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Overview of amyloidosis

Peter D Gorevic, MD
Section Editor
Peter H Schur, MD
Deputy Editor
Paul L Romain, MD


Amyloidosis is the general term used to refer to the extracellular tissue deposition of fibrils composed of low molecular weight subunits of a variety of proteins, many of which circulate as constituents of plasma. These deposits may result in a wide range of clinical manifestations depending upon their type, location, and the amount of deposition.

The subunit proteins forming amyloid deposits are derived from soluble precursors which have undergone conformational changes that lead to the adoption of a predominantly antiparallel beta-pleated sheet configuration. Multiple different human protein precursors of amyloid fibrils are known. Amyloid has a characteristic gross pathologic and microscopic appearance, demonstrating apple-green birefringence with polarized light microscopy of Congo red stained tissue. (See 'Pathology' below.)

A general overview of the pathogenesis, clinical manifestations, diagnosis, and treatment of the different amyloid disorders is presented here. The role of genetic factors in amyloidosis is discussed in detail elsewhere (see "Genetic factors in the amyloid diseases" and "Genetics of Alzheimer disease"). More detailed discussions of the individual disorders are also presented separately. (See appropriate topic reviews as indicated in the relevant sections below).


It was Rudolph Virchow in 1854 who adopted the term "amyloid," first introduced by Schleiden in 1838 to describe plant starch, to refer to tissue deposits of material that stained in a similar manner to cellulose when exposed to iodine [1]. In these original descriptions, amyloid deposits were noted by Rokitansky to have a "waxy" or "lardaceous" appearance grossly and by Virchow to be amorphous and hyaline on light microscopy. Congo red is a direct cotton dye and pH indicator that was developed by Paul Bottinger in 1883; it was later shown to confer typical apple-green birefringence with polarized microscopy, introduced in the 1920s by Bennhold for the better demonstration of amyloid. The use of thioflavine T, producing an intense yellow-green fluorescence, was popularized in the 1950s (picture 1A-D) [1]. Virchow recorded the prescient observation in his Cellular Pathology (1858) that "I am as yet much more inclined to admit, that the blood in this disease undergoes a chemical alteration in its fluid constituents, than that it contains the pathological substances in a material form."

Electron microscopic examination of amyloid deposits, first performed in 1959, generally demonstrates straight and unbranching fibrils 8 to 10 nm in width, which may be composed of protofilaments at higher resolution [2,3]. Transmission electron and atomic force microscopy have had a role in elucidating the three dimensional structure of these macromolecular aggregates and in defining folding intermediates, including small oligomers and amorphous aggregates [4]. In many instances, the type of amyloid fibril unit can be further defined by immunohistology (immunofluorescence or immunoenzymatic techniques) or by immunoelectron microscopy [5,6].

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Literature review current through: Oct 2017. | This topic last updated: Aug 29, 2017.
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