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Amyloid Nomenclature 2020: Update and Recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee

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Amyloid Nomenclature 2020: Update and Recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee Amyloid The Journal of Protein Folding Disorders ISSN: (Print) (Online) Journal homepage: https://www.tandfonline.com/loi/iamy20 Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee Merrill D. Benson , Joel N. Buxbaum , David S. Eisenberg , Giampaolo Merlini , Maria J. M. Saraiva , Yoshiki Sekijima , Jean D. Sipe & Per Westermark To cite this article: Merrill D. Benson , Joel N. Buxbaum , David S. Eisenberg , Giampaolo Merlini , Maria J. M. Saraiva , Yoshiki Sekijima , Jean D. Sipe & Per Westermark (2020) Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee, Amyloid, 27:4, 217-222, DOI: 10.1080/13506129.2020.1835263 To link to this article: https://doi.org/10.1080/13506129.2020.1835263 © 2020 The Author(s). Published by Informa Published online: 26 Oct 2020. UK Limited, trading as Taylor & Francis Group. Submit your article to this journal Article views: 1958 View related articles View Crossmark data Citing articles: 6 View citing articles Full Terms & Conditions of access and use can be found at https://www.tandfonline.com/action/journalInformation?journalCode=iamy20 AMYLOID 2020, VOL. 27, NO. 4, 217–222 https://doi.org/10.1080/13506129.2020.1835263 NOMENCLATURE ARTICLE Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee Merrill D. Bensona, Joel N. Buxbaumb, David S. Eisenbergc, Giampaolo Merlinid, Maria J. M. Saraivae, Yoshiki Sekijimaf, Jean D. Sipeg and Per Westermarkh aDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA; bDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, USA; cDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA; dAmyloid Research and Treatment Center, Foundation IRCCS Policlinico San Matteo, and University of Pavia, Pavia, Italy; eInstitute of Molecular and Cellular Biology, University of Porto, Molecular Neurobiology, Porto, Portugal; fDepartment of Medicine (Neurology and Rheumatology), Shinshu University School of Medicine, Matsumoto, Japan; gDepartment of Biochemistry (Retired), Boston University School of Medicine, Boston, MA, USA; hDepartment of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden ABSTRACT The ISA Nomenclature Committee met electronically before and directly after the XVII ISA International Symposium on Amyloidosis, which, unfortunately, had to be virtual in September 2020 due to the ongoing COVID-19 pandemic instead of a planned meeting in Tarragona in March. In addition to con- KEYWORDS firmation of basic nomenclature, several additional concepts were discussed, which are used in scien- Amyloid; fibril protein; nomenclature; aggegation; tific amyloid literature. Among such concepts are cytotoxic oligomers, protofibrils, primary and oligomer; inclusion secondary nucleation, seeding and cross-seeding, amyloid signature proteins, and amyloid plaques. Recommendations for their use are given. Definitions of amyloid and amyloidosis are confirmed. Possible novel human amyloid fibril proteins, appearing as ‘classical’ in vivo amyloid, were discussed. It was decided to include fibulin-like extracellular matrix protein 1 (amyloid protein: AEFEMP1), which appears as localised amyloid in portal veins. There are several possible amyloid proteins under investi- gation, and these are included in a new Table. Introduction extracellular substance that varied highly in distribution and properties and, if any, in clinical manifestations. This het- The Amyloidosis Nomenclature Committee of the International Society of Amyloidosis meets in association erogeneity led to several early classifications, the most well- with the International Symposia of Amyloidosis. These sym- known probably that of Reimann et al. [1] dividing the dis- posia initially appeared irregularly but are now organised eases in 1. Primary, 2. Secondary, 3. Tumour-forming, and every second year. This year, 2020, was an exception due to 4. Myeloma-associated amyloidosis. This classification has the COVID-19 pandemic which caused the symposium to had a very long survival but is with our increasing know- be postponed then converted to a virtual electronic format. ledge outdated and should not be used. Thus, Nomenclature meetings were held in spring and sum- Modern research on amyloid started with the demonstra- mer 2020 either by e-mail or via Zoom directly after the tion of a sub-microscopic fibrillary structure of a substance ISA Symposium. As previously, these Meetings have resulted that histologically appeared amorphous. Seminal X-ray dif- in the present update of the amyloid nomenclature includ- fraction studies of the fibrils revealed a generic cross-b ing recommendations. structure of amyloid fibrils of different origin. The molecu- lar nature of different amyloid fibril proteins was established Amyloid by amino acid sequence analyses with the subsequent con- clusion that they were derived from non-fibrillar precursors. The word ‘amyloid’ was introduced by Rudolf Virchow in 1854 describing a pathologic substance initially believed to At the second International Symposium on Amyloidosis, be related to cellulose or starch but soon shown to be of held in Helsinki, Finland in 1974, the chemical nature of protein nature. For more than 100 years, the word amyloid the first two amyloid fibril proteins were identified and it was almost explicitly used in human and veterinary medi- was at this symposium an embryo of a modern amyloid cine with little mechanistic insight. It was known as an fibril classification was born. CONTACT Per Westermark [email protected] Rudbeck Laboratory, Uppsala, 75185, Sweden ß 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way. 218 M. D. BENSON ET AL. Amyloid fibril 3. Recombinant fibrils of disease-related proteins and of functional amyloid proteins The basic structure of all amyloid is the fibril. An amyloid 4. Fibrils of synthetic or non-disease related peptides fibril is built up by twisted protofilaments. An amyloid pro- 5. Fibrils from condensates and hydrogels that give the tofilament is a stack of protein layers in b-sheet structure, cross-b diffraction pattern which when twisted about identical stacks, forms an amyl- oid fibril. Amyloid fibrils may be formed from 2, 3, 4, or many such protofilaments, or in some cases from a single Additional components in amyloid protofilament. Protofilaments are bound to each other in a parallel fashion via their sidechains. It is well known that amyloid deposits always contain add- Amyloid protofilaments and fibrils can be generated itional molecules. At least heparan sulphate proteoglycan in vitro from protein purified from ex vivo deposits but also (HSPG) and serum amyloid P-component (SAP or AP) are from synthetic or recombinant peptides. Such fibrils exhibit always present but there may be others. How these add- characteristic ultra-structural, X-ray crystallographic diffrac- itional proteins are integrated in the amyloid deposit is tion patterns, and the binding of dyes such as Thioflavin T presently unknown. Protein AP, which is identical with the and Congo red. Recently it has become clear that fibrils plasma protein serum amyloid P (SAP) is bound in a cal- generated in vivo may be different from those derived from cium-dependent fashion to the fibrils. Its importance in the same precursor obtained in the test tube [2]. amyloid pathogenesis is incompletely understood although In 2018, the Nomenclature Committee agreed on a gen- there is evidence that it acts as an inhibitor of fibril degrad- eral definition of the name ‘amyloid’ which earlier was used ation [4]. HSPG is clearly involved in the pathogenesis of differently by varying groups of researchers. In medicine it AA amyloidosis and its ubiquitous presence in other amyl- was used only for pathologic deposits of specific fibrillary oid deposits indicates a universal function in amyloidogene- protein aggregates with distinct microscopic properties, par- sis. Both these components belong to the so called ‘amyloid ticularly affinity for the dye Congo red with typical birefrin- signature proteins’, see below. gence. Thus, in medicine amyloid was regarded as abnormal, an opinion which became unsustainable when the concept of ‘functional amyloid’ was introduced. Chemists, Conceptions used in publications on amyloid and increasingly used the word amyloid for b-sheet protein amyloidosis fibrils of any kind, including synthetic or naturally appear- Appearance of amyloid ing fibrils. The committee agrees that the term ‘amyloid fibril’ should be used for any cross b-sheet fibril [3]. It is Plaque is a word that often is used in scientific literature to b recommended that when the word ‘amyloid’ is used, its describe the spread, small extracellular A deposits in the ’ nature and origin should be clear. cerebral cortex, particularly of patients with Alzheimer s dis- ease. This is an incorrect description of the Ab deposits Functional amyloid
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