Amyloidosis

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Related to amyloid disease: amyloidosis, Prion diseases

amyloidosis

[‚am·ə·loi′dō·səs]
(medicine)
Deposition of amyloid in one or more organs of the body.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

Amyloidosis

 

or amyloid dystrophy, a disorder of protein metabolism accompanied by the formation within tissues of a specific protein polysaccharide complex known as amyloid. The progress of the disease is associated with distortion of the protein-synthesizing function of the reticuloendothelial system and with accumulation of anomalous proteins in the blood plasma which act as autoantigens and also stimulate the formation of autoantibodies. As a result of antigen-antibody interaction, there is deposition of widely dispersed proteins which figure in the formation of amyloid. Once deposited in tissues, such as vascular and gland walls, the amyloid displaces functionally specialized elements of the organ; this process leads to the destruction of the organ.

Several types of amyloidosis are recognized: primary, secondary, and senile amyloidosis; amyloidosis with multiple myeloma; and localized tumorlike amyloidosis. Primary amyloidosis has no connection with any other disease; it affects mainly the cardiovascular system, alimentary tract, muscles, and skin. Secondary amyloidosis develops subsequent to other diseases which are accompanied by prolonged suppuration and tissue breakdown, such as tuberculosis, syphilis, and rheumatoid arthritis. It most often affects the spleen, liver, kidneys, adrenal glands, and intestines. Senile amyloidosis usually involves the heart. Amyloidosis may be either general or localized. Im-munodepressive and hepatic preparations are used in its treatment.

V. V. SEROV

The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.
References in periodicals archive ?
Both mature fibril and nonfibrillar oligomers have been hypothesized to be the possible pathogenic agents in amyloid diseases [3].
Giorgetti et al., "The workings of the amyloid diseases," Annals of Medicine, vol.
The topics include insights from crystallography into amyloid structures at the atomic level, structural and compositional information about pre-amyloid oligomers, the kinetics and mechanisms of amyloid formation, animal models of amyloid diseases, hormone anyloids in sickness and in health, and harnessing the self-assembling properties of proteins in spider silk and lung surfactant.
The introduction of the inhibitor into a tau protein solution completely prevented amyloid fibre formation, validating the idea that the structure-based design of therapeutics for amyloid diseases is a plausible option.