title: Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of Amyloidosis.
abstract: The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XIIIth International Symposium, May 6-10, 2012, Groningen, The Netherlands, to formulate recommendations on amyloid fibril protein nomenclature and to consider newly identified candidate amyloid fibril proteins for inclusion in the ISA Amyloid Fibril Protein Nomenclature List. The need to promote utilization of consistent and up to date terminology for both fibril chemistry and clinical classification of the resultant disease syndrome was emphasized. Amyloid fibril nomenclature is based on the chemical identity of the amyloid fibril forming protein; clinical classification of the amyloidosis should be as well. Although the importance of fibril chemistry to the disease process has been recognized for more than 40 years, to this day the literature contains clinical and histochemical designations that were used when the chemical diversity of amyloid diseases was poorly understood. Thus, the continued use of disease classifications such as familial amyloid neuropathy and familial amyloid cardiomyopathy generates confusion. An amyloid fibril protein is defined as follows: the protein must occur in body tissue deposits and exhibit both affinity for Congo red and green birefringence when Congo red stained deposits are viewed by polarization microscopy. Furthermore, the chemical identity of the protein must have been unambiguously characterized by protein sequence analysis when so is practically possible. Thus, in nearly all cases, it is insufficient to demonstrate mutation in the gene of a candidate amyloid protein; the protein itself must be identified as an amyloid fibril protein. Current ISA Amyloid Fibril Protein Nomenclature Lists of 30 human and 10 animal fibril proteins are provided together with a list of inclusion bodies that, although intracellular, exhibit some or all of the properties of the mainly extracellular amyloid fibrils.
authors.affiliation: Department of Biochemistry, Boston University School of Medicine, MA, USA. sipejd@verizon.net
authors.forename: Jean D
authors.initials: JD
authors.lastname: Sipe
authors.forename: Merrill D
authors.initials: MD
authors.lastname: Benson
authors.forename: Joel N
authors.initials: JN
authors.lastname: Buxbaum
authors.forename: Shu-ichi
authors.initials: S
authors.lastname: Ikeda
authors.forename: Giampaolo
authors.initials: G
authors.lastname: Merlini
authors.forename: Maria J M
authors.initials: MJ
authors.lastname: Saraiva
authors.forename: Per
authors.initials: P
authors.lastname: Westermark
mesh_terms: D058227:Amyloidogenic Proteins / Q000145:classification*; D000686:Amyloidosis / Q000145:classification*; D003224:Congo Red; D006651:Histocytochemistry; D006801:Humans; D008859:Microscopy, Polarization
chemical_list: D058227:Amyloidogenic Proteins; D003224:Congo Red