A primer of amyloid nomenclature

Abstract

The increasing knowledge of the exact biochemical nature of the localized and systemic amyloid disorders has made a logical and easily understood nomenclature absolutely necessary. Such a nomenclature, biochemically based, has been used for several years but the current literature is still mixed up with many clinical and histochemically based designations from the time when amyloid in general was poorly understood. All amyloid types are today preferably named by their major fibril protein. This makes a simple and rational nomenclature for the increasing number of amyloid disorders known in humans and animals.

Localized Tongue Amyloidosis in a Patient with Neurofibromatosis Type II

“…On microscopic examination of the excised lesion, detection of eosinophilic amorphous material positive for Congo-Red in association with the clinical and laboratory analysis confirmed the diagnosis of localized amyloidosis without systemic involvement. Amyloidosis represents a rare heterogenous group of conditions characterized by extracellular proteinaceous depositions of amyloid which may cause organ abnormalities [3,8]. The mechanism, of amyloid formation, includes amyloid (pro)precursor genes activation, under the influence of cytokines, clonal plasma cells, abnormal proteolysis and the production of several precursor pools of different amyloidogenic molecules, which in turn form fibrils of amyloid after their enrichment with proteoglycans, glycosaminoglycans, inorganic ions and serum amyloid P [3,21,22].…”

“…This disease can be acquired or hereditary, limited in a tissue/ organ with benign prognosis (localized form) or may affect multiple tissues/organs (kidneys, heart, liver, gastrointestinal tract, bladder etc.) leading to significant morbidity and at times mortality (systemic form) [2][3][4].…”

Ultrasonication: An Efficient Agitation for Accelerating the Supersaturation-Limited Amyloid Fibrillation of Proteins

“…5) Amyloid fibrillation (i.e., formation of amyloid fibrils) is thought to be a result of protein misfolding because their deposition is associated with the pathology of more than twenty serious disorders such as Alzheimer's disease, Parkinson's disease, type II diabetes, and dialysis-related amyloidosis. 6,7) On the other hand, amyloid-like structures are also utilized for beneficial purposes in nature, and are known as functional amyloids. [8][9][10] Because many structurally unrelated proteins can form amyloid fibrils, amyloid misfolding is considered a general property of polypeptide chains.…”

Mass spectrometry and the amyloid problem—How far can we go in the gas phase?

“…In fact, amyloid deposits are composed of protein fibrils and in principle there is one type of protein in each case of amyloidosis [3]. There are Ͼ20 such (quite different) proteins that undergo amyloidosis in humans in vivo and which are associated with a variety of diseases, including Alzheimer's, Parkinson's, Huntington's, hemodialysis-related amyloidosis, and the spongiform encephalopathies (Table 1) [4].…”