Fibrillar prion peptide (106-126) and scrapie prion protein hamper phagocytosis in microglia.
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| Abstract |
The inflammatory response in prion diseases is dominated by microglial activation. As macrophages of the central nervous system, the phagocytic capacity of microglia is well recognized, and it is possible that microglia are involved in the removal and processing of amyloid fibrils, thus preventing their harmful effect. We have analyzed the effects of a synthetic peptide of the human prion protein, PrP(106-126), which can form fibrils, and the pathogenic form of prion protein, PrPsc, on phagocytosis in microglia isolated from neonatal rat brain cultures. To some extent, fibrillar PrP(106-126) is internalized and processed. However, both synthetic prion peptide PrP(106-126) in a fibrillar form and pathogenic prion protein PrPsc severely hamper the phagocytic activity as measured by the uptake of beads by microglia. At a concentration that does not induce microglial death, PrP(106-126) reduced the number of beads internalized and altered their cytoplasmic distribution. This effect was not due to decreased binding of beads to the cell surface, nor restricted to specific classes of receptors. Although the PrP(106-126) did not prevent F-actin and Rac1 accumulation at sites of particle engulfment, it appeared to interfere with a later step of the internalization process.
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| Authors | Jaroslava Ciesielski-Treska, Nancy J Grant, Gabrielle Ulrich, Matthias Corrotte, Yannick Bailly, Anne-Marie Haeberle, Sylvette Chasserot-Golaz, Marie-France Bader |
| Journal | Glia (Glia) Vol. 46 Issue 2 Pg. 101-15 (Apr 15 2004) ISSN: 0894-1491 [Print] United States |
| PMID | 15042579 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
| Copyright | Copyright 2004 Wiley-Liss, Inc. |
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