Horiuchi M, Yamazaki N, Ikeda T, Ishiguro N, Shinagawa M
Department of Veterinary Public Health, Obihiro University of Agriculture and Veterinary Medicine, Hokkaido, Japan.
J Gen Virol. 1995 Oct;76 ( Pt 10):2583-7. doi: 10.1099/0022-1317-76-10-2583.
A cellular form of the prion protein (PrPC) is thought to be a substrate for an abnormal isoform of th eprion protein (PrPSc) in scrapie. PrPC is abundant in tissues of the central nervous system, but little is known about the distribution of PrPC in non-neuronal tissues of sheep, the natural host of scrapie. This study investigated the tissue distribution of PrPC in sheep. Although PrPC was abundant in neuronal tissues, it was detected in non-neuronal tissues such as spleen, lymph node, lung, heart, kidney, skeletal muscle, uterus, adrenal gland, parotid gland, intestine, proventriculus, abomasum and mammary gland. Neither PrPC nor PrP mRNA was detected in the liver. The tissue distribution of PrPC appears to be inconsistent with the tissues which possess scrapie infectivity, suggesting that factor(s) specific to certain cell types may be required to support multiplication of the scrapie agent.
在羊瘙痒病中，细胞形式的朊病毒蛋白（PrPC）被认为是异常朊病毒蛋白异构体（PrPSc）的底物。PrPC在中枢神经系统组织中含量丰富，但对于羊瘙痒病的天然宿主绵羊的非神经组织中PrPC的分布情况却知之甚少。本研究调查了PrPC在绵羊体内的组织分布。尽管PrPC在神经组织中含量丰富，但在脾脏、淋巴结、肺、心脏、肾脏、骨骼肌、子宫、肾上腺、腮腺、肠道、前胃、皱胃和乳腺等非神经组织中也检测到了它。在肝脏中未检测到PrPC和PrP mRNA。PrPC的组织分布似乎与具有瘙痒病感染性的组织不一致，这表明可能需要特定细胞类型的特定因子来支持瘙痒病病原体的增殖。
