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Prion-induced amyloid heart disease with high blood infectivity in transgenic mice

Academic Article
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Overview

authors

  • Trifilo, M. J.
  • Yajima, T.
  • Gu, Y. S.
  • Dalton, N.
  • Peterson, K. L.
  • Race, R. E.
  • Meade-White, K.
  • Portis, J. L.
  • Masliah, E.
  • Knowlton, K. U.
  • Chesebro, B.
  • Oldstone, Michael

publication date

  • July 2006

journal

  • Science  Journal

abstract

  • We investigated extraneural manifestations in scrapie-infected transgenic mice expressing prion protein lacking the glycophosphatydylinositol membrane anchor. In the brain, blood, and heart, both abnormal protease-resistant prion protein (PrPres) and prion infectivity were readily detected by immunoblot and by inoculation into nontransgenic recipients. The titer of infectious scrapie in blood plasma exceeded 10(7) 50% infectious doses per milliliter. The hearts of these transgenic mice contained PrPres-positive amyloid deposits that led to myocardial stiffness and cardiac disease.

subject areas

  • Amyloid
  • Amyloidosis
  • Animals
  • Blotting, Western
  • Cardiac Catheterization
  • Coronary Vessels
  • Disease Models, Animal
  • Glycosylphosphatidylinositols
  • Heart Diseases
  • Heart Function Tests
  • Immunohistochemistry
  • Mice
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Microcirculation
  • Myocardial Contraction
  • Myocardium
  • PrPC Proteins
  • PrPSc Proteins
  • Scrapie
  • Staining and Labeling
  • Time Factors
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Identity

PubMed Central ID

  • PMC1820586

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1128635

PubMed ID

  • 16825571
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Additional Document Info

start page

  • 94

end page

  • 97

volume

  • 313

issue

  • 5783

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