Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-02

AUTHORS

Robert Kisilevsky, Laura J. Lemieux, Paul E. Fraser, Xianqi Kong, Philip G. Hultin, Walter A. Szarek

ABSTRACT

Amyloid is a term for extracellular protein fibril deposits that have characteristic tinctorial and structural properties. Heparan sulphate, or the heparan sulphate proteoglycan perlecan, has been identified in all amyloids and implicated in the earliest stages of inflammation-associated (AA) amyloid induction. Heparan sulphate interacts with the AA amyloid precursor and the β-peptide of Alzheimer's amyloid, imparting characteristic secondary and tertiary amyloid structural features. These observations suggest that molecules that interfere with this interaction may prevent or arrest amyloidogenesis. We synthesized low-molecular-weight (135–1,000) anionic sulphonate or sulphate compounds. When administered orally, these compounds substantially reduced murine splenic AA amyloid progression. They also interfered with heparan sulphate-stimulated β-peptide fibril aggregation in vitro. More... »

PAGES

143-148

Journal

TITLE

Nature Medicine

ISSUE

2

VOLUME

1

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nm0295-143

    DOI

    http://dx.doi.org/10.1038/nm0295-143

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1052772818

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7585011


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