Abstract
The diagnosis of amyloidosis depends on finding deposits with congo red birefringence in affected tis-sue.These deposits comprise fibrils of highly ordered proteins or protein fragments that generally contain prominent ²-pleated sheet domains. Many proteins have regions that can aggregate into amyloid fibrils.Often only a small fragment of a larger molecule is compatible with fibril geometry and thus fibril formation occurs after cleaving the parent protein. Amyloid deposits can be found in any tissue.However, some depostis have no pathologic consequence while others can cause serious organ dysfunction by interrupting individual cellular physiology, cell-cell interactions and/or tissue integrity. When specific organ dysfunction has been identified, biopsy of that tissue often is the simplest diagnostic method(e.g.heart,kidney,liver). An alternative diagnostic approach for systermic amyloidosis is to examine tissue derived by aspiration of the abdominal fat pad. Both prognosis and treatment are based on identifying the protein in the fibril.Often, this protein can be iden-tified by immunofluorescence. Amyloid proteins vary widely and include immuno-globulins,inflammatory molecules, hormone precursors and inherited variants of normal serum proteins. Inherited forms of amyloidosis are uncommon but well-recognized. They often involve specific organs– e.g. heart,peripheral nerves,or blood vessels. Most have autosomal dominant inheritance.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Biewend ML, Menke DM, Calamia KT. The spectrum of localized amyloidosis: a case series of 20 patients and review of the literature. Amyloid 2006;13:135–42
Caughey B, Baron GS. Prions and their partners in crime. Nature 2006;443:803–10
Cohen FE, Kelly JW. Therapeutic approaches to protein-misfolding diseases. Nature 2003;426:905–9
Connors LH, Lim A, Prokaeva T, Roskens VA, Costello CE. Tabulation of human transthyretin (TTR) variants, 2003. Amyloid 2003;10: 160–84
Cunnane G, Whitehead AS. Amyloid precursors and amyloidosis in rheumatoid arthritis. Baill Clin Rheumatol. 1999;13(4):615–28
Dobson CM. Protein folding and misfolding. Nature 2003;426:884–90
Duston MA, Skinner M, Meenan RF, Cohen AS. Sensitivity, specificity, and predictive value of abdominal fat aspiration for the diagnosis of amyloidosis. Arthritis Rheum. 1989;32:82–5
Falk HR. Diagnosis and management of the cardiac amyloidoses. Circulation 2005;112:2047–60
Kyle RA, Therneau TM, Rajkumar V, et al A long-term study of prog nosis in monoclonal gammopathy of undetermined significance. N Engl J Med. 2002;346:564–9
Olsen KE, Sletten K, Westermark P. The use of subcutaneous fat tissue for amyloid typing by enzyme-linked immunosorbent assay. Am J Clin Pathol. 1999;111:355–62
Rocken C, Sletten K. Amyloid in surgical pathology. Virchows Archiv. 2003;443:3–16
Sack GH Jr, Talbot CC Jr, Seuanez H, O'Brien SJ. Molecular analysis of the human serum amyloid A (SAA) gene family. Scand J Immunol. 1989;29:113–9
Selkoe DJ. Aging, amyloid, and Alzheimer's disease. N Engl J Med. 1989;320(22):1484–7
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer Science+Business Media B.V.
About this chapter
Cite this chapter
Sack, G.H. (2009). Amyloidosis. In: Stone, J.H. (eds) A Clinician's Pearls and Myths in Rheumatology. Springer, London. https://doi.org/10.1007/978-1-84800-934-9_46
Download citation
DOI: https://doi.org/10.1007/978-1-84800-934-9_46
Publisher Name: Springer, London
Print ISBN: 978-1-84800-933-2
Online ISBN: 978-1-84800-934-9
eBook Packages: MedicineMedicine (R0)