Therapeutic Potential of Direct Clearance of the Amyloid-β in Alzheimer's Disease.

Alzheimer’s disease amyloid-β cerebrospinal fluid lipoprotein receptor-related protein 1 receptor for advanced glycation endproducts

Journal

Brain sciences
ISSN: 2076-3425
Titre abrégé: Brain Sci
Pays: Switzerland
ID NLM: 101598646

Informations de publication

Date de publication:
10 Feb 2020
Historique:
received: 23 01 2020
revised: 05 02 2020
accepted: 05 02 2020
entrez: 14 2 2020
pubmed: 14 2 2020
medline: 14 2 2020
Statut: epublish

Résumé

Alzheimer's disease (AD) is characterized by deposition and accumulation of amyloid-β (Aβ) and its corresponding plaques within the brain. Although much debate exists whether these plaques are the cause or the effect of AD, the accumulation of Aβ is linked with the imbalance between the production and clearance of Aβ. The receptor for advanced glycation endproducts (RAGE) facilitates entry of free Aβ from the peripheral stream. Conversely, lipoprotein receptor-related protein 1 (LRP1), located in the abluminal side at the blood-brain barrier mediates the efflux of Aβ. Research on altering the rates of clearance of A by targeting these two pathways has been extensively study. Additionally, a cerebrospinal fluid (CSF) circulation assistant device has also been evaluated as an approach to increase solute concentration in the CSF via mechanical drainage, to allow for removal of Aβ from the brain. Herein, we provide a brief review of these approaches that are designed to re-establish a homeostatic Aβ balance in the brain.

Identifiants

pubmed: 32050618
pii: brainsci10020093
doi: 10.3390/brainsci10020093
pmc: PMC7071829
pii:
doi:

Types de publication

Journal Article

Langues

eng

Déclaration de conflit d'intérêts

The authors declare no conflicts of interest.

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Auteurs

Dong Eun Kim (DE)

Massachusetts College of Pharmacy and Health Science University, Boston, MA 02115, USA.

Ronny Priefer (R)

Massachusetts College of Pharmacy and Health Science University, Boston, MA 02115, USA.

Classifications MeSH