uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
AA Amyloidosis: Pathogenesis and Targeted Therapy
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Molecular and Morphological Pathology.
2015 (English)In: Annual Review Of Pathology: Mechanisms Of Disease, Vol 10, ANNUAL REVIEWS, 2015, Vol. 10, 321-344 p.Chapter in book (Refereed)
Abstract [en]

The understanding of why and how proteins misfold and aggregate into amyloid fibrils has increased considerably during recent years. Central to amyloid formation is an increase in the frequency of the beta-sheet structure, leading to hydrogen bonding between misfolded monomers and creating a fibril that is comparably resistant to degradation. Generation of amyloid fibrils is nucleation dependent, and once formed, fibrils recruit and catalyze the conversion of native molecules. In AA amyloidosis, the expression of cytokines, particularly interleukin 6, leads to overproduction of serum amyloid A (SAA) by the liver. A chronically high plasma concentration of SAA results in the aggregation of amyloid into cross-beta-sheet fibrillar deposits by mechanisms not fully understood. Therefore, AA amyloidosis can be thought of as a consequence of long-standing inflammatory disease. This review summarizes current knowledge about AA amyloidosis. The systemic amyloidoses have been regarded as intractable conditions, but improvements in the understanding of fibril composition and pathogenesis over the past decade have led to the development of a number of different therapeutic approaches with promising results.

Place, publisher, year, edition, pages
ANNUAL REVIEWS, 2015. Vol. 10, 321-344 p.
, Annual Review of Pathology-Mechanisms of Disease, ISSN 1553-4006 ; 10
Keyword [en]
acute phase, fibril, rheumatoid arthritis, serum amyloid A, strains, toxic oligomer
National Category
Other Medical Sciences not elsewhere specified
URN: urn:nbn:se:uu:diva-247615DOI: 10.1146/annurev-pathol-020712-163913ISI: 000348560600011PubMedID: 25387054ISBN: 978-0-8243-4310-1OAI: oai:DiVA.org:uu-247615DiVA: diva2:797222
Available from: 2015-03-23 Created: 2015-03-22 Last updated: 2015-03-23Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Westermark, Gunilla T.Westermark, Per
By organisation
Department of Medical Cell BiologyMolecular and Morphological Pathology
Other Medical Sciences not elsewhere specified

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 408 hits
ReferencesLink to record
Permanent link

Direct link