Proteoglycans and Glycosaminoglycans in Misfolded Proteins Formation in Alzheimer's Disease

ISSN: 1875-5305 (Online)
ISSN: 0929-8665 (Print)

Volume 22 , 12 Issues, 2015

Download PDF Flyer

Protein & Peptide Letters

Aims & ScopeAbstracted/Indexed in

Submit Abstracts Online Submit Manuscripts Online

Prof. Ben M. Dunn
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL

View Full Editorial Board

Subscribe Purchase Articles Order Reprints

Current: 1.068
5 - Year: 1.124

Proteoglycans and Glycosaminoglycans in Misfolded Proteins Formation in Alzheimer's Disease

Protein & Peptide Letters, 21(10): 1048-1056.

Author(s): Peipei Wang and Kan Ding.

Affiliation: Glycobiology and Glycochemistry Lab, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.


Misfolded protein amyloid-beta protein (Aβ) and tau protein are two high hallmarks of Alzheimer’s disease (AD), representing significant targets in treating AD. Researches on mechanisms of the two proteins inducing neuron dysfunctions provide therapeutic strategies of AD, including inhibition of Aβ production and aggregation, acceleration of Aβ clearance as well as reduction of tau hyperphosphorylation. Proteoglycans (PGs) consist of a core protein and glycosaminoglycans (GAGs) chains, with enormous structural diversity due to variation in the core protein, the number of GAGs chains as well as extent and position of sulfation. Considerable evidences have indicated that PGs and GAGs play important roles in Aβ and tau processing. Numbers of GAGs and analogues have potential therapeutic function in AD. In this Review, we focus on the relationship of PGs and GAGs with misfolded proteins in AD and their potential therapeutic implications.


Alzheimer’s disease, amyloid-beta protein, glycosaminoglycans, proteoglycans, tau protein.

Purchase Online Order Reprints Order Eprints Rights and Permissions

Article Details

Volume: 21
Issue Number: 10
First Page: 1048
Last Page: 1056
Page Count: 9
DOI: 10.2174/0929866521666140626095145

Related Journals

Webmaster Contact: Copyright © 2015 Bentham Science