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The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease. / Gough, Mallory; Blanthorn-Hazell, Sophee; Parkin, Edward T.
In: Journal of Alzheimer's Disease, Vol. 43, No. 4, 2015, p. 1163-1168.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Gough, M, Blanthorn-Hazell, S & Parkin, ET 2015, 'The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease', Journal of Alzheimer's Disease, vol. 43, no. 4, pp. 1163-1168. https://doi.org/10.3233/JAD-141650

APA

Gough, M., Blanthorn-Hazell, S., & Parkin, E. T. (2015). The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease. Journal of Alzheimer's Disease, 43(4), 1163-1168. https://doi.org/10.3233/JAD-141650

Vancouver

Gough M, Blanthorn-Hazell S, Parkin ET. The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease. Journal of Alzheimer's Disease. 2015;43(4):1163-1168. Epub 2014 Aug 28. doi: 10.3233/JAD-141650

Author

Gough, Mallory ; Blanthorn-Hazell, Sophee ; Parkin, Edward T. / The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease. In: Journal of Alzheimer's Disease. 2015 ; Vol. 43, No. 4. pp. 1163-1168.

Bibtex

@article{5c12e76a82fb45d4b63828a0b8cb020f,
title = "The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease",
abstract = "Amyloid-β protein precursor (AβPP) proteolysis by β- and γ-secretases generates neurotoxic amyloid-β (Aβ)-peptides in Alzheimer's disease (AD). We have investigated the role of histidine residues within the extracellular E1 copper binding and Aβ domains of AβPP in its proteolysis. By stably expressing histidine to alanine AβPP mutant constructs in SH-SY5Y cells, we show that mutations in the E1 copper binding domain had no impact on α- or β-secretase processing. Mutation of histidine 14 within the Aβ-domain specifically down-regulated β-secretase processing without impacting on non-amyloidogenic proteolysis. Understanding how histidine 14 participates in AβPP proteolysis may reveal new intervention points for AD treatments.",
keywords = "Amyloid-β protein precursor, amyloidogenic processing, β-secretase, histidine 14",
author = "Mallory Gough and Sophee Blanthorn-Hazell and Parkin, {Edward T}",
year = "2015",
doi = "10.3233/JAD-141650",
language = "English",
volume = "43",
pages = "1163--1168",
journal = "Journal of Alzheimer's Disease",
issn = "1387-2877",
publisher = "NLM (Medline)",
number = "4",

}

RIS

TY - JOUR

T1 - The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease

AU - Gough, Mallory

AU - Blanthorn-Hazell, Sophee

AU - Parkin, Edward T

PY - 2015

Y1 - 2015

N2 - Amyloid-β protein precursor (AβPP) proteolysis by β- and γ-secretases generates neurotoxic amyloid-β (Aβ)-peptides in Alzheimer's disease (AD). We have investigated the role of histidine residues within the extracellular E1 copper binding and Aβ domains of AβPP in its proteolysis. By stably expressing histidine to alanine AβPP mutant constructs in SH-SY5Y cells, we show that mutations in the E1 copper binding domain had no impact on α- or β-secretase processing. Mutation of histidine 14 within the Aβ-domain specifically down-regulated β-secretase processing without impacting on non-amyloidogenic proteolysis. Understanding how histidine 14 participates in AβPP proteolysis may reveal new intervention points for AD treatments.

AB - Amyloid-β protein precursor (AβPP) proteolysis by β- and γ-secretases generates neurotoxic amyloid-β (Aβ)-peptides in Alzheimer's disease (AD). We have investigated the role of histidine residues within the extracellular E1 copper binding and Aβ domains of AβPP in its proteolysis. By stably expressing histidine to alanine AβPP mutant constructs in SH-SY5Y cells, we show that mutations in the E1 copper binding domain had no impact on α- or β-secretase processing. Mutation of histidine 14 within the Aβ-domain specifically down-regulated β-secretase processing without impacting on non-amyloidogenic proteolysis. Understanding how histidine 14 participates in AβPP proteolysis may reveal new intervention points for AD treatments.

KW - Amyloid-β protein precursor

KW - amyloidogenic processing

KW - β-secretase

KW - histidine 14

U2 - 10.3233/JAD-141650

DO - 10.3233/JAD-141650

M3 - Journal article

C2 - 25171714

VL - 43

SP - 1163

EP - 1168

JO - Journal of Alzheimer's Disease

JF - Journal of Alzheimer's Disease

SN - 1387-2877

IS - 4

ER -