Layfield R, Fergusson J, Aitken A, Lowe J, Landon M, Mayer R J
Department of Biochemistry, University of Nottingham Medical School, Queen's Medical Centre, UK.
Neurosci Lett. 1996 May 3;209(1):57-60. doi: 10.1016/0304-3940(96)12598-2.
The localisation of 14-3-3 proteins compared to that of tau and ubiquitin-protein conjugates in sections of hippocampus from Alzheimer's disease (AD) brains was examined by immunohistochemistry. In all cases (n = 10), anti-14-3-3 stained a proportion of neurofibrillary tangles (NFT). In general, NFT stained by anti-14-3-3 were smaller than those stained by anti-tau or anti-ubiquitin-protein conjugates and were more confined to the neuronal cell body. Occasionally, cortical Lewy bodies in cases of Lewy body dementia were also found to be 14-3-3-positive. Since 14-3-3 proteins are central to MAP kinase signalling, the results support the proposal that this pathway is in part responsible for the hyperphosphorylation of tau, which leads to the formation of the paired helical filaments seen in AD brains.
通过免疫组织化学方法，研究了阿尔茨海默病（AD）患者大脑海马体切片中14-3-3蛋白与tau蛋白和泛素-蛋白缀合物的定位情况。在所有病例（n = 10）中，抗14-3-3抗体均能使一部分神经原纤维缠结（NFT）染色。一般来说，被抗14-3-3抗体染色的NFT比被抗tau抗体或抗泛素-蛋白缀合物染色的NFT小，且更局限于神经元细胞体。偶尔，路易体痴呆病例中的皮质路易体也被发现呈14-3-3阳性。由于14-3-3蛋白是丝裂原活化蛋白激酶信号传导的核心，这些结果支持了这样一种观点，即该信号通路部分地导致了tau蛋白的过度磷酸化，进而导致AD大脑中出现双螺旋丝。
