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http://dx.doi.org/10.4014/mbl.1503.03002

Enhanced Formation of Scrapie Prion Protein in Cultured Cells by Treatment with Mycosporine-like Amino Acids (MAAs)  

Lee, Jihyun (Department of Pharmacy, Hanyang University)
Moh, Sang-Hyun (Anti-Aging Research Institute of Bio-FD&C Co. Ltd.)
Ryou, Chongsuk (Department of Pharmacy, Hanyang University)
Kim, Dae-Hwan (College of Pharmacy Institute of Pharmaceutical Science and Technology, College of Pharmacy, Hanyang University)
Publication Information
Microbiology and Biotechnology Letters / v.43, no.2, 2015 , pp. 91-96 More about this Journal
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.
Keywords
Protein aggregation; prion; PrP; mycosporine-like amino acids;
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