Kosik K S
Harvard Medical School, Brigham and Women's Hospital, Boston, MA 02115.
Brain Pathol. 1993 Jan;3(1):39-43. doi: 10.1111/j.1750-3639.1993.tb00724.x.
Tau protein was a well-studied molecule before it was discovered in the Alzheimer neurofibrillary tangles. As a microtubule-associated protein (MAP), it continues to be of interest to microtubule biologists who have provided a rather rich knowledge about this protein. Recent work suggests that tau, a neuronal MAP, is capable of generating some features of an axonal shape and an axon-like organization of the cytoskeleton. The importance of tau in pathology stems from its relationship to Alzheimer paired helical filaments and dystrophic neurites. Tau was first believed to be a component of paired helical filaments based upon immunocytochemical grounds (1-6) and then conclusively demonstrated by protein chemical techniques (7-9). Most recently it was shown that bacterially expressed tau fragments from the microtubule-binding domain can self-assemble into paired helical filaments that resemble those from the Alzheimer brain (10).
在阿尔茨海默病神经原纤维缠结中发现tau蛋白之前,它就是一个被充分研究的分子。作为一种微管相关蛋白(MAP),它仍然是微管生物学家感兴趣的对象,这些生物学家已经提供了关于这种蛋白相当丰富的知识。最近的研究表明,神经元MAP——tau能够产生轴突形状和细胞骨架的轴突样组织的一些特征。tau在病理学中的重要性源于它与阿尔茨海默病双螺旋丝和营养不良性神经突的关系。基于免疫细胞化学依据(1 - 6),tau最初被认为是双螺旋丝的一个组成部分,随后通过蛋白质化学技术得到了确凿证明(7 - 9)。最近有研究表明,来自微管结合结构域的细菌表达的tau片段能够自组装成类似于阿尔茨海默病大脑中的双螺旋丝(10)。