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The Bri2 and Bri3 BRICHOS Domains Interact Differently with Aβ42 and Alzheimer Amyloid Plaques.

Journal of Alzheimer's disease reports (2018-11-28)
Lisa Dolfe, Simone Tambaro, Helene Tigro, Marta Del Campo, Jeroen J M Hoozemans, Birgitta Wiehager, Caroline Graff, Bengt Winblad, Maria Ankarcrona, Margit Kaldmäe, Charlotte E Teunissen, Annica Rönnbäck, Jan Johansson, Jenny Presto
ABSTRACT

Alzheimer's disease (AD) is the most common form of dementia and there is no successful treatment available. Evidence suggests that fibril formation of the amyloid β-peptide (Aβ) is a major underlying cause of AD, and treatment strategies that reduce the toxic effects of Aβ amyloid are sought for. The BRICHOS domain is found in several proteins, including Bri2 (also called integral membrane protein 2B (ITM2B)), mutants of which are associated with amyloid and neurodegeneration, and Bri3 (ITM2C). We have used mouse hippocampal neurons and brain tissues from mice and humans and show Bri3 deposits dispersed on AD plaques. In contrast to what has been shown for Bri2, Bri3 immunoreactivity is decreased in AD brain homogenates compared to controls. Both Bri2 and Bri3 BRICHOS domains interact with Aβ40 and Aβ42 present in neurons and reduce Aβ42 amyloid fibril formation in vitro, but Bri3 BRICHOS is less efficient. These results indicate that Bri2 and Bri3 BRICHOS have different roles in relation to Aβ aggregation.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Amyloid β42 Antibody, clone G2-11, clone G2-11, from mouse
Sigma-Aldrich
Anti-ITM2C antibody produced in mouse, purified immunoglobulin, buffered aqueous solution
Sigma-Aldrich
Anti-ITM2B antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

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