Ablation of prion protein in wild type human amyloid precursor protein (APP) transgenic mice does not alter the proteolysis of APP, levels of amyloid-β or pathologic phenotypeCitation formats

  • External authors:
  • Isobel J. Whitehouse
  • Deborah Brown
  • Herbert Baybutt
  • Abigail B. Diack
  • Pedro Piccardo
  • Jean C. Manson

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Ablation of prion protein in wild type human amyloid precursor protein (APP) transgenic mice does not alter the proteolysis of APP, levels of amyloid-β or pathologic phenotype. / Whitehouse, Isobel J.; Brown, Deborah; Baybutt, Herbert ; Diack, Abigail B. ; Kellett, Katherine; Piccardo, Pedro; Manson, Jean C. ; Hooper, Nigel.

In: PLoS ONE, Vol. 11, No. 7, e0159119, 22.07.2016.

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Whitehouse, Isobel J. ; Brown, Deborah ; Baybutt, Herbert ; Diack, Abigail B. ; Kellett, Katherine ; Piccardo, Pedro ; Manson, Jean C. ; Hooper, Nigel. / Ablation of prion protein in wild type human amyloid precursor protein (APP) transgenic mice does not alter the proteolysis of APP, levels of amyloid-β or pathologic phenotype. In: PLoS ONE. 2016 ; Vol. 11, No. 7.

Bibtex

@article{93c4bde7d002496ab5927b6e5270c3be,
title = "Ablation of prion protein in wild type human amyloid precursor protein (APP) transgenic mice does not alter the proteolysis of APP, levels of amyloid-β or pathologic phenotype",
abstract = "The cellular prion protein (PrPC) has been proposed to play an important role in the pathogenesis of Alzheimer’s disease. In cellular models PrPC inhibited the action of the β-secretase BACE1 on wild type amyloid precursor protein resulting in a reduction in amyloid-β (Aβ) peptides. Here we have assessed the effect of genetic ablation of PrPC in transgenic mice expressing human wild type amyloid precursor protein (line I5). Deletion of PrPC had no effect on the α- and β-secretase proteolysis of the amyloid precursor protein (APP) nor on the amount of Aβ38, Aβ40 or Aβ42 in the brains of the mice. In addition, ablation of PrPC did not alter Aβ deposition or histopathology phenotype in this transgenic model. Thus using this transgenic model we could not provide evidence to support the hypothesis that PrPC regulates Aβ production.",
author = "Whitehouse, {Isobel J.} and Deborah Brown and Herbert Baybutt and Diack, {Abigail B.} and Katherine Kellett and Pedro Piccardo and Manson, {Jean C.} and Nigel Hooper",
year = "2016",
month = "7",
day = "22",
doi = "10.1371/journal.pone.0159119",
language = "English",
volume = "11",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "7",

}

RIS

TY - JOUR

T1 - Ablation of prion protein in wild type human amyloid precursor protein (APP) transgenic mice does not alter the proteolysis of APP, levels of amyloid-β or pathologic phenotype

AU - Whitehouse, Isobel J.

AU - Brown, Deborah

AU - Baybutt, Herbert

AU - Diack, Abigail B.

AU - Kellett, Katherine

AU - Piccardo, Pedro

AU - Manson, Jean C.

AU - Hooper, Nigel

PY - 2016/7/22

Y1 - 2016/7/22

N2 - The cellular prion protein (PrPC) has been proposed to play an important role in the pathogenesis of Alzheimer’s disease. In cellular models PrPC inhibited the action of the β-secretase BACE1 on wild type amyloid precursor protein resulting in a reduction in amyloid-β (Aβ) peptides. Here we have assessed the effect of genetic ablation of PrPC in transgenic mice expressing human wild type amyloid precursor protein (line I5). Deletion of PrPC had no effect on the α- and β-secretase proteolysis of the amyloid precursor protein (APP) nor on the amount of Aβ38, Aβ40 or Aβ42 in the brains of the mice. In addition, ablation of PrPC did not alter Aβ deposition or histopathology phenotype in this transgenic model. Thus using this transgenic model we could not provide evidence to support the hypothesis that PrPC regulates Aβ production.

AB - The cellular prion protein (PrPC) has been proposed to play an important role in the pathogenesis of Alzheimer’s disease. In cellular models PrPC inhibited the action of the β-secretase BACE1 on wild type amyloid precursor protein resulting in a reduction in amyloid-β (Aβ) peptides. Here we have assessed the effect of genetic ablation of PrPC in transgenic mice expressing human wild type amyloid precursor protein (line I5). Deletion of PrPC had no effect on the α- and β-secretase proteolysis of the amyloid precursor protein (APP) nor on the amount of Aβ38, Aβ40 or Aβ42 in the brains of the mice. In addition, ablation of PrPC did not alter Aβ deposition or histopathology phenotype in this transgenic model. Thus using this transgenic model we could not provide evidence to support the hypothesis that PrPC regulates Aβ production.

U2 - 10.1371/journal.pone.0159119

DO - 10.1371/journal.pone.0159119

M3 - Article

VL - 11

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 7

M1 - e0159119

ER -