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Genetic factors in the amyloid diseases

Peter D Gorevic, MD
Section Editors
Peter H Schur, MD
Benjamin A Raby, MD, MPH
Deputy Editor
Paul L Romain, MD


Amyloidosis is a generic term that refers to the extracellular tissue deposition of fibrils composed of low molecular weight subunits (5 to 25 kD) of proteins, many of which are normal constituents of serum. The fibrils are insoluble polymers comprised of these low molecular weight subunit proteins. These subunits are derived, in turn, from soluble precursors, which undergo conformational changes that lead to the adoption of a predominantly antiparallel beta-pleated sheet configuration [1,2].

Amyloid deposits appear as amorphous hyaline material on light microscopy (picture 1A-D). The fibrils bind Congo red (leading to green birefringence under polarized light) and thioflavine T (producing an intense yellow-green fluorescence). Electron microscopic examination of the ultrastructure of amyloid deposits generally demonstrates straight and unbranching fibrils, which may be composed of protofilaments at higher resolution [3]. Immunohistochemical [4] and biochemical [5] techniques can be used to identify the type of protein subunit.

Routes to fibrillogenesis include partial folding or unfolding of the precursor protein that may be facilitated by acidification or proteolysis and that may be accelerated by nucleation [6-9]. Fibril formation is also associated with co-deposition of other substances, notably including glycosaminoglycans (GAGs, particularly heparan sulfate), serum amyloid P-component (SAP, a member of the pentraxin family that includes C-reactive protein), and specific apolipoproteins (E and J) [10-12]. Cofactors, including molecular chaperones and proteases, may significantly modulate fibrillogenesis at any of several steps involved in the conversion of soluble precursors to fibrils and may potentially influence the deposition phase of amyloid in tissue, as well as resorption [13-15].

The importance of heredity in the expression of amyloid diseases has been recognized for many years [16]. Some amyloid disorders appear to be entirely due to heritable abnormalities in precursor proteins. In addition, the expression of acquired amyloidoses may be affected by genetically determined factors.

The genetic contributions to various types of amyloidosis will be reviewed here. Three types of genetic abnormalities have been identified in amyloidogenic proteins: polymorphisms, variant molecules (eg, due to missense mutations, deletions, or premature stop codons), and genetically determined posttranslational modifications (table 1). In addition, mutations in genes for non-amyloidogenic proteins can play a permissive role in amyloid development. Examples include pyrin mutations in familial Mediterranean fever and presenilin mutations in early-onset Alzheimer disease.

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Literature review current through: Dec 2017. | This topic last updated: Jul 19, 2016.
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  1. Rostagno A, Holton JL, Lashley T, et al. Cerebral amyloidosis: amyloid subunits, mutants and phenotypes. Cell Mol Life Sci 2010; 67:581.
  2. Wechalekar AD, Gillmore JD, Hawkins PN. Systemic amyloidosis. Lancet 2016; 387:2641.
  3. Jahn TR, Makin OS, Morris KL, et al. The common architecture of cross-beta amyloid. J Mol Biol 2010; 395:717.
  4. Schönland SO, Hegenbart U, Bochtler T, et al. Immunohistochemistry in the classification of systemic forms of amyloidosis: a systematic investigation of 117 patients. Blood 2012; 119:488.
  5. Brambilla F, Lavatelli F, Merlini G, Mauri P. Clinical proteomics for diagnosis and typing of systemic amyloidoses. Proteomics Clin Appl 2013; 7:136.
  6. Chiti F, Dobson CM. Amyloid formation by globular proteins under native conditions. Nat Chem Biol 2009; 5:15.
  7. Arosio P, Knowles TP, Linse S. On the lag phase in amyloid fibril formation. Phys Chem Chem Phys 2015; 17:7606.
  8. Palaninathan SK, Mohamedmohaideen NN, Snee WC, et al. Structural insight into pH-induced conformational changes within the native human transthyretin tetramer. J Mol Biol 2008; 382:1157.
  9. Tipping KW, Karamanos TK, Jakhria T, et al. pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proc Natl Acad Sci U S A 2015; 112:5691.
  10. Pepys MB. Amyloidosis. Annu Rev Med 2006; 57:223.
  11. Dergunov AD. Role of ApoE in conformation-prone diseases and atherosclerosis. Biochemistry (Mosc) 2006; 71:707.
  12. Iannuzzi C, Irace G, Sirangelo I. The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity. Molecules 2015; 20:2510.
  13. McLaurin J, Yang D, Yip CM, Fraser PE. Review: modulating factors in amyloid-beta fibril formation. J Struct Biol 2000; 130:259.
  14. Doyle SM, Genest O, Wickner S. Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol 2013; 14:617.
  15. Marcoux J, Mangione PP, Porcari R, et al. A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis. EMBO Mol Med 2015; 7:1337.
  16. Thomas PK. Genetic factors in amyloidosis. J Med Genet 1975; 12:317.
  17. Huff ME, Balch WE, Kelly JW. Pathological and functional amyloid formation orchestrated by the secretory pathway. Curr Opin Struct Biol 2003; 13:674.
  18. Das M, Gursky O. Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights. Adv Exp Med Biol 2015; 855:175.
  19. Moraitakis G, Goodfellow JM. Simulations of human lysozyme: probing the conformations triggering amyloidosis. Biophys J 2003; 84:2149.
  20. Calero M, Pawlik M, Soto C, et al. Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type. J Neurochem 2001; 77:628.
  21. Maury CP, Nurmiaho-Lassila EL, Boysen G, Liljeström M. Fibrillogenesis in gelsolin-related familial amyloidosis. Amyloid 2003; 10 Suppl 1:21.
  22. Levy E, Prelli F, Frangione B. Studies on the first described Alzheimer's disease amyloid beta mutant, the Dutch variant. J Alzheimers Dis 2006; 9:329.
  23. Sahlin C, Lord A, Magnusson K, et al. The Arctic Alzheimer mutation favors intracellular amyloid-beta production by making amyloid precursor protein less available to alpha-secretase. J Neurochem 2007; 101:854.
  24. Yazaki M, Liepnieks JJ, Barats MS, et al. Hereditary systemic amyloidosis associated with a new apolipoprotein AII stop codon mutation Stop78Arg. Kidney Int 2003; 64:11.
  25. Ghiso J, Vidal R, Rostagno A, et al. A newly formed amyloidogenic fragment due to a stop codon mutation causes familial British dementia. Ann N Y Acad Sci 2000; 903:129.
  26. Maury CP, Sletten K, Totty N, et al. Identification of the circulating amyloid precursor and other gelsolin metabolites in patients with G654A mutation in the gelsolin gene (Finnish familial amyloidosis): pathogenetic and diagnostic implications. Lab Invest 1997; 77:299.
  27. Nepomuceno AI, Mason CJ, Muddiman DC, et al. Detection of genetic variants of transthyretin by liquid chromatography-dual electrospray ionization fourier-transform ion-cyclotron-resonance mass spectrometry. Clin Chem 2004; 50:1535.
  28. Altland K, Benson MD, Costello CE, et al. Genetic microheterogeneity of human transthyretin detected by IEF. Electrophoresis 2007; 28:2053.
  29. Benson MD. The hereditary amyloidoses. In: Amyloid and Related Disorders: Surgical Pathology and Clinical Correlations, Springer, 2012. p.53.
  30. Rowczenio DM, Noor I, Gillmore JD, et al. Online registry for mutations in hereditary amyloidosis including nomenclature recommendations. Hum Mutat 2014; 35:E2403.
  31. Connors LH, Lim A, Prokaeva T, et al. Tabulation of human transthyretin (TTR) variants, 2003. Amyloid 2003; 10:160.
  32. Sekijima, Y, Yoshida, et al. Familial Transthyretin Amyloidosis. In: Gene Reviews, Pagon, RA, Bird, TC, Dolan, CR, Stephens, K (Eds), University of Washington, Seattle 2010.
  33. Hemminki K, Li X, Försti A, et al. Non-Hodgkin lymphoma in familial amyloid polyneuropathy patients in Sweden. Blood 2013; 122:458.
  34. Zaros C, Genin E, Hellman U, et al. On the origin of the transthyretin Val30Met familial amyloid polyneuropathy. Ann Hum Genet 2008; 72:478.
  35. Kato-Motozaki Y, Ono K, Shima K, et al. Epidemiology of familial amyloid polyneuropathy in Japan: Identification of a novel endemic focus. J Neurol Sci 2008; 270:133.
  36. Hellman U, Suhr O. Regional differences and similarities of FAP in Sweden. Amyloid 2012; 19 Suppl 1:53.
  37. Hellman U, Alarcon F, Lundgren HE, et al. Heterogeneity of penetrance in familial amyloid polyneuropathy, ATTR Val30Met, in the Swedish population. Amyloid 2008; 15:181.
  38. Olsson M, Norgren N, Obayashi K, et al. A possible role for miRNA silencing in disease phenotype variation in Swedish transthyretin V30M carriers. BMC Med Genet 2010; 11:130.
  39. Coelho T, Maurer MS, Suhr OB. THAOS - The Transthyretin Amyloidosis Outcomes Survey: initial report on clinical manifestations in patients with hereditary and wild-type transthyretin amyloidosis. Curr Med Res Opin 2013; 29:63.
  40. Parman Y, Adams D, Obici L, et al. Sixty years of transthyretin familial amyloid polyneuropathy (TTR-FAP) in Europe: where are we now? A European network approach to defining the epidemiology and management patterns for TTR-FAP. Curr Opin Neurol 2016; 29 Suppl 1:S3.
  41. Quarta CC, Buxbaum JN, Shah AM, et al. The amyloidogenic V122I transthyretin variant in elderly black Americans. N Engl J Med 2015; 372:21.
  42. Jacobson DR, Alexander AA, Tagoe C, Buxbaum JN. Prevalence of the amyloidogenic transthyretin (TTR) V122I allele in 14 333 African-Americans. Amyloid 2015; 22:171.
  43. Augustin S, Llige D, Andreu A, et al. Familial amyloidosis in a large Spanish kindred resulting from a D38V mutation in the transthyretin gene. Eur J Clin Invest 2007; 37:673.
  44. Kristen AV, Ehlermann P, Helmke B, et al. Transthyretin valine-94-alanine, a novel variant associated with late-onset systemic amyloidosis with cardiac involvement. Amyloid 2007; 14:283.
  45. Maurer MS, Hanna M, Grogan M, et al. Genotype and Phenotype of Transthyretin Cardiac Amyloidosis: THAOS (Transthyretin Amyloid Outcome Survey). J Am Coll Cardiol 2016; 68:161.
  46. Lobato L, Rocha A. Transthyretin amyloidosis and the kidney. Clin J Am Soc Nephrol 2012; 7:1337.
  47. McColgan P, Viegas S, Gandhi S, et al. Oculoleptomeningeal Amyloidosis associated with transthyretin Leu12Pro in an African patient. J Neurol 2015; 262:228.
  48. Almeida MR, Alves IL, Terazaki H, et al. Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M. Biochem Biophys Res Commun 2000; 270:1024.
  49. Hornstrup LS, Frikke-Schmidt R, Nordestgaard BG, Tybjærg-Hansen A. Genetic stabilization of transthyretin, cerebrovascular disease, and life expectancy. Arterioscler Thromb Vasc Biol 2013; 33:1441.
  50. Cruts M, Theuns J, Van Broeckhoven C. Locus-specific mutation databases for neurodegenerative brain diseases. Hum Mutat 2012; 33:1340.
  51. Prusiner SB. Biology and genetics of prions causing neurodegeneration. Annu Rev Genet 2013; 47:601.
  52. Hsiao K, Baker HF, Crow TJ, et al. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 1989; 338:342.
  53. Liberski PP. Gerstmann-Sträussler-Scheinker disease. Adv Exp Med Biol 2012; 724:128.
  54. Medori R, Tritschler HJ, LeBlanc A, et al. Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene. N Engl J Med 1992; 326:444.
  55. Gambetti P, Parchi P, Chen SG. Hereditary Creutzfeldt-Jakob disease and fatal familial insomnia. Clin Lab Med 2003; 23:43.
  56. Kiuru-Enari S, Haltia M. Hereditary gelsolin amyloidosis. Handb Clin Neurol 2013; 115:659.
  57. Efebera YA, Sturm A, Baack EC, et al. Novel gelsolin variant as the cause of nephrotic syndrome and renal amyloidosis in a large kindred. Amyloid 2014; 21:110.
  58. Obici L, Palladini G, Giorgetti S, et al. Liver biopsy discloses a new apolipoprotein A-I hereditary amyloidosis in several unrelated Italian families. Gastroenterology 2004; 126:1416.
  59. Rowczenio D, Dogan A, Theis JD, et al. Amyloidogenicity and clinical phenotype associated with five novel mutations in apolipoprotein A-I. Am J Pathol 2011; 179:1978.
  60. Magy N, Liepnieks JJ, Yazaki M, et al. Renal transplantation for apolipoprotein AII amyloidosis. Amyloid 2003; 10:224.
  61. Benson MD. Ostertag revisited: the inherited systemic amyloidoses without neuropathy. Amyloid 2005; 12:75.
  62. Nasr SH, Dasari S, Hasadsri L, et al. Novel Type of Renal Amyloidosis Derived from Apolipoprotein-CII. J Am Soc Nephrol 2017; 28:439.
  63. Valleix S, Verona G, Jourde-Chiche N, et al. D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile. Nat Commun 2016; 7:10353.
  64. Röcken C, Becker K, Fändrich M, et al. ALys amyloidosis caused by compound heterozygosity in exon 2 (Thr70Asn) and exon 4 (Trp112Arg) of the lysozyme gene. Hum Mutat 2006; 27:119.
  65. Sattianayagam PT, Gibbs SD, Rowczenio D, et al. Hereditary lysozyme amyloidosis -- phenotypic heterogeneity and the role of solid organ transplantation. J Intern Med 2012; 272:36.
  66. Girnius S, Skinner M, Spencer B, et al. A new lysozyme tyr54asn mutation causing amyloidosis in a family of Swedish ancestry with gastrointestinal symptoms. Amyloid 2012; 19:182.
  67. Lachmann HJ, Booth DR, Booth SE, et al. Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis. N Engl J Med 2002; 346:1786.
  68. Zhen DB, Swiecicki PL, Zeldenrust SR, et al. Frequencies and geographic distributions of genetic mutations in transthyretin- and non-transthyretin-related familial amyloidosis. Clin Genet 2015; 88:396.
  69. Gillmore JD, Lachmann HJ, Wechalekar A, Hawkins PN. Hereditary fibrinogen A alpha-chain amyloidosis: clinical phenotype and role of liver transplantation. Blood 2010; 115:4313; author reply 4314.
  70. Haidinger M, Werzowa J, Kain R, et al. Hereditary amyloidosis caused by R554L fibrinogen Aα-chain mutation in a Spanish family and review of the literature. Amyloid 2013; 20:72.
  71. Palsdottir A, Snorradottir AO, Thorsteinsson L. Hereditary cystatin C amyloid angiopathy: genetic, clinical, and pathological aspects. Brain Pathol 2006; 16:55.
  72. Valleix S, Gillmore JD, Bridoux F, et al. Hereditary systemic amyloidosis due to Asp76Asn variant β2-microglobulin. N Engl J Med 2012; 366:2276.
  73. Comenzo RL, Zhou P, Fleisher M, et al. Seeking confidence in the diagnosis of systemic AL (Ig light-chain) amyloidosis: patients can have both monoclonal gammopathies and hereditary amyloid proteins. Blood 2006; 107:3489.
  74. Benson MD, Liepnieks JJ, Kluve-Beckerman B. Hereditary systemic immunoglobulin light-chain amyloidosis. Blood 2015; 125:3281.
  75. Kiuru S. Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide. Amyloid 1998; 5:55.
  76. Holmgren G, Hellman U, Lundgren HE, et al. Impact of homozygosity for an amyloidogenic transthyretin mutation on phenotype and long term outcome. J Med Genet 2005; 42:953.
  77. Sequeiros J, Saraiva MJ. Onset in the seventh decade and lack of symptoms in heterozygotes for the TTRMet30 mutation in hereditary amyloid neuropathy-type I (Portuguese, Andrade). Am J Med Genet 1987; 27:345.
  78. Koike H, Sobue G. Late-onset familial amyloid polyneuropathy in Japan. Amyloid 2012; 19 Suppl 1:55.
  79. Jacobson DR, Pastore RD, Yaghoubian R, et al. Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans. N Engl J Med 1997; 336:466.
  80. Obici L, Raimondi S, Lavatelli F, et al. Susceptibility to AA amyloidosis in rheumatic diseases: a critical overview. Arthritis Rheum 2009; 61:1435.
  81. Papadopoulos VP, Giaglis S, Mitroulis I, Ritis K. The population genetics of familial mediterranean fever: a meta-analysis study. Ann Hum Genet 2008; 72:752.
  82. Tunca M, Akar S, Onen F, et al. Familial Mediterranean fever (FMF) in Turkey: results of a nationwide multicenter study. Medicine (Baltimore) 2005; 84:1.
  83. Altunoğlu A, Erten Ş, Canoz MB, et al. Phenotype 2 familial mediterranean fever: evaluation of 22 case series and review of the literature on phenotype 2 FMF. Ren Fail 2013; 35:226.
  84. Lachmann HJ, Goodman HJ, Gilbertson JA, et al. Natural history and outcome in systemic AA amyloidosis. N Engl J Med 2007; 356:2361.
  85. Touitou I, Sarkisian T, Medlej-Hashim M, et al. Country as the primary risk factor for renal amyloidosis in familial Mediterranean fever. Arthritis Rheum 2007; 56:1706.
  86. Booth DR, Booth SE, Gillmore JD, et al. SAA1 alleles as risk factors in reactive systemic AA amyloidosis. Amyloid 1998; 5:262.
  87. Ajiro J, Narita I, Sato F, et al. SAA1 gene polymorphisms and the risk of AA amyloidosis in Japanese patients with rheumatoid arthritis. Mod Rheumatol 2006; 16:294.
  88. Migita K, Agematsu K, Masumoto J, et al. The contribution of SAA1 polymorphisms to Familial Mediterranean fever susceptibility in the Japanese population. PLoS One 2013; 8:e55227.
  89. Utku U, Dilek M, Akpolat I, et al. SAA1 alpha/alpha alleles in Behçet's disease related amyloidosis. Clin Rheumatol 2007; 26:927.
  90. Akar N, Hasipek M, Oztürk A, et al. Serum amyloid A1 -13 T/C alleles in Turkish familial Mediterranean fever patients with and without amyloidosis. J Nephrol 2006; 19:318.
  91. Pettersson T, Konttinen YT. Amyloidosis-recent developments. Semin Arthritis Rheum 2010; 39:356.
  92. Lane T, Loeffler JM, Rowczenio DM, et al. AA amyloidosis complicating the hereditary periodic fever syndromes. Arthritis Rheum 2013; 65:1116.
  93. Pras M. Amyloidosis of familial mediterranean fever and the MEFV gene. Amyloid 2000; 7:289.
  94. Ong FS, Vakil H, Xue Y, et al. The M694V mutation in Armenian-Americans: a 10-year retrospective study of MEFV mutation testing for familial Mediterranean fever at UCLA. Clin Genet 2013; 84:55.
  95. Lidar M, Kedem R, Berkun Y, et al. Familial Mediterranean fever in Ashkenazi Jews: the mild end of the clinical spectrum. J Rheumatol 2010; 37:422.
  96. Ozen S, Aktay N, Lainka E, et al. Disease severity in children and adolescents with familial Mediterranean fever: a comparative study to explore environmental effects on a monogenic disease. Ann Rheum Dis 2009; 68:246.
  97. Marek-Yagel D, Berkun Y, Padeh S, et al. Clinical disease among patients heterozygous for familial Mediterranean fever. Arthritis Rheum 2009; 60:1862.
  98. Masters SL, Simon A, Aksentijevich I, Kastner DL. Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*). Annu Rev Immunol 2009; 27:621.
  99. Medlej-Hashim M, Delague V, Chouery E, et al. Amyloidosis in familial Mediterranean fever patients: correlation with MEFV genotype and SAA1 and MICA polymorphisms effects. BMC Med Genet 2004; 5:4.
  100. van der Hilst JC, Simon A, Drenth JP. Hereditary periodic fever and reactive amyloidosis. Clin Exp Med 2005; 5:87.
  101. Lachmann HJ, Papa R, Gerhold K, et al. The phenotype of TNF receptor-associated autoinflammatory syndrome (TRAPS) at presentation: a series of 158 cases from the Eurofever/EUROTRAPS international registry. Ann Rheum Dis 2014; 73:2160.
  102. Kubota T, Koike R. Cryopyrin-associated periodic syndromes: background and therapeutics. Mod Rheumatol 2010; 20:213.
  103. Toker O, Hashkes PJ. Critical appraisal of canakinumab in the treatment of adults and children with cryopyrin-associated periodic syndrome (CAPS). Biologics 2010; 4:131.
  104. Obici L, Manno C, Muda AO, et al. First report of systemic reactive (AA) amyloidosis in a patient with the hyperimmunoglobulinemia D with periodic fever syndrome. Arthritis Rheum 2004; 50:2966.
  105. Ter Haar NM, Jeyaratnam J, Lachmann HJ, et al. The Phenotype and Genotype of Mevalonate Kinase Deficiency: A Series of 114 Cases From the Eurofever Registry. Arthritis Rheumatol 2016; 68:2795.
  106. ISSAID: the International Society of Systemic Autoinflammatory Diseases. Copyright. Available at http://fmf.igh.cnrs.fr/ISSAID (Accessed on September 24, 2013).
  107. Milhavet F, Cuisset L, Hoffman HM, et al. The infevers autoinflammatory mutation online registry: update with new genes and functions. Hum Mutat 2008; 29:803.
  108. Touitou I, Lesage S, McDermott M, et al. Infevers: an evolving mutation database for auto-inflammatory syndromes. Hum Mutat 2004; 24:194.
  109. Sarrauste de Menthière C, Terrière S, Pugnère D, et al. INFEVERS: the Registry for FMF and hereditary inflammatory disorders mutations. Nucleic Acids Res 2003; 31:282.
  110. Klintworth GK. Corneal dystrophies. Orphanet J Rare Dis 2009; 4:7.
  111. Kawasaki S, Kinoshita S. Clinical and basic aspects of gelatinous drop-like corneal dystrophy. Dev Ophthalmol 2011; 48:97.
  112. Niel-Butschi F, Kantelip B, Iwaszkiewicz J, et al. Genotype-phenotype correlations of TGFBI p.Leu509Pro, p.Leu509Arg, p.Val613Gly, and the allelic association of p.Met502Val-p.Arg555Gln mutations. Mol Vis 2011; 17:1192.
  113. Khurana R, Agarwal A, Bajpai VK, et al. Unraveling the amyloid associated with human medullary thyroid carcinoma. Endocrinology 2004; 145:5465.
  114. Verga U, Fugazzola L, Cambiaghi S, et al. Frequent association between MEN 2A and cutaneous lichen amyloidosis. Clin Endocrinol (Oxf) 2003; 59:156.
  115. Westermark P, Murphy C, Eulitz M, et al. Galectin 7-associated cutaneous amyloidosis. Amyloid 2010; 17(Suppl 1):71.