Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines

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Sipe, Jean D.Boston Univ, Sch Med, Dept Biochem, Boston, MA 02118 USA. (author)

Amyloid fibril proteins and amyloidosis : chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines

Article/chapterEnglish2016

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2016-11-24
Informa UK Limited,2016
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LIBRIS-ID:oai:DiVA.org:uu-313540
https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-313540URI
https://doi.org/10.1080/13506129.2016.1257986DOI

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Language:English
Summary in:English

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The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XVth Symposium of the Society, 3 July-7 July 2016, Uppsala, Sweden, to assess and formulate recommendations for nomenclature for amyloid fibril proteins and the clinical classification of the amyloidoses. An amyloid fibril must exhibit affinity for Congo red and with green, yellow or orange birefringence when the Congo red-stained deposits are viewed with polarized light. While congophilia and birefringence remain the gold standard for demonstration of amyloid deposits, new staining and imaging techniques are proving useful. To be included in the nomenclature list, in addition to congophilia and birefringence, the chemical identity of the protein must be unambiguously characterized by protein sequence analysis when possible. In general, it is insufficient to identify a mutation in the gene of a candidate amyloid protein without confirming the variant changes in the amyloid fibril protein. Each distinct form of amyloidosis is uniquely characterized by the chemical identity of the amyloid fibril protein that deposits in the extracellular spaces of tissues and organs and gives rise to the disease syndrome. The fibril proteins are designated as protein A followed by a suffix that is an abbreviation of the parent or precursor protein name. To date, there are 36 known extracellular fibril proteins in humans, 2 of which are iatrogenic in nature and 9 of which have also been identified in animals. Two newly recognized fibril proteins, AApoCII derived from apolipoprotein CII and AApoCIII derived from apolipoprotein CIII, have been added. AApoCII amyloidosis and AApoCIII amyloidosis are hereditary systemic amyloidoses. Intracellular protein inclusions displaying some of the properties of amyloid, intracellular amyloid have been reported. Two proteins which were previously characterized as intracellular inclusions, tau and -synuclein, are now recognized to form extracellular deposits upon cell death and thus have been included in Table 1 as ATau and ASyn.

Subject headings and genre

MEDICIN OCH HÄLSOVETENSKAP Medicinska och farmaceutiska grundvetenskaper Cell- och molekylärbiologi hsv//swe
MEDICAL AND HEALTH SCIENCES Basic Medicine Cell and Molecular Biology hsv//eng
MEDICIN OCH HÄLSOVETENSKAP Klinisk medicin Klinisk laboratoriemedicin hsv//swe
MEDICAL AND HEALTH SCIENCES Clinical Medicine Clinical Laboratory Medicine hsv//eng
Amyloid fibril
amyloid protein
amyloidosis
inclusion body
nomenclature
Patologi
Pathology

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Benson, Merrill D.Indiana Univ Sch Med, Dept Pathol & Lab Med, Indianapolis, IN 46202 USA. (author)
Buxbaum, Joel N.Scripps Res Inst, Dept Mol & Expt Med, 10666 N Torrey Pines Rd, La Jolla, CA 92037 USA. (author)
Ikeda, Shu-ichiShinshu Univ, Sch Med, Dept Med Neurol & Rheumatol, Matsumoto, Nagano, Japan. (author)
Merlini, GiampaoloUniv Pavia, Amyloid Res & Treatment Ctr, Pavia, Italy.;IRCCS Policlin San Matteo, Pavia, Italy. (author)
Saraiva, Maria J. M.Univ Porto, Inst Mol & Cellular Biol, Amyloid Unit, Oporto, Portugal. (author)
Westermark, PerUppsala universitet,Klinisk och experimentell patologi,Per Westermark(Swepub:uu)perweste (author)
Boston Univ, Sch Med, Dept Biochem, Boston, MA 02118 USA.Indiana Univ Sch Med, Dept Pathol & Lab Med, Indianapolis, IN 46202 USA. (creator_code:org_t)

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In:Amyloid: Informa UK Limited23:4, s. 209-2131350-61291744-2818

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