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Verfasst von:Enzlein, Thomas [VerfasserIn]   i
 Lashley, Tammaryn [VerfasserIn]   i
 Sammour, Denis Abu [VerfasserIn]   i
 Hopf, Carsten [VerfasserIn]   i
 Chávez-Gutiérrez, Lucía [VerfasserIn]   i
Titel:Integrative single-plaque analysis reveals signature Aβ and lipid profiles in the Alzheimer’s brain
Verf.angabe:Thomas Enzlein, Tammaryn Lashley, Denis Abu Sammour, Carsten Hopf, and Lucía Chávez-Gutiérrez
Jahr:2024
Umfang:9 S.
Illustrationen:Illustrationen
Fussnoten:Online veröffentlicht: 3. Juni 2024 ; Gesehen am 15.01.2025
Titel Quelle:Enthalten in: Analytical chemistry
Ort Quelle:Columbus, Ohio : American Chemical Society, 1947
Jahr Quelle:2024
Band/Heft Quelle:96(2024), 24, Seite 9799-9807
ISSN Quelle:1520-6882
Abstract:Cerebral accumulation of amyloid-β (Aβ) initiates molecular and cellular cascades that lead to Alzheimer’s disease (AD). However, amyloid deposition does not invariably lead to dementia. Amyloid-positive but cognitively unaffected (AP-CU) individuals present widespread amyloid pathology, suggesting that molecular signatures more complex than the total amyloid burden are required to better differentiate AD from AP-CU cases. Motivated by the essential role of Aβ and the key lipid involvement in AD pathogenesis, we applied multimodal mass spectrometry imaging (MSI) and machine learning (ML) to investigate amyloid plaque heterogeneity, regarding Aβ and lipid composition, in AP-CU versus AD brain samples at the single-plaque level. Instead of focusing on a population mean, our analytical approach allowed the investigation of large populations of plaques at the single-plaque level. We found that different (sub)populations of amyloid plaques, differing in Aβ and lipid composition, coexist in the brain samples studied. The integration of MSI data with ML-based feature extraction further revealed that plaque-associated gangliosides GM2 and GM1, as well as Aβ1-38, but not Aβ1-42, are relevant differentiators between the investigated pathologies. The pinpointed differences may guide further fundamental research investigating the role of amyloid plaque heterogeneity in AD pathogenesis/progression and may provide molecular clues for further development of emerging immunotherapies to effectively target toxic amyloid assemblies in AD therapy. Our study exemplifies how an integrative analytical strategy facilitates the unraveling of complex biochemical phenomena, advancing our understanding of AD from an analytical perspective and offering potential avenues for the refinement of diagnostic tools.
DOI:doi:10.1021/acs.analchem.3c05557
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

kostenfrei: Volltext: https://doi.org/10.1021/acs.analchem.3c05557
 DOI: https://doi.org/10.1021/acs.analchem.3c05557
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:191464994X
Verknüpfungen:→ Zeitschrift

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