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Publication Detail
Amyloid persistence in decellularized liver: biochemical and histopathological characterization
  • Publication Type:
    Journal article
  • Authors:
    Mazza G, Simons JP, Al-Shawi R, Ellmerich S, Urbani L, Giorgetti S, Taylor GW, Gilbertson JA, Hall AR, Al-Akkad W, Dhar D, Hawkins PN, De Coppi P, Pinzani M, Bellotti V, Mangione PP
  • Publication date:
  • Pagination:
    1, 7
  • Journal:
  • Volume:
  • Issue:
  • Status:
  • Print ISSN:
  • Keywords:
    AA amyloidosis, AEF, amyloid, decellularized liver, scaffold
  • Notes:
    © 2015 The Authors. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Systemic amyloidoses are a group of debilitating and often fatal diseases in which fibrillar protein aggregates are deposited in the extracellular spaces of a range of tissues. The molecular basis of amyloid formation and tissue localization is still unclear. Although it is likely that the extracellular matrix (ECM) plays an important role in amyloid deposition, this interaction is largely unexplored, mostly because current analytical approaches may alter the delicate and complicated three-dimensional architecture of both ECM and amyloid. We describe here a decellularization procedure for the amyloidotic mouse liver which allows high-resolution visualization of the interactions between amyloid and the constitutive fibers of the extracellular matrix. The primary structure of the fibrillar proteins remains intact and the amyloid fibrils retain their amyloid enhancing factor activity.
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