TY - JOUR
T1 - Heparan sulphate proteoglycans in Alzheimer's disease and amyloid-related disorders
AU - Van Horssen, Jack
AU - Wesseling, Pieter
AU - Van Den Heuvel, Lambert P.W.J.
AU - De Waal, Robert M.W.
AU - Verbeek, Marcel M.
PY - 2003/8/1
Y1 - 2003/8/1
N2 - Proteoglycans are associated with all kinds of amyloid deposits in the human body. These complex macromolecules, in particular heparan sulphate proteoglycans, have also been implicated in several features of the pathogenesis of Alzheimer's disease (AD), including the genesis of senile plaques, cerebrovascular amyloid, and neurofibrillary tangles. In this review we focus on the role of proteoglycans and glycosaminoglycans in amyloidogenesis in general and in AD in particular. Heparan sulphate proteoglycans may promote amyloid-β peptide (Aβ) or tau fibrillisation on the one hand, and provide resistance against proteolytic breakdown on the other. Knowledge about the role of proteoglycans in AD pathology may eventually be of therapeutic use, because small polysulphated compounds, which can interfere with the interaction between proteoglycan and Aβ, have been shown to stop or even prevent amyloidogenesis.
AB - Proteoglycans are associated with all kinds of amyloid deposits in the human body. These complex macromolecules, in particular heparan sulphate proteoglycans, have also been implicated in several features of the pathogenesis of Alzheimer's disease (AD), including the genesis of senile plaques, cerebrovascular amyloid, and neurofibrillary tangles. In this review we focus on the role of proteoglycans and glycosaminoglycans in amyloidogenesis in general and in AD in particular. Heparan sulphate proteoglycans may promote amyloid-β peptide (Aβ) or tau fibrillisation on the one hand, and provide resistance against proteolytic breakdown on the other. Knowledge about the role of proteoglycans in AD pathology may eventually be of therapeutic use, because small polysulphated compounds, which can interfere with the interaction between proteoglycan and Aβ, have been shown to stop or even prevent amyloidogenesis.
UR - http://www.scopus.com/inward/record.url?scp=0038376613&partnerID=8YFLogxK
U2 - 10.1016/S1474-4422(03)00484-8
DO - 10.1016/S1474-4422(03)00484-8
M3 - Review article
C2 - 12878436
AN - SCOPUS:0038376613
SN - 1474-4422
VL - 2
SP - 482
EP - 492
JO - Lancet Neurology
JF - Lancet Neurology
IS - 8
ER -