Journal
ACTA NEUROPATHOLOGICA
Volume 118, Issue 1, Pages 115-130Publisher
SPRINGER
DOI: 10.1007/s00401-009-0501-8
Keywords
Central nervous system; Cerebral amyloid angiopathy; Amyloid proteins; Amyloid-beta; ABri; ADan; Cystatin C; Transthyretin; Prion protein; Gelsolin; Genetics; Biochemistry; Pathogenesis
Categories
Funding
- NIA NIH HHS [P01 AG010491, AG10491, P01 AG010491-130005] Funding Source: Medline
- NINDS NIH HHS [R01 NS051715, NS051715, R01 NS051715-03] Funding Source: Medline
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In cerebral amyloid angiopathy (CAA), amyloid fibrils deposit in walls of arteries, arterioles and less frequently in veins and capillaries of the central nervous system, often resulting in secondary degenerative vascular changes. Although the amyloid-beta peptide is by far the commonest amyloid subunit implicated in sporadic and rarely in hereditary forms of CAA, a number of other proteins may also be involved in rare familial diseases in which CAA is also a characteristic morphological feature. These latter proteins include the ABri and ADan subunits in familial British dementia and familial Danish dementia, respectively, which are also known under the umbrella term BRI2 gene-related dementias, variant cystatin C in hereditary cerebral haemorrhage with amyloidosis of Icelandic-type, variant transthyretins in meningo-vascular amyloidosis, disease-associated prion protein (PrPSc) in hereditary prion disease with premature stop codon mutations and mutated gelsolin (AGel) in familial amyloidosis of Finnish type. In this review, the characteristic morphological features of the different CAAs is described and the implication of the biochemical, genetic and transgenic animal data for the pathogenesis of CAA is discussed.
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