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Amyloidosis
Author(s) -
TAN S.Y.,
PEPYS M.B.
Publication year - 1994
Publication title -
histopathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.626
H-Index - 124
eISSN - 1365-2559
pISSN - 0309-0167
DOI - 10.1111/j.1365-2559.1994.tb00001.x
Subject(s) - amyloidosis , amyloid (mycology) , beta 2 microglobulin , thioflavin , pathology , islet , aa amyloidosis , medicine , fibril , chemistry , alzheimer's disease , biochemistry , immunology , endocrinology , disease , diabetes mellitus , familial mediterranean fever
Amyloidosis is a heterogeneous group of disorders characterized by extracellular deposition of abnormal protein fibrils which are dérived from different proteins in different forms of the disease. Asymptomatic amyloid deposition in a variety of tissues is a universal accompaniment of ageing, and clinical amyloidosis is not rare. Intracerebral and cerebrovascular β‐protein amyloid deposits are a hallmark of the pathology of both sporadic and familial Alzheimer's disease, β 2 ‐microglobulin‐derived amyloid is a common complication of long term haemodialysis, and islet amyloid polypeptide is the fibril protein in the universal islet amyloidosis of type II diabetes mellitus. New fibril proteins have lately been identified in hereditary amyloidosis, including variants of gelsolin, apolipoprotein AI, lysozyme and fibrinogen. The development of radiolabelled serum amyloid P component (SAP) scintigraphy has allowed amyloid to be diagnosed non‐invasively in vivo for the first time, provided unique insight into the distribution and size of amyloid deposits, and yielded novel information on the natural history and the effects of treatment. Amyloid deposits are in a state of dynamic turnover and can regress if new fibril formation is halted. The recent elucidation of the three dimensional structure of human SAP may enable the design of specific therapeutic agents.