Cellular and Molecular Life Sciences

, Volume 67, Issue 4, pp 581–600

Cerebral amyloidosis: amyloid subunits, mutants and phenotypes

  • A. Rostagno
  • J. L. Holton
  • T. Lashley
  • T. Revesz
  • Jorge Ghiso
Review

DOI: 10.1007/s00018-009-0182-4

Cite this article as:
Rostagno, A., Holton, J.L., Lashley, T. et al. Cell. Mol. Life Sci. (2010) 67: 581. doi:10.1007/s00018-009-0182-4

Abstract

Cerebral amyloid diseases are part of a complex group of chronic and progressive entities bracketed together under the common denomination of protein folding disorders and characterized by the intra- and extracellular accumulation of fibrillar aggregates. Of the more than 25 unrelated proteins known to produce amyloidosis in humans only about a third of them are associated with cerebral deposits translating in cognitive deficits, dementia, stroke, cerebellar and extrapyramidal signs, or a combination thereof. The familial forms reviewed herein, although infrequent, provide unique paradigms to examine the role of amyloid in the mechanism of disease pathogenesis and to dissect the link between vascular and parenchymal amyloid deposition and their differential contribution to neurodegeneration.

Keywords

Amyloid proteinsCerebral amyloid angiopathyAmyloid plaquesProtein folding disorders

Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009

Authors and Affiliations

  • A. Rostagno
    • 1
  • J. L. Holton
    • 3
  • T. Lashley
    • 3
  • T. Revesz
    • 3
  • Jorge Ghiso
    • 1
    • 2
  1. 1.Department of PathologyNew York University School of MedicineNew YorkUSA
  2. 2.Department of PsychiatryNew York University School of MedicineNew YorkUSA
  3. 3.Department of Molecular Neuroscience, UCL Institute of Neurology, Queen Square Brain Bank for Neurological DisordersUniversity College LondonLondonUK