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.
journal_name
Immunobiologyjournal_title
Immunobiologyauthors
Sim RB,Kishore U,Villiers CL,Marche PN,Mitchell DAdoi
10.1016/j.imbio.2007.04.001subject
Has Abstractpub_date
2007-01-01 00:00:00pages
355-62issue
4-5eissn
0171-2985issn
1878-3279pii
S0171-2985(07)00048-4journal_volume
212pub_type
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