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Despite these obvious public health concerns, surprisingly little is known about the mechanism by which PrP-scrapie (PrP<jats:sup>Sc<\/jats:sup>), the most reliable surrogate marker of infection in BSE-contaminated food, crosses the human intestinal epithelial cell barrier. Here we show that digestive enzyme (DE) treatment of sporadic CJD brain homogenate generates a C-terminal fragment similar to the proteinase K-resistant PrP<jats:sup>Sc<\/jats:sup>core of 27-30 kDa implicated in prion disease transmission and pathogenesis. Notably, DE treatment results in a PrP<jats:sup>Sc<\/jats:sup>-protein complex that is avidly transcytosed in vesicular structures across an<jats:italic>in vitro<\/jats:italic>model of the human intestinal epithelial cell barrier, regardless of the amount of endogenous PrP<jats:sup>C<\/jats:sup>expression. Unexpectedly, PrP<jats:sup>Sc<\/jats:sup>is cotransported with ferritin, a prominent component of the DE-treated PrP<jats:sup>Sc<\/jats:sup>-protein complex. The transport of PrP<jats:sup>Sc<\/jats:sup>-ferritin is sensitive to low temperature, brefeldin-A, and nocodazole treatment and is inhibited by excess free ferritin, implicating a receptor- or transporter-mediated pathway. Because ferritin shares considerable homology across species, these data suggest that PrP<jats:sup>Sc<\/jats:sup>-associated proteins, in particular ferritin, may facilitate PrP<jats:sup>Sc<\/jats:sup>uptake in the intestine from distant species, leading to a carrier state in humans.<\/jats:p>","DOI":"10.1523\/jneurosci.2864-04.2004","type":"journal-article","created":{"date-parts":[[2004,12,15]],"date-time":"2004-12-15T21:09:50Z","timestamp":1103144990000},"page":"11280-11290","source":"Crossref","is-referenced-by-count":87,"title":["Protease-Resistant Human Prion Protein and Ferritin Are Cotransported across Caco-2 Epithelial Cells: Implications for Species Barrier in Prion Uptake from the Intestine"],"prefix":"10.1523","volume":"24","author":[{"given":"Ravi 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