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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Activation of human microglia by fibrillar prion protein-related peptides is enhanced by amyloid- associated factors SAP and C1q.

Complement activation products C1q and C3d, serum amyloid P component (SAP) and activated glial cells accumulate in amyloid deposits of conformationally changed prion protein (PrP(Sc)) in Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker disease and scrapie-infected mouse brain. Biological properties, including the potential to activate microglia, relate to prion ( PrP) peptide fibrillogenic abilities. We investigated if SAP and C1q influence the fibrillogenic properties of human and mouse PrP peptide and concomitantly their stimulatory effects on human microglia in vitro. PrP-peptide induced microglial IL-6 and TNF-alpha release significantly increased in the presence of SAP and C1q. Also, SAP and C1q enhanced PrP-peptide fibril formation as revealed by electron microscopy and thioflavin S-based quantitative assays. This suggests that SAP and C1q contribute to fibrillar state-dependent cellular effects of PrP. Combined, ultrastructural and thioflavin assays, together with microglial cytokine release measurements, provide a test system to screen potential, fibrillarity impeding therapeutics for prion disease.[1]


  1. Activation of human microglia by fibrillar prion protein-related peptides is enhanced by amyloid-associated factors SAP and C1q. Veerhuis, R., Boshuizen, R.S., Morbin, M., Mazzoleni, G., Hoozemans, J.J., Langedijk, J.P., Tagliavini, F., Langeveld, J.P., Eikelenboom, P. Neurobiol. Dis. (2005) [Pubmed]
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