Abstract
The amyloid diseases involve a wide variety of proteins that share in common the property of forming fibrils (1). Deposition and accumulation of these fibrils in various tissues, ultimately interfering with normal organ function, results in the clinical entity known as amyloidosis. The amyloidoses can occur either as isolated localized processes or as systemic disorders involving multiple organ systems. Furthermore, amyloidosis may occur as a primary disease process or as a secondary consequence of other diseases. Both light and heavy chain (formerly known as primary) amyloidosis and familial amyloidosis belong to the former group, whereas serum amyloid A protein and beta2-microglobulin (dialysis-associated) amyloidosis belong to the latter group. In the United States, primary (idiopathic) amyloidosis is the most common form of amyloid disease, while serum amyloid A-associated amyloidosis occurs more commonly in other countries. Alzheimer’s disease and prion deposition disease are the only forms of localized amyloid fibril deposition which often lead to serious illness; other forms of localized amyloid deposition usually lead only to mechanical interference and generally are considered to be benign.
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Sarraf, P., Kay, J. (2008). The Amyloidoses. In: Klippel, J.H., Stone, J.H., Crofford, L.J., White, P.H. (eds) Primer on the Rheumatic Diseases. Springer, New York, NY. https://doi.org/10.1007/978-0-387-68566-3_29
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DOI: https://doi.org/10.1007/978-0-387-68566-3_29
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