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

Amyloid

Volumn 23, Issue 4, 2016, Pages 209-213

  Sipe, Jean D ^a   Benson, Merrill D ^b   Buxbaum, Joel N ^c   Ikeda, Shu Ichi ^d   Merlini, Giampaolo ^e   Saraiva, Maria J M ^f   Westermark, Per ^g  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

^d SHINSHU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^e FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

^f UNIVERSITY OF PORTO   (Portugal)

^g UPPSALA UNIVERSITY   (Sweden)

Author keywords

Amyloid fibril; amyloid protein; amyloidosis; inclusion body; nomenclature

Indexed keywords

AMYLOID; AMYLOID PROTEIN; APOLIPOPROTEIN C2; APOLIPOPROTEIN C3; CELL PROTEIN; ALPHA SYNUCLEIN; BIOLOGICAL MARKER; COLORING AGENT; CONGO RED; PREALBUMIN; PROTEIN PRECURSOR; TAU PROTEIN;

AMYLOIDOSIS; ARTICLE; BIOPHYSICS; CELL INCLUSION; CHEMICAL ANALYSIS; CLINICAL CLASSIFICATION; HUMAN; MEDICAL SOCIETY; NOMENCLATURE; NONHUMAN; PRACTICE GUIDELINE; PRIORITY JOURNAL; PROTEIN FUNCTION; BIREFRINGENCE; CHEMISTRY; CLASSIFICATION; GENE EXPRESSION; GENETICS; METABOLISM; PATHOLOGY; PROCEDURES; SEQUENCE ANALYSIS; STAINING;

ALPHA-SYNUCLEIN; AMYLOIDOGENIC PROTEINS; AMYLOIDOSIS; APOLIPOPROTEIN C-II; APOLIPOPROTEIN C-III; BIOMARKERS; BIREFRINGENCE; COLORING AGENTS; CONGO RED; GENE EXPRESSION; GUIDELINES AS TOPIC; HUMANS; PREALBUMIN; PROTEIN PRECURSORS; SEQUENCE ANALYSIS, PROTEIN; STAINING AND LABELING; TAU PROTEINS; TERMINOLOGY AS TOPIC;

EID: 84997221695     PISSN: 13506129     EISSN: 17442818     Source Type: Journal    
DOI: 10.1080/13506129.2016.1257986     Document Type: Article

References (22)

1. Cohen AS, Franklin EC, Glenner GG, Natvig JB, Osserman EF, Wegelius O., Nomenclature. In:Wegelius O, Pasternack A, eds. Amyloidosis. London:Academic Press;1976:ix
2. Sjölander D, Bijzet J, Hazenberg BP, Nilsson KP, Hammarström P., Sensitive and rapid assessment of amyloid by oligothiophene fluorescence in subcutaneous fat tissue. Amyloid 2015;22:19–25
3. Gillmore JD, Maurer MS, Falk RH, Merlini G, Damy T, Dispenzieri A, Wechalekar AD, et al. Nonbiopsy diagnosis of cardiac transthyretin amyloidosis. Circulation 2016;133:2404–12
4. Nasr SH, Dasari S, Hasadsri L, Theis JD, Vrana JA, Gertz MA, Muppa P, et al. Novel type of renal amyloidosis derived from apolipoprotein-CII. J Am Soc Nephrol 2016; In press
5. Valleix S, Verona G, Jourde-Chiche N, Nédelec B, Mangione PP, Bridoux F, Mangé A, et al. D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile. Nat Commun 2016;7:10353
6. den Dunnen JT, Dalgleish R, Maglott DR, Hart RK, Greenblatt MS, McGowan-Jordan J, Roux AF, et al. HGVS recommendations for the description of sequence variants:2016 update. Hum Mutat 2016;37:564–9
7. IUPAC-IUB Joint Commission on Biochemical Nomenclature. Nomenclature and symbolism for amino acids and peptides. Recommendations 1983. Eur J Biochem 1984;138:9–37
8. Mead S, Gandhi S, Beck J, Caine D, Gajulapalli D, Carswell C, Hyare H, et al. A novel prion disease associated with diarrhea and autonomic neuropathy. N Engl J Med 2013;369:1904–14
9. WHO-IUIS Nomenclature Sub-Committee. Nomenclature of amyloid and amyloidosis. Bull World Health Organ 1993;71:105–12
10. Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, Saraiva MJ, Westermark P., Nomenclature 2014:amyloid fibril proteins and clinical classification of the amyloidosis. Amyloid 2014;21:221–4
11. Ano Bom AP, Rangel LP, Costa DC, de Oliveira GA, Sanches D, Braga CA, Gava LM, et al. Mutant p53 aggregates into prion-like amyloid oligomers and fibrils:implications for cancer. J Biol Chem 2012;287:28152–62
12. Münch J, Rücker E, Ständker L, Adermann K, Goffinet C, Schindler M, Wildum S, et al. Semen-derived amyloid fibrils drastically enhance HIV infection. Cell 2007;131:1059–71
13. Usmani SM, Zirafi O, Müller JA, Sandi-Monroy NL, Yadav JK, Meier C, Weil T, et al. Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen. Nat Commun 2014;5:3508
14. Van Dis ES, Moore TC, Lavender KJ, Messer RJ, Keppler OT, Verheyen J, Dittmer U, et al. No SEVI-mediated enhancement of rectal HIV-1 transmission of HIV-1 in two humanized mouse cohorts. Virology 2016;488:88–95
15. Kalkunte SS, Neubeck S, Norris WE, Cheng SB, Kostadinov S, Vu Hoang D, Ahmed A, et al. Transthyretin is dysregulated in preeclampsia, and its native form prevents the onset of disease in a preclinical mouse model. Am J Pathol 2013;183:1425–36
16. Maury CPJ., The emerging concept of functional amyloid. J Intern Med 2009;265:329–34
17. Westermark P, Benson MD, Buxbaum JN, Cohen AS, Frangione B, Ikeda S-I, Masters CL, et al. A primer of amyloid nomenclature. Amyloid 2007;14:179–83
18. Stangou AJ, Heaton ND, Hawkins PN., Transmission of systemic transthyretin amyloidosis by means of domino liver transplantation. N Engl J Med 2005;352:2356
19. Sipe JD. Revised nomenclature for serum amyloid A (SAA). Nomenclature Committee of the International Society of Amyloidosis. Part 2. Amyloid 1999;6:67–70
20. Pitkänen P, Westermark P, Cornwell GG, III. Senile systemic amyloidosis. Am J Pathol 1984;117:391–9
21. Westermark P, Sletten K, Johansson B, Cornwell GG., III,. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci USA 1990;87:2843–5
22. Benditt EP, Cohen AS, Costa PP, Franklin EC, Glenner GG, Husby G, Mandema E, et al. Guidelines for nomenclature. In:Glenner GG, Costa PP, Freitas AF, eds. Amyloid and amyloidosis. Amsterdam:Excerpta Medica;1980:xI–XII