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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