Hope J, Shearman M S, Baxter H C, Chong A, Kelly S M, Price N C
BBSRC & MRC Neuropathogenesis Unit, BBSRC Institute for Animal Health, Edinburgh.
Neurodegeneration. 1996 Mar;5(1):1-11. doi: 10.1006/neur.1996.0001.
The abnormal form of the prion protein (PrPSc), a synthetic prion protein peptide fragment (PrP106-126) and fragments of the Alzheimer's protein precursor, APP, have been shown to be cytotoxic in vitro. We have used synchronous, clonal cell models originally developed to study the toxicity of the Alzheimer's disease amyloid peptide, A beta 25-35, to investigate the actions of PrP peptides. We found that the cytotoxicity of the PrP106-126 depends on its state of aggregation and the cellular expression of PrPc, and is independent of a loss of MTT reduction activity in the absence of cell death associated with the cellular effects of A beta 25-35. These factors may play a role in the lesion specificity of different pathological phenotypes of prion-protein related diseases.
朊病毒蛋白（PrPSc）的异常形式、一种合成的朊病毒蛋白肽片段（PrP106 - 126）以及阿尔茨海默病蛋白前体APP的片段，已被证明在体外具有细胞毒性。我们使用了最初为研究阿尔茨海默病淀粉样肽Aβ25 - 35的毒性而开发的同步克隆细胞模型，来研究PrP肽的作用。我们发现PrP106 - 126的细胞毒性取决于其聚集状态和PrPc的细胞表达，并且在没有与Aβ25 - 35的细胞效应相关的细胞死亡情况下，与MTT还原活性的丧失无关。这些因素可能在朊病毒蛋白相关疾病不同病理表型的病变特异性中起作用。
