The role of HS (heparan sulphate) in the pathology of AD (Alzheimer's disease) is multifaceted. HS and other glycosaminoglycans have been widely reported to be associated with neuritic plaques. HS has also been shown to promote the aggregation of Aβ (amyloid β-peptide), the proteinaceous component of neuritic plaques. Recently, we described a novel and contrasting role for HS in the pathology of AD: HS can inhibit the formation of Aβ, by directly interacting with the protease BACE1 (β-site amyloid precursor protein cleaving enzyme 1; β-secretase 1), that cleaves the amyloid precursor protein and is the rate limiting step in the generation of Aβ. Here, we review the current roles of HS and the potential for HS-derivatives in the treatment of AD.
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October 2005
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Research Article|
October 26 2005
Novel heparan sulphate analogues: inhibition of β-secretase cleavage of amyloid precursor protein
S.J. Patey;
S.J. Patey
1
1Molecular Glycobiology Research Group, School of Biological Sciences, The University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.
1To whom correspondence should be addressed (email s.j.patey@liv.ac.uk).
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E.A. Yates;
E.A. Yates
1Molecular Glycobiology Research Group, School of Biological Sciences, The University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.
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J.E. Turnbull
J.E. Turnbull
1Molecular Glycobiology Research Group, School of Biological Sciences, The University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.
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Biochem Soc Trans (2005) 33 (5): 1116–1118.
Article history
Received:
June 27 2005
Citation
S.J. Patey, E.A. Yates, J.E. Turnbull; Novel heparan sulphate analogues: inhibition of β-secretase cleavage of amyloid precursor protein. Biochem Soc Trans 26 October 2005; 33 (5): 1116–1118. doi: https://doi.org/10.1042/BST0331116
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