Role of proteoglycans and glycosaminoglycans in the pathogenesis of Alzheimer's disease and related disorders: amyloidogenesis and therapeutic strategies--a review

Journal of Neuroscience Research
Toshio ArigaRobert K Yu

Abstract

The extracellular accumulation of amyloid beta proteins (Abetas) in neuritic plaques is one of the hallmarks of Alzheimer's disease (AD). The binding of Abetas to extracellular membranes (ECMs) is a critical step in developing AD. Abetas bind to many biomolecules, including lipids, proteins, and proteoglycans (PGs). PGs play several roles in amyloid formation, including promoting the aggregation of Abetas into insoluble amyloid fibrils, which contributes to the increased neurotoxicity of Abetas. Although Abetas readily self-aggregate to form amyloid fibrils in vitro, their binding to PGs and heparin enhances amyloid aggregation and fibril formation. The sulfate moiety in glycosaminoglycans (GAGs), the carbohydrate portion of PGs, is necessary for the formation of amyloid fibrils; no fibrils are observed in the presence of hyaluronic acid (HA), a nonsulfated GAG. PGs and Abetas are known to colocalize in senile plaques (SPs) and neurofibrillary tangles (NFTs) in the AD brain. The binding site of PGs to Abetas has been identified in the 13-16-amino-acid region (His-His-Gln-Lys) of Abetas and represents a unique target site for inhibition of amyloid fibril formation; His13 in particular is an important residue critical for interac...Continue Reading

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