Multiple Factors Contribute to the Peripheral Induction of Cerebral -Amyloidosis

• DOI: 10.1523/jneurosci.1608-14.2014
• Publication Date: 2014-07-30T17:05:04Z
• Authors: Y. S. Eisele; S. K. Fritschi; T. Hamaguchi; U. Obermuller; P. Fuger; A. Skodras; C. Schafer; J. Odenthal; M. Heikenwalder; M. Staufenbiel; M. Jucker
• Keywords: Amyloid (mycology)

Deposition of aggregated amyloid-β (Aβ) peptide in brain is an early event and hallmark pathology Alzheimer9s disease cerebral Aβ angiopathy. Experimental evidence supports the concept that multimers can act as seeds structurally corrupt other peptides by a self-propagating mechanism. Here we compare induction β-amyloidosis intraperitoneal applications Aβ-containing extracts three Aβ-precursor protein (APP) transgenic mouse lines differ levels transgene expression periphery (APP23 mice, APP23 mice lacking murine APP, R1.40 mice). Results revealed beta-amyloidosis induction, which could be blocked with anti-Aβ antibody, was dependent on amount inoculated extract level APP/Aβ but not periphery. The induced deposits occurred characteristic pattern consistent entry at multiple locations. Intraperitoneally injected detected blood monocytes some peripheral tissues (liver, spleen) up to 30 d after injection escaped histological biochemical detection thereafter. These results suggest intraperitoneally are transported from corruptive templating host occurs sites, most efficiently regions high availability soluble Aβ.