The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.

People with Down syndrome (DS), caused by trisomy of chromosome 21 have a greatly increased risk of developing Alzheimer's disease (AD). This is in part because of triplication of a chromosome 21 gene, APP. This gene encodes amyloid precursor protein, which is cleaved to form amyloid-β that acc...

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Main Authors: Yixing Wu, Heather T Whittaker, Suzanna Noy, Karen Cleverley, Veronique Brault, Yann Herault, Elizabeth M C Fisher, Frances K Wiseman
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2021-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0242236
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author Yixing Wu
Heather T Whittaker
Suzanna Noy
Karen Cleverley
Veronique Brault
Yann Herault
Elizabeth M C Fisher
Frances K Wiseman
author_facet Yixing Wu
Heather T Whittaker
Suzanna Noy
Karen Cleverley
Veronique Brault
Yann Herault
Elizabeth M C Fisher
Frances K Wiseman
author_sort Yixing Wu
collection DOAJ
description People with Down syndrome (DS), caused by trisomy of chromosome 21 have a greatly increased risk of developing Alzheimer's disease (AD). This is in part because of triplication of a chromosome 21 gene, APP. This gene encodes amyloid precursor protein, which is cleaved to form amyloid-β that accumulates in the brains of people who have AD. Recent experimental results demonstrate that a gene or genes on chromosome 21, other than APP, when triplicated significantly accelerate amyloid-β pathology in a transgenic mouse model of amyloid-β deposition. Multiple lines of evidence indicate that cysteine cathepsin activity influences APP cleavage and amyloid-β accumulation. Located on human chromosome 21 (Hsa21) is an endogenous inhibitor of cathepsin proteases, CYSTATIN B (CSTB) which is proposed to regulate cysteine cathepsin activity in vivo. Here we determined if three copies of the mouse gene Cstb is sufficient to modulate amyloid-β accumulation and cathepsin activity in a transgenic APP mouse model. Duplication of Cstb resulted in an increase in transcriptional and translational levels of Cstb in the mouse cortex but had no effect on the deposition of insoluble amyloid-β plaques or the levels of soluble or insoluble amyloid-β42, amyloid-β40, or amyloid-β38 in 6-month old mice. In addition, the increased CSTB did not alter the activity of cathepsin B enzyme in the cortex of 3-month or 6-month old mice. These results indicate that the single-gene duplication of Cstb is insufficient to elicit a disease-modifying phenotype in the dupCstb x tgAPP mice, underscoring the complexity of the genetic basis of AD-DS and the importance of multiple gene interactions in disease.
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spelling doaj-art-ef70aabd7c9645f4a1ceae65bf660fef2025-08-20T02:23:16ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-01167e024223610.1371/journal.pone.0242236The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.Yixing WuHeather T WhittakerSuzanna NoyKaren CleverleyVeronique BraultYann HeraultElizabeth M C FisherFrances K WisemanPeople with Down syndrome (DS), caused by trisomy of chromosome 21 have a greatly increased risk of developing Alzheimer's disease (AD). This is in part because of triplication of a chromosome 21 gene, APP. This gene encodes amyloid precursor protein, which is cleaved to form amyloid-β that accumulates in the brains of people who have AD. Recent experimental results demonstrate that a gene or genes on chromosome 21, other than APP, when triplicated significantly accelerate amyloid-β pathology in a transgenic mouse model of amyloid-β deposition. Multiple lines of evidence indicate that cysteine cathepsin activity influences APP cleavage and amyloid-β accumulation. Located on human chromosome 21 (Hsa21) is an endogenous inhibitor of cathepsin proteases, CYSTATIN B (CSTB) which is proposed to regulate cysteine cathepsin activity in vivo. Here we determined if three copies of the mouse gene Cstb is sufficient to modulate amyloid-β accumulation and cathepsin activity in a transgenic APP mouse model. Duplication of Cstb resulted in an increase in transcriptional and translational levels of Cstb in the mouse cortex but had no effect on the deposition of insoluble amyloid-β plaques or the levels of soluble or insoluble amyloid-β42, amyloid-β40, or amyloid-β38 in 6-month old mice. In addition, the increased CSTB did not alter the activity of cathepsin B enzyme in the cortex of 3-month or 6-month old mice. These results indicate that the single-gene duplication of Cstb is insufficient to elicit a disease-modifying phenotype in the dupCstb x tgAPP mice, underscoring the complexity of the genetic basis of AD-DS and the importance of multiple gene interactions in disease.https://doi.org/10.1371/journal.pone.0242236
spellingShingle Yixing Wu
Heather T Whittaker
Suzanna Noy
Karen Cleverley
Veronique Brault
Yann Herault
Elizabeth M C Fisher
Frances K Wiseman
The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.
PLoS ONE
title The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.
title_full The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.
title_fullStr The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.
title_full_unstemmed The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.
title_short The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.
title_sort effects of cstb duplication on app amyloid β pathology and cathepsin b activity in a mouse model
url https://doi.org/10.1371/journal.pone.0242236
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