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Editorial
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Volume 356:2413-2415 June 7, 2007 Number 23
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Advances in the Treatment of Amyloidosis
S. Vincent Rajkumar, M.D., and Morie A. Gertz, M.D.

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by Dember, L. M.
-PubMed Citation
All forms of amyloidosis are characterized by the deposition of extracellular fibrils in various tissues. These fibrils are the result of the misfolding of a protein from its normal {alpha}-helical configuration into a β-pleated sheet. Amyloid fibrils are rigid, linear, and nonbranching and measure approximately 7.5 to 10 nm in width.1 The structure of the β-pleated sheet allows the binding of Congo red stain, which emits a characteristic apple-green birefringence under polarized light. The disease is often devastating, and options for treatment are limited.

There are distinct types of amyloidosis, which are classified according to the protein composition of the . . . [Full Text of this Article]


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From the Division of Hematology, Mayo Clinic College of Medicine, Rochester, MN.



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