Seitelberg F, Lassmann H
Instituto de Neurología, Universidad de Viena, Austria.
Gac Med Mex. 1990 Sep-Oct;126(5):367-73.
The reported findings suggest that ubiquitination of pathological proteinaceous intracytoplasmic inclusions is not at all specific of AD. On the contrary it appears to be a general biochemical marker for disorders in the degradation of a variety of cytoskeletal and other cytoplasmic proteins. The pattern of affected cytoskeletal components is not specific of AD/SDAT tangles. Tau definitely is present also in PSP tangles and possibly in Pick bodies but not in Lewy bodies. Furthermore, reactivity to tau, although not associated with ubiquitin but with Actin has been described in Hirano bodies. Therefore it has to be considered that the intracytoplasmic accumulation of cytoskeletal protein/ubiquitin complexes in itself is a rather unspecific cellular reaction pattern, possibly a secondary reaction to cell injury of any type especially, however, of neuronal aging. Nevertheless, the manifestation of NFT in an excessive quantity, intensity, and dynamics with severe concomitant lesions as in AD/SDAT undoubtedly is a true pathological and in this sense a disease-specific change.
报道的研究结果表明,病理性蛋白质胞质内包涵体的泛素化并非阿尔茨海默病所特有。相反,它似乎是多种细胞骨架蛋白和其他细胞质蛋白降解紊乱的一种普遍生化标志物。受影响的细胞骨架成分模式并非阿尔茨海默病/老年性痴呆缠结所特有。tau蛋白肯定也存在于进行性核上性麻痹缠结中,可能也存在于皮克小体中,但不存在于路易小体中。此外,在 Hirano 小体中也描述了对 tau 蛋白的反应性,尽管它与泛素无关,而是与肌动蛋白有关。因此,必须认识到细胞骨架蛋白/泛素复合物的胞质内积累本身是一种相当非特异性的细胞反应模式,可能是对任何类型细胞损伤的继发反应,尤其是神经元衰老。然而,与阿尔茨海默病/老年性痴呆一样,大量、高强度和动态的神经纤维缠结表现以及严重的伴随病变无疑是一种真正的病理变化,从这个意义上说,是一种疾病特异性改变。