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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.

Keywords

Light Chain Familial Mediterranean Fever Amyloid Deposit Amyloid Fibril Fibril Formation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. Biewend ML, Menke DM, Calamia KT. The spectrum of localized amyloidosis: a case series of 20 patients and review of the literature. Amyloid 2006;13:135–42PubMedCrossRefGoogle Scholar
  2. Caughey B, Baron GS. Prions and their partners in crime. Nature 2006;443:803–10PubMedCrossRefGoogle Scholar
  3. Cohen FE, Kelly JW. Therapeutic approaches to protein-misfolding diseases. Nature 2003;426:905–9PubMedCrossRefGoogle Scholar
  4. Connors LH, Lim A, Prokaeva T, Roskens VA, Costello CE. Tabulation of human transthyretin (TTR) variants, 2003. Amyloid 2003;10: 160–84PubMedCrossRefGoogle Scholar
  5. Cunnane G, Whitehead AS. Amyloid precursors and amyloidosis in rheumatoid arthritis. Baill Clin Rheumatol. 1999;13(4):615–28Google Scholar
  6. Dobson CM. Protein folding and misfolding. Nature 2003;426:884–90PubMedCrossRefGoogle Scholar
  7. 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;32:82–5PubMedCrossRefGoogle Scholar
  8. Falk HR. Diagnosis and management of the cardiac amyloidoses. Circulation 2005;112:2047–60PubMedCrossRefGoogle Scholar
  9. 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;346:564–9PubMedCrossRefGoogle Scholar
  10. 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;111:355–62PubMedGoogle Scholar
  11. Rocken C, Sletten K. Amyloid in surgical pathology. Virchows Archiv. 2003;443:3–16PubMedCrossRefGoogle Scholar
  12. 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;29:113–9PubMedCrossRefGoogle Scholar
  13. Selkoe DJ. Aging, amyloid, and Alzheimer's disease. N Engl J Med. 1989;320(22):1484–7PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  • George H. SackJr
    • 1
  1. 1.Johns Hopkins University School of MedicineMedicine and Biological ChemistryBaltimoreUSA

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