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000162686 0247_ $$2doi$$a10.1186/s40478-021-01263-x
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000162686 037__ $$aDZNE-2021-01343
000162686 041__ $$aEnglish
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000162686 1001_ $$00000-0002-1153-0440$$aJoshi, Pranav$$b0
000162686 245__ $$aTREM2 modulates differential deposition of modified and non-modified Aβ species in extracellular plaques and intraneuronal deposits.
000162686 260__ $$aLondon$$bBiomed Central$$c2021
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000162686 520__ $$aProgressive accumulation of Amyloid-β (Aβ) deposits in the brain is a characteristic neuropathological hallmark of Alzheimer's disease (AD). During disease progression, extracellular Aβ plaques undergo specific changes in their composition by the sequential deposition of different modified Aβ species. Microglia are implicated in the restriction of amyloid deposits and play a major role in internalization and degradation of Aβ. Recent studies showed that rare variants of the Triggering Receptor Expressed on Myeloid cells 2 (TREM2) are associated with an increased risk for AD. Post-translational modifications of Aβ could modulate the interaction with TREM2, and the uptake by microglia. Here, we demonstrate that genetic deletion of TREM2 or expression of a disease associated TREM2 variant in mice lead to differential accumulation of modified and non-modified Aβ species in extracellular plaques and intraneuronal deposits. Human brains with rare TREM2 AD risk variants also showed altered deposition of modified Aβ species in the different brain lesions as compared to cases with the common variant of TREM2. These findings indicate that TREM2 plays a critical role in the development and the composition of Aβ deposits, not only in extracellular plaques, but also intraneuronally, that both could contribute to the pathogenesis of AD.
000162686 536__ $$0G:(DE-HGF)POF4-352$$a352 - Disease Mechanisms (POF4-352)$$cPOF4-352$$fPOF IV$$x0
000162686 536__ $$0G:(DE-HGF)POF4-353$$a353 - Clinical and Health Care Research (POF4-353)$$cPOF4-353$$fPOF IV$$x1
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000162686 650_7 $$2Other$$aAβ
000162686 650_7 $$2Other$$aIntraneuronal
000162686 650_7 $$2Other$$aMicroglia
000162686 650_7 $$2Other$$aPost-translational modification
000162686 650_7 $$2Other$$aTREM2
000162686 650_7 $$2Other$$aVascular deposits
000162686 650_2 $$2MeSH$$aAged
000162686 650_2 $$2MeSH$$aAged, 80 and over
000162686 650_2 $$2MeSH$$aAlzheimer Disease: pathology
000162686 650_2 $$2MeSH$$aAmyloid beta-Peptides: chemistry
000162686 650_2 $$2MeSH$$aAmyloid beta-Peptides: metabolism
000162686 650_2 $$2MeSH$$aAnimals
000162686 650_2 $$2MeSH$$aFemale
000162686 650_2 $$2MeSH$$aHumans
000162686 650_2 $$2MeSH$$aMale
000162686 650_2 $$2MeSH$$aMembrane Glycoproteins: genetics
000162686 650_2 $$2MeSH$$aMembrane Glycoproteins: metabolism
000162686 650_2 $$2MeSH$$aMice
000162686 650_2 $$2MeSH$$aNeurons: pathology
000162686 650_2 $$2MeSH$$aPlaque, Amyloid: chemistry
000162686 650_2 $$2MeSH$$aPlaque, Amyloid: pathology
000162686 650_2 $$2MeSH$$aReceptors, Immunologic: genetics
000162686 650_2 $$2MeSH$$aReceptors, Immunologic: metabolism
000162686 7001_ $$00000-0001-8594-100X$$aRiffel, Florian$$b1
000162686 7001_ $$00000-0002-2792-7047$$aKumar, Sathish$$b2
000162686 7001_ $$0P:(DE-2719)9000326$$aVillacampa, Nàdia$$b3$$udzne
000162686 7001_ $$aTheil, Sandra$$b4
000162686 7001_ $$00000-0001-5807-190X$$aParhizkar, Samira$$b5
000162686 7001_ $$0P:(DE-2719)2202037$$aHaass, Christian$$b6$$udzne
000162686 7001_ $$aColonna, Marco$$b7
000162686 7001_ $$0P:(DE-2719)2000008$$aHeneka, Michael$$b8$$udzne
000162686 7001_ $$0P:(DE-2719)2811333$$aArzberger, Thomas$$b9$$udzne
000162686 7001_ $$0P:(DE-2719)2810441$$aHerms, Jochen$$b10$$udzne
000162686 7001_ $$0P:(DE-HGF)0$$aWalter, Jochen$$b11
000162686 773__ $$0PERI:(DE-600)2715589-4$$a10.1186/s40478-021-01263-x$$gVol. 9, no. 1, p. 168$$n1$$p168$$tActa Neuropathologica Communications$$v9$$x2051-5960$$y2021
000162686 8564_ $$uhttps://pub.dzne.de/record/162686/files/DZNE-2021-01343.pdf$$yOpenAccess
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