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Virchows Archiv

, Volume 443, Issue 1, pp 3–16 | Cite as

Amyloid in surgical pathology

  • Christoph Röcken
  • Knut Sletten
Review Article

Abstract

Amyloid is defined as a proteinaceous tissue deposit that shows a typical green birefringence in polarized light after staining with Congo red, the presence of non-branching linear fibrils of indefinite length with a mean diameter of 10 nm, and a distinct X-ray diffraction pattern consistent with Pauling's model of a cross β-fibril. Amyloid may deposit locally or may present as a systemic disease. The origin of amyloid is diverse: 25 different fibril proteins have been described so far. The precursor proteins differ from each other in their primary structures and functions. The only common denominator is the propensity to form anti-parallel cross β-fibrils under certain circumstances. Early diagnosis of amyloid is still a major challenge in surgical pathology. Histological proof can be obtained using Congo-red staining and polarization microscopy. However, small deposits may be difficult to discern, and sensitivity can be improved using fluorescence microscopy. Classification of amyloid is mandatory, since amyloid is treatable and different treatment regimens are applied to different amyloid diseases. This review focuses on the epidemiology, clinical features, pathology and diagnosis of amyloid in surgical pathology.

Keywords

Amyloid Surgical pathology 

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Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  1. 1.Department of PathologyOtto-von-Guericke-UniversityMagdeburgGermany
  2. 2.Biotechnology Center of OsloUniversity of OsloNorway

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