Journal
JOURNAL OF NEUROCHEMISTRY
Volume 107, Issue 3, Pages 636-646Publisher
WILEY
DOI: 10.1111/j.1471-4159.2008.05628.x
Keywords
amyloid; lactoferrin; N2a cells; prion; PrPC; PrPSc
Categories
Funding
- Bovine Spongiform Encephalopathy Control Project of the Ministry of Agriculture, Forestry and Fisheries of Japan
- Special Coordination Funds
- Ministry of Education, Culture, Sports, Science and Technology, Japan
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Prion diseases are fatal neurodegenerative disorders, and the conformational conversion of normal cellular prion protein (PrPC) into its pathogenic, amyloidogenic isoform (PrPSc) is the essential event in the pathogenesis of these diseases. Lactoferrin (LF) is a cationic iron-binding glycoprotein belonging to the transferrin (TF) family, which accumulates in the amyloid deposits in the brain in neurodegenerative disorders, such as Alzheimer's disease and Pick's disease. In the present study, we have examined the effects of LF on PrPSc formation by using cell culture models. Bovine LF inhibited PrPSc accumulation in scrapie-infected cells in a time- and dose-dependent manner, whereas TF was not inhibitory. Bioassays of LF-treated cells demonstrated prolonged incubation periods compared with non-treated cells indicating a reduction of prion infectivity. LF mediated the cell surface retention of PrPC by diminishing its internalization and was capable of interacting with PrPC in addition to PrPSc. Furthermore, LF partially inhibited the formation of protease-resistant PrP as determined by the protein misfolding cyclic amplification assay. Our results suggest that LF has multifunctional antiprion activities.
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