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C1q binding and complement activation by prions and amyloids.

Authors :
Sim RB
Kishore U
Villiers CL
Marche PN
Mitchell DA
Source :
Immunobiology [Immunobiology] 2007; Vol. 212 (4-5), pp. 355-62. Date of Electronic Publication: 2007 May 10.
Publication Year :
2007

Abstract

C1q binds to many non-self and altered-self-materials. These include microorganisms, immune complexes, apoptotic and necrotic cells and their breakdown products, and amyloids. C1q binding to amyloid fibrils found as extracellular deposits in tissues, and subsequent complement activation are involved in the pathology of several amyloid diseases, such as Alzheimer's disease. Prion diseases, such as scrapie also involve formation of amyloid by polymerization of the host prion protein (PrP). Complement activation is likely to contribute to neuronal damage in the end stages of prion diseases, but is also thought to participate in the initial infection, dissemination and replication stages. Infectious prion particles are likely to bind C1q and activate the complement system. Bound complement proteins may then influence the uptake and transport of prion particles by dendritic cells (DCs) and their subsequent proliferation at sites such as follicular DCs.

Details

Language :
English
ISSN :
0171-2985
Volume :
212
Issue :
4-5
Database :
MEDLINE
Journal :
Immunobiology
Publication Type :
Academic Journal
Accession number :
17544820
Full Text :
https://doi.org/10.1016/j.imbio.2007.04.001