Kretzschmar H A, Prusiner S B, Stowring L E, DeArmond S J
Am J Pathol. 1986 Jan;122(1):1-5.
Scrapie is a slow degenerative encephalopathy of animals caused by unusual infectious particles termed prions. A cDNA encoding the only apparent component of the prion, a protein designated PrP 27-30, has recently been cloned and sequenced. By measuring mRNA levels using in situ hybridization with the PrP cDNA, the authors found that prion proteins are synthesized almost exclusively within neurons. The levels of PrP mRNA varied among different types of neurons, but did not change during scrapie infection. A cDNA encoding glial fibrillary acidic protein (GFAP) was a positive control; GFAP mRNA was confined to astrocytes. Our finding of PrP mRNA in neurons may explain the degeneration and vacuolation that occurs in these cells during scrapie infection.
羊瘙痒症是一种由被称为朊病毒的异常感染性颗粒引起的动物缓慢退化性脑病。最近已克隆并测序了编码朊病毒唯一明显成分(一种名为PrP 27 - 30的蛋白质)的cDNA。通过使用PrP cDNA进行原位杂交来测量mRNA水平,作者发现朊病毒蛋白几乎仅在神经元内合成。PrP mRNA的水平在不同类型的神经元中有所不同,但在羊瘙痒症感染期间并未改变。编码胶质纤维酸性蛋白(GFAP)的cDNA是阳性对照;GFAP mRNA局限于星形胶质细胞。我们在神经元中发现PrP mRNA可能解释了在羊瘙痒症感染期间这些细胞中发生的退化和空泡化现象。