TY - JOUR
T1 - BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.
AU - Del Campo Milan, M.
AU - Oliveira, C.R.
AU - Scheper, W.
AU - Zwart, R.
AU - Korth, C.
AU - Muller-Schiffmann, A.
AU - Kostallas, G
AU - Biverstal, H
AU - Presto, J
AU - Johansson, J.
AU - Hoozemans, J.J.
AU - Pereira, C.F.
AU - Teunissen, C.E.
PY - 2015
Y1 - 2015
N2 - Alzheimer's disease (AD) is pathologically characterized by the presence of misfolded proteins such as amyloid beta (Aβ) in senile plaques, and hyperphosphorylated tau and truncated tau in neurofibrillary tangles (NFT). The BRI2 protein inhibits Aβ aggregation via its BRICHOS domain and regulates critical proteins involved in initiating the amyloid cascade, which has been hypothesized to be central in AD pathogenesis. We recently detected the deposition of BRI2 ectodomain associated with Aβ plaques and concomitant changes in its processing enzymes in early stages of AD. Here, we aimed to investigate the effects of recombinant BRI2 ectodomain (rBRI2
AB - Alzheimer's disease (AD) is pathologically characterized by the presence of misfolded proteins such as amyloid beta (Aβ) in senile plaques, and hyperphosphorylated tau and truncated tau in neurofibrillary tangles (NFT). The BRI2 protein inhibits Aβ aggregation via its BRICHOS domain and regulates critical proteins involved in initiating the amyloid cascade, which has been hypothesized to be central in AD pathogenesis. We recently detected the deposition of BRI2 ectodomain associated with Aβ plaques and concomitant changes in its processing enzymes in early stages of AD. Here, we aimed to investigate the effects of recombinant BRI2 ectodomain (rBRI2
UR - http://www.scopus.com/inward/record.url?eid=2-s2.0-84925393089&partnerID=MN8TOARS
U2 - 10.1007/s00018-014-1769-y
DO - 10.1007/s00018-014-1769-y
M3 - Article
SN - 1420-682X
VL - 72
SP - 1599
EP - 1611
JO - Cellular and Molecular Life Sciences
JF - Cellular and Molecular Life Sciences
IS - 8
ER -
