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The metabolism of glycosaminoglycans is impaired in prion diseases

Academic Article
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Overview

authors

  • Mayer-Sonnenfeld, T.
  • Zeigler, M.
  • Halimi, M.
  • Dayan, Y.
  • Herzog, C.
  • Lasmezas, Corinne
  • Gabizon, R.

publication date

  • December 2005

journal

  • Neurobiology of Disease  Journal

abstract

  • It is well established that the conversion of PrP(C) to PrP(Sc) is the key event in prion disease biology. In addition, several lines of evidence suggest that glycosaminoglycans (GAGs) and in particular heparan sulfate (HS) may play a role in the PrP(C) to PrP(Sc) conversion process. It has been proposed that PrP(Sc) accumulation in prion diseases may induce aberrant activation of lysosomal activity, which has been shown to result in neurodegeneration in a number of diseases, especially lysosomal storage disorders. Among such diseases, only the ones resulting from defects in GAGs degradation are accompanied by secretion of large amounts of GAG metabolites in urine. In this work, we show that GAGs are secreted in the urine of prion-infected animals and humans, and surprisingly, also in the urine of mice ablated for the PrP gene. We hypothesize that both the presence of PrP(Sc) or the absence of PrP(C) may alter the metabolism of GAGs.

subject areas

  • Animals
  • Brain
  • Creutzfeldt-Jakob Syndrome
  • Cricetinae
  • Disease Models, Animal
  • Enzyme Activation
  • Glycosaminoglycans
  • Hexosaminidases
  • Humans
  • Lysosomes
  • Male
  • Mice
  • Mice, Knockout
  • Neurons
  • PrPC Proteins
  • PrPSc Proteins
  • Prion Diseases
  • Scrapie
  • Sheep
  • Up-Regulation
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Research

keywords

  • glycosaminoglycans
  • metabolism
  • prion diseases
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Identity

International Standard Serial Number (ISSN)

  • 0969-9961

Digital Object Identifier (DOI)

  • 10.1016/j.nbd.2005.05.009

PubMed ID

  • 15951190
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Additional Document Info

start page

  • 738

end page

  • 743

volume

  • 20

issue

  • 3

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