Cole G M, Timiras P S
Department of Physiology-Anatomy, University of California at Berkeley 94720.
Neurosci Lett. 1987 Aug 18;79(1-2):207-12. doi: 10.1016/0304-3940(87)90698-7.
The ubiquitin-dependent protein degradation system plays a major role in the removal of abnormal and denatured proteins which may form insoluble aggregates in pathological conditions or during other cellular stress. Neuritic plaques and neurofibrillary tangles in sections of Alzheimer's cortex contain insoluble aggregates of proteins and are shown here to specifically immunostain with an antiserum to ubiquitin-protein conjugates. Plaque core amyloid and normal neurons do not immunostain and sodium dodecyl sulphate (SDS)-insoluble tangle preparations are not ubiquitin-positive on slot blots. The possible role and consequences of ubiquitination in tangle and plaque production in Alzheimer's disease are discussed.
泛素依赖性蛋白质降解系统在清除异常和变性蛋白质方面发挥着主要作用，这些蛋白质可能在病理条件下或其他细胞应激过程中形成不溶性聚集体。阿尔茨海默病皮质切片中的神经炎性斑块和神经原纤维缠结含有蛋白质的不溶性聚集体，此处显示它们可与抗泛素-蛋白质缀合物抗血清发生特异性免疫染色。斑块核心淀粉样蛋白和正常神经元不发生免疫染色，十二烷基硫酸钠（SDS）不溶性缠结制剂在狭缝印迹上也不是泛素阳性。本文讨论了泛素化在阿尔茨海默病缠结和斑块形成中的可能作用及后果。
