI：
10.1016/j.febslet.2005.01.039
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发表时间：
2005-02
期刊：
影响因子：
3.5
通讯作者：
T. Taniguchi;M. Sumida;Shuko Hiraoka;K. Tomoo;T. Kakehi;K. Minoura;S. Sugiyama;K. Inaka;T. Ishida;N. Saito;C. Tanaka
中科院分区：
文献类型：
--
作者：
T. Taniguchi;M. Sumida;Shuko Hiraoka;K. Tomoo;T. Kakehi;K. Minoura;S. Sugiyama;K. Inaka;T. Ishida;N. Saito;C. Tanaka
Tau是tau蛋白病（包括阿尔茨海默病）中神经病理学的主要抗原组分。虽然可溶性tau转化为不溶性聚合纤维状形式是tau蛋白病发病机制中的关键因素，但这种变化的机制尚不清楚，也没有可用的纤维形成抑制剂。针对微管结合结构域的第1或第2重复的单克隆抗体，但不是C-末端16个残基，完全抑制tau聚集成PHF。此外，它们不抑制tau诱导的微管蛋白组装。因此，它们可用于研究tau蛋白转化，并且将是有用的治疗先导材料。
Tau is the major antigenic component of neurofibrillary pathology in tauopathy, including Alzheimer’s disease. Although conversion of soluble tau to an insoluble polymerized fibrillar form is a key factor in the pathogenesis of tauopathy, the mechanism of the change is unclear and no inhibitors of fibril formation are available. Monoclonal antibodies against the 1st or 2nd repeat of the microtubule binding domain, but not the C-terminal 16 residues, completely inhibited tau aggregation into PHF. Furthermore, they did not inhibit tau-induced tubulin assembly. Thus, they are useful to investigate tau protein conversion and will be useful therapeutic lead materials.