Open AccessAmyloid‐beta 1‐40 is associated with alterations in NG2+ pericyte population ex vivo and in vitro
Author(s) -
Schultz Nina,
Brännström Kristoffer,
Byman Elin,
Moussaud Simon,
Nielsen Henrietta M.,
Olofsson Anders,
Wennström Malin
Publication year - 2018
Publication title -
aging cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.103
H-Index - 140
eISSN - 1474-9726
pISSN - 1474-9718
DOI - 10.1111/acel.12728
Subject(s) - pericyte , biology , ex vivo , population , amyloid beta , microbiology and biotechnology , in vitro , viability assay , alzheimer's disease , pathology , biochemistry , peptide , endothelial stem cell , disease , medicine , environmental health
Summary The population of brain pericytes, a cell type important for vessel stability and blood brain barrier function, has recently been shown altered in patients with Alzheimer's disease ( AD ). The underlying reason for this alteration is not fully understood, but progressive accumulation of the AD characteristic peptide amyloid‐beta (Aβ) has been suggested as a potential culprit. In the current study, we show reduced number of hippocampal NG 2+ pericytes and an association between NG 2+ pericyte numbers and Aβ1‐40 levels in AD patients. We further demonstrate, using in vitro studies, an aggregation‐dependent impact of Aβ1‐40 on human NG 2+ pericytes. Fibril‐ EP Aβ1‐40 exposure reduced pericyte viability and proliferation and increased caspase 3/7 activity. Monomer Aβ1‐40 had quite the opposite effect: increased pericyte viability and proliferation and reduced caspase 3/7 activity. Oligomer‐ EP Aβ1‐40 had no impact on either of the cellular events. Our findings add to the growing number of studies suggesting a significant impact on pericytes in the brains of AD patients and suggest different aggregation forms of Aβ1‐40 as potential key regulators of the brain pericyte population size.