著者

Yasuhisa Ano Akikazu Sakudo Ryuta Uraki Juri Kono Masayoshi Yukawa Takashi Onodera

出版者

内閣府食品安全委員会

雑誌

Food Safety (ISSN:21878404)

巻号頁・発行日

vol.1, no.1, pp.2013005-2013005, 2013 (Released:2013-11-20)

参考文献数

51

被引用文献数

3

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Infectious prion diseases include Kuru and its variant, Creutzfeldt-Jakob disease, in humans, scrapie in sheep, and bovine spongiform encephalopathy in cattle. In these diseases, the pathogenic prion protein (PrPSc) enters the host through the gastrointestinal tract and migrates to the central nervous system, where PrPSc induces characteristic pathological changes. The mechanisms underlying this intercellular transfer are not fully understood. After oral administration, PrPSc withstands the digestive process and may be incorporated by microfold cells (M cells) or villous columnar epithelial cells in the intestine. Based on Western Blot with specific markers, liquid chromatography, and morphological analysis, the cellular prion protein (PrPC) and PrPSc in the cells are associated with exosomes, membranous vesicles that are secreted upon fusion of multivesicular endosomes with the plasma membranes. Exosomes may play a role in PrP transportation through intestinal epithelium. Cells may exploit the nature of endosome-derived exosomes to communicate with each other in normal and pathological situations, providing for a novel route of cell-to-cell communication and therefore of pathogen transmission in the intestinal epithelium. In addition, since most bovine spongiform encephalopathy cases were exposed to the agent in the first six months of life, developmental alteration of the intestinal defense and immune system may also be involved in the susceptibility to infection.