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Misfolded proteins can form aggregates and induce a self-perpetuating process leading to the amplification and spreading of pathological protein assemblies. These misfolded protein assemblies act as seeds of aggregation. In an  in vivo  exogenous seeding model, both the features of seeds and the position at which seeding originates are precisely defined. Ample evidence from studies on intracerebal injection of amyloid-beta (Aβ)-rich brain extracts suggests that Aβ aggregation can be initiated by prion-like seeding. In this mini-review article, we will summarize the past and current literature on Aβ seeding in mouse models of AD and discuss its implementation as a tool to study cerebral amyloidosis and associated pathology.

Aβ Seeding as a Tool to Study Cerebral Amyloidosis and Associated Pathology