Accumulation of heparan sulfate proteoglycans in cerebellar senile plaques

Horssen, Jack van; Kleinnijenhuis, Johanneke; Maass, Cathy; Rensink, Annemieke A.M.; Otte-Höller, Irene; Gourichon, David; Heuvel, L.P.W.J. van den; Wesseling, Pieter; Waal, R.M.W. de; Verbeek, Marcel M.

doi:10.1016/s0197-4580(02)00010-6

Cited by 63 publications

(35 citation statements)

References 37 publications

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“…In addition, endothelial cells in fetal lung tissue, but not adult lung tissue, express syndecan-4 (59). Syndecan-3 is the predominant syndecan in the nervous system, where it was first identified, and has been associated with the generation of cerebellar fibrillar plaques in Alzheimer's disease (60,61). Interestingly, it is also an HSPG in the musculoskeletal system.…”

Section: Discussionmentioning

confidence: 99%

Induction of a CXCL8 binding site on endothelial syndecan‐3 in rheumatoid synovium

Patterson

Gardner

Shaw

et al. 2005

Arthritis & Rheumatism

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Section: Discussionmentioning

confidence: 99%

Induction of a CXCL8 binding site on endothelial syndecan‐3 in rheumatoid synovium

Patterson

Gardner

Shaw

et al. 2005

Arthritis & Rheumatism

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“…Lower Parenchymal and Cerebrovascular Amyloid Burden in Double-transgenic Mice-HS and HSPGs preferentially colocalize with the amyloid core of mature plaques, a small region at the center of most A␤ deposits in both the AD brain and A␤PP transgenic models (3)(4)(5)(6)(7). To further characterize the A␤ plaques, we stained adjacent sections of the mouse brains with Congo red fluorescent dye, which detects only the amyloid core of mature plaques.…”

Section: A-c)mentioning

confidence: 99%

“…However, the functional role of HS in AD pathogenesis is not yet fully resolved (1,2). HS and HS proteoglycans (HSPGs) colocalize particularly with mature A␤ deposits in the AD brain and animal models thereof (3)(4)(5)(6)(7). The conformation and fibrillar state of A␤ influences its molecular interaction with the HS-like molecule heparin (8), a highly sulfated glycosaminoglycan that is commonly used in vitro as a model for HS.…”

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confidence: 99%

Overexpression of Heparanase Lowers the Amyloid Burden in Amyloid-β Precursor Protein Transgenic Mice

Jendresen

Cui

Zhang

et al. 2015

Journal of Biological Chemistry

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Background: Heparan sulfate colocalizes with amyloid-␤ in senile plaques of Alzheimer disease. Results: Overexpression of the heparan sulfate-degrading enzyme (heparanase) lowers the amyloid burden in a transgenic mouse model of Alzheimer disease. Conclusion: Heparan sulfate modulates amyloid-␤ deposition. Significance: We present the first direct in vivo proof that heparan sulfate actively participates in senile plaque formation.

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“…The HS chains associated with amyloid deposits could be derived from Gpc-1 as this PG is abundantly expressed in cerebral amyloid angiopathy associated with Alzheimer's disease and other forms of cerebral amyloidosis (5,55). HS chains and hyperphosphorylated tau protein have been found to coexist in nerve cells at early stages of Alzheimer's disease (56).…”

Section: Figmentioning

confidence: 99%

Prion, Amyloid β-derived Cu(II) Ions, or Free Zn(II) Ions Support S-Nitroso-dependent Autocleavage of Glypican-1 Heparan Sulfate

Mani

Cheng

Havsmark

et al. 2003

Journal of Biological Chemistry

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Copper are generally bound to proteins, e.g. the prion and the amyloid ␤ proteins. We have previously shown that copper ions are required to nitrosylate thiol groups in the core protein of glypican-1, a heparan sulfate-substituted proteoglycan. When S-nitrosylated glypican-1 is then exposed to an appropriate reducing agent, such as ascorbate, nitric oxide is released and autocatalyzes deaminative cleavage of the glypican-1 heparan sulfate side chains at sites where the glucosamines are N-unsubstituted. These processes take place in a stepwise manner, whereas glypican-1 recycles via a caveolin-1-associated pathway where copper ions could be provided by the prion protein. Here we show, by using both biochemical and microscopic techniques, that (a) the glypican-1 core protein binds copper(II) ions, reduces them to copper(I) when the thiols are nitrosylated and reoxidizes copper(I) to copper(II) when ascorbate releases nitric oxide; (b) maximally S-nitrosylated glypican-1 can cleave its own heparan sulfate chains at all available sites in a nitroxyl ion-dependent reaction; (c) free zinc(II) ions, which are redox inert, also support autocleavage of glypican-1 heparan sulfate, probably via transnitrosation, whereas they inhibit copper(II)-supported degradation; and (d) copper(II)-loaded but not zinc(II)-loaded prion protein or amyloid ␤ peptide support heparan sulfate degradation. As glypican-1 in prion null cells is poorly S-nitrosylated and as ectopic expression of cellular prion protein restores S-nitrosylation of glypican-1 in these cells, we propose that one function of the cellular prion protein is to deliver copper(II) for the S-nitrosylation of recycling glypican-1.

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Accumulation of heparan sulfate proteoglycans in cerebellar senile plaques

Cited by 63 publications

References 37 publications

Induction of a CXCL8 binding site on endothelial syndecan‐3 in rheumatoid synovium

Induction of a CXCL8 binding site on endothelial syndecan‐3 in rheumatoid synovium

Overexpression of Heparanase Lowers the Amyloid Burden in Amyloid-β Precursor Protein Transgenic Mice

Prion, Amyloid β-derived Cu(II) Ions, or Free Zn(II) Ions Support S-Nitroso-dependent Autocleavage of Glypican-1 Heparan Sulfate

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