Skip to main content
PMC home page
Bulletin of the World Health Organization logoLink to Bulletin of the World Health Organization
. 1993;71(1):105–112.

Nomenclature of amyloid and amyloidosis. WHO-IUIS Nomenclature Sub-Committee.

PMCID: PMC2393434  PMID: 8440029

Abstract

This classification of amyloid and amyloidosis is based on the amyloid fibril proteins, followed by a designation of the fibril protein precursor. Additional information includes the protein type or variant (where applicable) and the clinical diagnosis.

Full text

PDF
105

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Benditt E. P., Eriksen N., Hermodson M. A., Ericsson L. H. The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett. 1971 Dec 1;19(2):169–173. doi: 10.1016/0014-5793(71)80506-9. [DOI] [PubMed] [Google Scholar]
  2. Benditt E. P., Eriksen N., Hermodson M. A., Ericsson L. H. The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett. 1971 Dec 1;19(2):169–173. doi: 10.1016/0014-5793(71)80506-9. [DOI] [PubMed] [Google Scholar]
  3. Costa P. P., Figueira A. S., Bravo F. R. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4499–4503. doi: 10.1073/pnas.75.9.4499. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Costa P. P., Figueira A. S., Bravo F. R. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4499–4503. doi: 10.1073/pnas.75.9.4499. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gejyo F., Yamada T., Odani S., Nakagawa Y., Arakawa M., Kunitomo T., Kataoka H., Suzuki M., Hirasawa Y., Shirahama T. A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin. Biochem Biophys Res Commun. 1985 Jun 28;129(3):701–706. doi: 10.1016/0006-291x(85)91948-5. [DOI] [PubMed] [Google Scholar]
  6. Gejyo F., Yamada T., Odani S., Nakagawa Y., Arakawa M., Kunitomo T., Kataoka H., Suzuki M., Hirasawa Y., Shirahama T. A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin. Biochem Biophys Res Commun. 1985 Jun 28;129(3):701–706. doi: 10.1016/0006-291x(85)91948-5. [DOI] [PubMed] [Google Scholar]
  7. Ghiso J., Jensson O., Frangione B. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C). Proc Natl Acad Sci U S A. 1986 May;83(9):2974–2978. doi: 10.1073/pnas.83.9.2974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ghiso J., Jensson O., Frangione B. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C). Proc Natl Acad Sci U S A. 1986 May;83(9):2974–2978. doi: 10.1073/pnas.83.9.2974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Glenner G. G., Harbaugh J., Ohma J. I., Harada M., Cuatrecasas P. An amyloid protein: the amino-terminal variable fragment of an immunoglobulin light chain. Biochem Biophys Res Commun. 1970 Dec 9;41(5):1287–1289. doi: 10.1016/0006-291x(70)90227-5. [DOI] [PubMed] [Google Scholar]
  10. Glenner G. G., Harbaugh J., Ohma J. I., Harada M., Cuatrecasas P. An amyloid protein: the amino-terminal variable fragment of an immunoglobulin light chain. Biochem Biophys Res Commun. 1970 Dec 9;41(5):1287–1289. doi: 10.1016/0006-291x(70)90227-5. [DOI] [PubMed] [Google Scholar]
  11. Glenner G. G., Terry W., Harada M., Isersky C., Page D. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971 Jun 11;172(3988):1150–1151. doi: 10.1126/science.172.3988.1150. [DOI] [PubMed] [Google Scholar]
  12. Glenner G. G., Terry W., Harada M., Isersky C., Page D. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971 Jun 11;172(3988):1150–1151. doi: 10.1126/science.172.3988.1150. [DOI] [PubMed] [Google Scholar]
  13. Glenner G. G., Wong C. W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 1984 May 16;120(3):885–890. doi: 10.1016/s0006-291x(84)80190-4. [DOI] [PubMed] [Google Scholar]
  14. Glenner G. G., Wong C. W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 1984 May 16;120(3):885–890. doi: 10.1016/s0006-291x(84)80190-4. [DOI] [PubMed] [Google Scholar]
  15. Gorevic P. D., Casey T. T., Stone W. J., DiRaimondo C. R., Prelli F. C., Frangione B. Beta-2 microglobulin is an amyloidogenic protein in man. J Clin Invest. 1985 Dec;76(6):2425–2429. doi: 10.1172/JCI112257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Gorevic P. D., Casey T. T., Stone W. J., DiRaimondo C. R., Prelli F. C., Frangione B. Beta-2 microglobulin is an amyloidogenic protein in man. J Clin Invest. 1985 Dec;76(6):2425–2429. doi: 10.1172/JCI112257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Haltia M., Prelli F., Ghiso J., Kiuru S., Somer H., Palo J., Frangione B. Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein. Biochem Biophys Res Commun. 1990 Mar 30;167(3):927–932. doi: 10.1016/0006-291x(90)90612-q. [DOI] [PubMed] [Google Scholar]
  18. Haltia M., Prelli F., Ghiso J., Kiuru S., Somer H., Palo J., Frangione B. Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein. Biochem Biophys Res Commun. 1990 Mar 30;167(3):927–932. doi: 10.1016/0006-291x(90)90612-q. [DOI] [PubMed] [Google Scholar]
  19. Hellman U., Wernstedt C., Westermark P., O'Brien T. D., Rathbun W. B., Johnson K. H. Amino acid sequence from degu islet amyloid-derived insulin shows unique sequence characteristics. Biochem Biophys Res Commun. 1990 Jun 15;169(2):571–577. doi: 10.1016/0006-291x(90)90369-x. [DOI] [PubMed] [Google Scholar]
  20. Hellman U., Wernstedt C., Westermark P., O'Brien T. D., Rathbun W. B., Johnson K. H. Amino acid sequence from degu islet amyloid-derived insulin shows unique sequence characteristics. Biochem Biophys Res Commun. 1990 Jun 15;169(2):571–577. doi: 10.1016/0006-291x(90)90369-x. [DOI] [PubMed] [Google Scholar]
  21. Higuchi K., Yonezu T., Tsunasawa S., Sakiyama F., Takeda T. The single proline-glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A-II. FEBS Lett. 1986 Oct 20;207(1):23–27. doi: 10.1016/0014-5793(86)80006-0. [DOI] [PubMed] [Google Scholar]
  22. Higuchi K., Yonezu T., Tsunasawa S., Sakiyama F., Takeda T. The single proline-glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A-II. FEBS Lett. 1986 Oct 20;207(1):23–27. doi: 10.1016/0014-5793(86)80006-0. [DOI] [PubMed] [Google Scholar]
  23. Hsiao K., Baker H. F., Crow T. J., Poulter M., Owen F., Terwilliger J. D., Westaway D., Ott J., Prusiner S. B. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature. 1989 Mar 23;338(6213):342–345. doi: 10.1038/338342a0. [DOI] [PubMed] [Google Scholar]
  24. Hsiao K., Baker H. F., Crow T. J., Poulter M., Owen F., Terwilliger J. D., Westaway D., Ott J., Prusiner S. B. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature. 1989 Mar 23;338(6213):342–345. doi: 10.1038/338342a0. [DOI] [PubMed] [Google Scholar]
  25. Husby G., Natvig J. B., Michaelsen T. E., Sletten K., Höst H. Unique amyloid protein subunit common to different types of amyloid fibril. Nature. 1973 Aug 10;244(5415):362–364. doi: 10.1038/244362a0. [DOI] [PubMed] [Google Scholar]
  26. Husby G., Natvig J. B., Michaelsen T. E., Sletten K., Höst H. Unique amyloid protein subunit common to different types of amyloid fibril. Nature. 1973 Aug 10;244(5415):362–364. doi: 10.1038/244362a0. [DOI] [PubMed] [Google Scholar]
  27. Johansson B., Wernstedt C., Westermark P. Atrial natriuretic peptide deposited as atrial amyloid fibrils. Biochem Biophys Res Commun. 1987 Nov 13;148(3):1087–1092. doi: 10.1016/s0006-291x(87)80243-7. [DOI] [PubMed] [Google Scholar]
  28. Johansson B., Wernstedt C., Westermark P. Atrial natriuretic peptide deposited as atrial amyloid fibrils. Biochem Biophys Res Commun. 1987 Nov 13;148(3):1087–1092. doi: 10.1016/s0006-291x(87)80243-7. [DOI] [PubMed] [Google Scholar]
  29. Levin M., Franklin E. C., Frangione B., Pras M. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest. 1972 Oct;51(10):2773–2776. doi: 10.1172/JCI107098. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Levin M., Franklin E. C., Frangione B., Pras M. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest. 1972 Oct;51(10):2773–2776. doi: 10.1172/JCI107098. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Levin M., Pras M., Franklin E. C. Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component. J Exp Med. 1973 Aug 1;138(2):373–380. doi: 10.1084/jem.138.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Levin M., Pras M., Franklin E. C. Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component. J Exp Med. 1973 Aug 1;138(2):373–380. doi: 10.1084/jem.138.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Linke R. P., Heilmann K. L., Nathrath W. B., Eulitz M. Identification of amyloid A protein in a sporadic Muckle-Wells syndrome. N-terminal amino acid sequence after isolation from formalin-fixed tissue. Lab Invest. 1983 Jun;48(6):698–704. [PubMed] [Google Scholar]
  34. Linke R. P., Heilmann K. L., Nathrath W. B., Eulitz M. Identification of amyloid A protein in a sporadic Muckle-Wells syndrome. N-terminal amino acid sequence after isolation from formalin-fixed tissue. Lab Invest. 1983 Jun;48(6):698–704. [PubMed] [Google Scholar]
  35. Maury C. P., Alli K., Baumann M. Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. FEBS Lett. 1990 Jan 15;260(1):85–87. doi: 10.1016/0014-5793(90)80072-q. [DOI] [PubMed] [Google Scholar]
  36. Maury C. P., Alli K., Baumann M. Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. FEBS Lett. 1990 Jan 15;260(1):85–87. doi: 10.1016/0014-5793(90)80072-q. [DOI] [PubMed] [Google Scholar]
  37. Nichols W. C., Dwulet F. E., Liepnieks J., Benson M. D. Variant apolipoprotein AI as a major constituent of a human hereditary amyloid. Biochem Biophys Res Commun. 1988 Oct 31;156(2):762–768. doi: 10.1016/s0006-291x(88)80909-4. [DOI] [PubMed] [Google Scholar]
  38. Nichols W. C., Dwulet F. E., Liepnieks J., Benson M. D. Variant apolipoprotein AI as a major constituent of a human hereditary amyloid. Biochem Biophys Res Commun. 1988 Oct 31;156(2):762–768. doi: 10.1016/s0006-291x(88)80909-4. [DOI] [PubMed] [Google Scholar]
  39. Nordlie M., Sletten K., Husby G., Ranløv P. J. A new prealbumin variant in familial amyloid cardiomyopathy of Danish origin. Scand J Immunol. 1988 Jan;27(1):119–122. doi: 10.1111/j.1365-3083.1988.tb02329.x. [DOI] [PubMed] [Google Scholar]
  40. Nordlie M., Sletten K., Husby G., Ranløv P. J. A new prealbumin variant in familial amyloid cardiomyopathy of Danish origin. Scand J Immunol. 1988 Jan;27(1):119–122. doi: 10.1111/j.1365-3083.1988.tb02329.x. [DOI] [PubMed] [Google Scholar]
  41. Parmelee D. C., Titani K., Ericsson L. H., Eriksen N., Benditt E. P., Walsh K. A. Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein. Biochemistry. 1982 Jul 6;21(14):3298–3303. doi: 10.1021/bi00257a008. [DOI] [PubMed] [Google Scholar]
  42. Parmelee D. C., Titani K., Ericsson L. H., Eriksen N., Benditt E. P., Walsh K. A. Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein. Biochemistry. 1982 Jul 6;21(14):3298–3303. doi: 10.1021/bi00257a008. [DOI] [PubMed] [Google Scholar]
  43. Prusiner S. B., Groth D. F., Bolton D. C., Kent S. B., Hood L. E. Purification and structural studies of a major scrapie prion protein. Cell. 1984 Aug;38(1):127–134. doi: 10.1016/0092-8674(84)90533-6. [DOI] [PubMed] [Google Scholar]
  44. Prusiner S. B., Groth D. F., Bolton D. C., Kent S. B., Hood L. E. Purification and structural studies of a major scrapie prion protein. Cell. 1984 Aug;38(1):127–134. doi: 10.1016/0092-8674(84)90533-6. [DOI] [PubMed] [Google Scholar]
  45. Saraiva M. J., Birken S., Costa P. P., Goodman D. S. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest. 1984 Jul;74(1):104–119. doi: 10.1172/JCI111390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Saraiva M. J., Birken S., Costa P. P., Goodman D. S. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest. 1984 Jul;74(1):104–119. doi: 10.1172/JCI111390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Sletten K., Westermark P., Natvig J. B. Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid. J Exp Med. 1976 Apr 1;143(4):993–998. doi: 10.1084/jem.143.4.993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Sletten K., Westermark P., Natvig J. B. Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid. J Exp Med. 1976 Apr 1;143(4):993–998. doi: 10.1084/jem.143.4.993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S. Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Commun. 1983 Nov 15;116(3):880–888. doi: 10.1016/s0006-291x(83)80224-1. [DOI] [PubMed] [Google Scholar]
  50. Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S. Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Commun. 1983 Nov 15;116(3):880–888. doi: 10.1016/s0006-291x(83)80224-1. [DOI] [PubMed] [Google Scholar]
  51. Westermark P., Sletten K., Johansson B., Cornwell G. G., 3rd Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2843–2845. doi: 10.1073/pnas.87.7.2843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Westermark P., Sletten K., Johansson B., Cornwell G. G., 3rd Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2843–2845. doi: 10.1073/pnas.87.7.2843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Westermark P., Wernstedt C., Wilander E., Sletten K. A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem Biophys Res Commun. 1986 Nov 14;140(3):827–831. doi: 10.1016/0006-291x(86)90708-4. [DOI] [PubMed] [Google Scholar]
  54. Westermark P., Wernstedt C., Wilander E., Sletten K. A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem Biophys Res Commun. 1986 Nov 14;140(3):827–831. doi: 10.1016/0006-291x(86)90708-4. [DOI] [PubMed] [Google Scholar]

Articles from Bulletin of the World Health Organization are provided here courtesy of World Health Organization

RESOURCES