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Mycosporine-like amino acids (MAAs) 처리에 따른 배양세포 내 스크래피 프리온 단백질의 형성증가Enhanced formation of scrapie prion protein in cultured ceils by treatment with mycosporine-like amino acids (MAAs)

Other Titles
Enhanced formation of scrapie prion protein in cultured ceils by treatment with mycosporine-like amino acids (MAAs)
Authors
Lee, J.Moh, S.-H.Ryou, C.Kim, D.-H.
Issue Date
Jun-2015
Publisher
Korean Society for Microbiolog and Biotechnology
Keywords
Mycosporine-like amino acids; Prion; Protein aggregation; PrP
Citation
Korean Journal of Microbiology and Biotechnology, v.43, no.2, pp 91 - 96
Pages
6
Indexed
SCOPUS
KCI
Journal Title
Korean Journal of Microbiology and Biotechnology
Volume
43
Number
2
Start Page
91
End Page
96
URI
https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/20585
DOI
10.4014/mbl.1503.03002
ISSN
1598-642X
Abstract
Prions are proteinaceous infectious particles that cause neurodegenerative diseases, such as scrapie in sheep, bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease (CJD) in humans. Although the detailed process, regarding the abnormal conversion of prion proteins (PrP), remains to be fully elucidated, a number of environmental factors appear to affect the formation of misfolded PrP, termed PrPSc. Because oceanic algae contain mycosporine-like amino acids (MAAs), which exhibit cellular defensive activities under a variety of stress conditions, we investigated the level of PrPSc in prion-infected neuroblastoma cells using mycosporine-glycine, porphyra-334 and shinorine. When judged by the level of protease-resistant PrPSc in western blots, porphyra-334 and shinorine increased the level of PrPSc in cells, but mycosporine-glycine did not. The current results indicate that the MAAs tested in this study enhance the formation of PrPSc. © 2015, The Korean Society for Microbiology and Biotechnology.
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