BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.

M. Del Campo Milan; C.R. Oliveira; W. Scheper; R. Zwart; C. Korth; A. Muller-Schiffmann; G Kostallas; H Biverstal; J Presto; J. Johansson; J.J. Hoozemans; C.F. Pereira; C.E. Teunissen; M. del Campo

doi:https://doi.org/10.1007/s00018-014-1769-y

BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.

M. Del Campo Milan, C.R. Oliveira, W. Scheper, R. Zwart, C. Korth, A. Muller-Schiffmann, G Kostallas, H Biverstal, J Presto, J. Johansson, J.J. Hoozemans, C.F. Pereira, C.E. Teunissen, M. del Campo

Research output: Contribution to journal › Article › Academic › peer-review

12 Citations (Scopus)

Abstract

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

Original language	English
Pages (from-to)	1599-1611
Journal	Cellular and molecular life sciences
Volume	72
Issue number	8
DOIs	https://doi.org/10.1007/s00018-014-1769-y
Publication status	Published - 2015

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Del Campo Milan, M., Oliveira, C. R., Scheper, W., Zwart, R., Korth, C., Muller-Schiffmann, A., Kostallas, G., Biverstal, H., Presto, J., Johansson, J., Hoozemans, J. J., Pereira, C. F., Teunissen, C. E., & del Campo, M. (2015). BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells. Cellular and molecular life sciences, 72(8), 1599-1611. https://doi.org/10.1007/s00018-014-1769-y

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title = "BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.",

abstract = "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",

author = "{Del Campo Milan}, M. and C.R. Oliveira and W. Scheper and R. Zwart and C. Korth and A. Muller-Schiffmann and G Kostallas and H Biverstal and J Presto and J. Johansson and J.J. Hoozemans and C.F. Pereira and C.E. Teunissen and {del Campo}, M.",

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Del Campo Milan, M, Oliveira, CR, Scheper, W, Zwart, R, Korth, C, Muller-Schiffmann, A, Kostallas, G, Biverstal, H, Presto, J, Johansson, J, Hoozemans, JJ, Pereira, CF, Teunissen, CE & del Campo, M 2015, 'BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.', Cellular and molecular life sciences, vol. 72, no. 8, pp. 1599-1611. https://doi.org/10.1007/s00018-014-1769-y

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.

AU - del Campo, M.

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

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U2 - https://doi.org/10.1007/s00018-014-1769-y

DO - https://doi.org/10.1007/s00018-014-1769-y

M3 - Article

C2 - 25336154

SN - 1420-682X

VL - 72

SP - 1599

EP - 1611

JO - Cellular and molecular life sciences

JF - Cellular and molecular life sciences

IS - 8

ER -

BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.

Abstract

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