Oligomeric human Aβ1-42 inhibits antigen presentation

The goal of this study is to investigate the involvement of inflammation in Alzheimer’s disease (AD) and to clarify the signaling pathways involved in the presence of beta-amyloidosis, a hallmark of AD pathogenesis, to help identifying potential targets for therapy. To do that, we isolated bone marrow-derived progenitor cells from femurs, tibiae and hip bones of non-transgenic C57BL/6 mice according to established protocols , and we maturated them with LPS. To obtain an unbiased view of gene regulation in mouse bone marrow-derived dendritic cells (BM-DCs) exposed to pre-aggregated beta-amyloid peptide (Aβ) oligomers, we analyzed the transcriptome of untreated immature control BM-DCs (‘Ctrl’), LPS-treated BM-DCs (’LPS’), Aβ1-42 oligomer-treated BM-DCs (‘Aβ‘) and BM-DCs treated with Aβ1-42 oligomers and LPS (‘Aβ+LPS‘) via explorative RNA-sequencing. Relative comparison of mRNA profile of mouse bone marrow-derived dendritic cells with different treatments: (1) control bone marrow-derived dendritic cells (‘Ctrl’), (2) LPS-treated bone marrow-derived dendritic cells (’LPS’), (3) Aβ1-42 oligomer-treated bone marrow-derived dendritic cells (‘Aβ‘), (4) and bone marrow-derived dendritic cells treated with Aβ1-42 oligomers and LPS (‘Aβ+LPS‘). The RNA sequencing was performed in single reads of 100bp length using Illumina HiSeq3000 (Illumina), data were generated in triplicate.