The amyloidoses are a group of β‐structure protein deposition diseases that may be systemic or localised, sporadic, hereditary or associated with chronic inflammation. Many serum proteins are capable of forming β‐structure and participate in the formation of 10 nm fibrils which are the hallmark of amyloid deposits. These proteins include immunoglobulin light chains, several proteins synthesised mainly by the liver (serum amyloid A, fibrinogen, apolipoproteins AI and AII, leukocyte chemotaxin factor‐2) plus lysozyme, cystatin‐C, gelsolin and probably others not yet identified. Pathology is the result of displacement of normal tissue structures. The systemic forms of amyloidosis may cause the nephrotic syndrome and renal failure, cardiac arrhythmias and heart failure, hepatic failure and bowel dysfunction in varying combinations and degrees of severity.

Key Concepts

  • Amyloidosis is a generic term to designate any biologic condition where protein fibrils measure 8–12 nm and aggregate to form deposits in extracellular space of most body organs.
  • Many proteins have the potential to form amyloid fibrils. Some have extensive β‐structure, a prerequisite for fibril formation, while others may acquire β‐structure during catabolism (metabolic processes).
  • Some normal proteins have properties to form amyloid fibrils. Alzheimer β‐protein and transthyretin have this capacity.
  • Mutation either inherited or acquired in some proteins can accelerate the path to amyloid fibril formation.
  • Treatment of amyloidosis may target reduction of the amount of precursor protein available for fibril formation or alteration of metabolic processes intrinsic to the generation of amyloid fibrils.

Keywords: amyloid; amyloidosis; protein deposition diseases

Figure 1. Histological sections of an endomyocardial biopsy from a patient with amyloid cardiomyopathy. (a) Amyloid deposits are eosinophilic and disrupt normal myocardial fibres (haematoxylin and eosin). (b) Amyloid deposits have an affinity for Congo red. (c) Same section as in (b) in polarised light showing green birefringence characteristic of Congo red‐stained amyloid fibril deposits.
Figure 2. Computer graphic model of a κI amyloid light chain variable region protein (VL) based on X‐ray crystallographic diffraction data of VL protein produced by recombinant DNA technology. This model has eight β‐strands in two planes with extensive hydrogen bonding (Schormann et al., ).
Figure 3. Computer graphic model of transthyretin tetramer. Thyroxine binds in the central channel and vitamin A–RBP binds on the surface of the tetramer. Each monomer has extensive β‐sheet structure.


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Benson MD, James S, Scott K, Liepnieks JJ, et al. (2008) Leukocyte chemotactic factor 2: a novel renal amyloid protein. Kidney International 74: 218–222.

Benson MD and Kincaid JC (2007) Invited review: the molecular biology and clinical features of amyloid neuropathy. Muscle & Nerve 36: 411–423.

Benson MD, Liepnieks JJ and Kluve‐Beckerman B (2015) Hereditary systemic immunoglobulin light‐chain amyloidosis. Blood First Edition online.

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Schormann N, Murrell JR, Liepnieks JJ and Benson MD (1995) Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America 92: 9490–9494.

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Sipe JD, Benson MD, Buxbaum JN, et al. (2014) Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis. Amyloid 21: 221–224.

Westermark P, Benson MD, Buxbaum JN, et al. (2007) A primer of amyloid nomenclature. Amyloid 14: 179–183.

Further Reading

Benson MD (2001) Amyloidosis. In: Scriver CR, Beaudet AL, Sly WS and Valle D, (eds). The Metabolic and Molecular Bases of Inherited Disease, 8th, part 22, Connective Tissues edn. Vol. IV, chap. 209, pp. 5345–5378. New York: McGraw‐Hill.

Benson MD (2005) Amyloidosis. In: Koopman WJ and Moreland LW, (eds). Arthritis and Allied Conditions: A Textbook of Rheumatology, 15th edn. Vol. 2, chap. 93, pp. 1933–1960. Philadelphia: Williams & Wilkins, A Waverly Company.

Benson MD (2010) LECT2 amyloidosis (invited editorial commentary). Kidney International 77: 757–759.

Benson MD (2013) Amyloidosis and other protein deposition diseases. In: Rimoin DL, Connor JM, Pyeritz RE and Korf BR, (eds). Emery and Rimoin's Principles and Practice of MEDICAL GENETICS – electronic chapter (update), 6th, chap. 79 edn, pp. 2144–2161. Philadelphia, PA: Churchill Livingstone publishers.

Benson MD and Uemichi T (1996) Review: transthyretin amyloidosis. Amyloid. International Journal of Experimental and Clinical Investigation 3: 44–56.

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Benson, Merrill D(Jun 2015) Amyloidosis. In: eLS. John Wiley & Sons Ltd, Chichester. [doi: 10.1002/9780470015902.a0002146.pub3]