Skip to main content
SpringerLink
Log in

Diagnosis of the type of amyloid in paraffin wax embedded tissue sections using antisera against human and animal amyloid proteins

  • Published:
Virchows Archiv A Aims and scope Submit manuscript

Summary

Different histochemical techniques were compared on paraffin wax embedded tissue sections for routine classification of amyloid; the following methods were used: potassium permanganate, the indirect immunoperoxidase method using polyclonal anti-human amyloid antisera (anti-AA, anti-Aλ, anti-Aκ and anti-AF) and the peroxidase-antiperoxidase (PAP) method using antisera against human, bovine, hamster and canine AA amyloid. Anti-human AA antiserum appeared to be a useful tool in this respect. Polyclonal anti-AL antisera may be helpful in diagnosing AL amyloid, but were of less value than anti-AA serum.

Strong cross reactivity between anti-bovine AA antiserum and human AA amyloid deposits was found. This indicates that animal amyloid AA antisera can also be used for the diagnosis of AA amyloid in human tissues.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Antonutto G, Bartoli M, Melato M (1975) Histochemical study on systemic amyloid microdeposits with special reference to parathyroid intra-follicular deposits. Virch Arch [Pathol Anat] 368:23–34

    Google Scholar 

  • Bausserman LL, Herbert PN, McAdam KPWJ (1980) Heterogeneity of human serum amyloid A protein. J Exp Med 152:641–656

    Google Scholar 

  • Bausserman LL, Saritelli AL, Herbert PN, McAdam KPWJ, Schulman RS (1982) NH2-terminal analysis of four of the polymorphic forms of human serum amyloid A protein. Biochem Biophys Acta 704:556–559

    Google Scholar 

  • Benditt EP, Eriksen N (1977) A protein SAA is associated with high density lipoprotein from human serum. Proc Natl Acad Sci USA 74:4025–4028

    Google Scholar 

  • Cooper JH (1975) Histochemical properties of pancreatic-insular amyloid. Lab Invest 32:421

    Google Scholar 

  • Cornwell GG, Husby G, Westermark P, Natvig JB, Michaelsen TE, Skogen B (1977) Identification and characterization of different amyloid fibril proteins in tissue sections. Scand J Immunol 6:1071–1080

    Google Scholar 

  • Doepel FM, Glorioso JL, Newcomer CE, Skinner M, Abrams GD (1981) Enzyme-linked immunosorbent assay of serum protein SAA in Rhesus monkeys with secondary amyloidosis. Lab Invest 45:7–13

    Google Scholar 

  • Dwulet FE, Benson MD (1984) Primary structure of an amyloid prealbumin and its plasma precursor in a heredo-familial polyneuropathy of Swedish origin. Proc Natl Acad Sci USA 81:694–698

    Google Scholar 

  • Eriksen N, Benditt EP (1980) Isolation and characterization of the amyloid-related apoprotein (SAA) from human high density lipoprotein. Proc Natl Acad Sci USA 77:6860–6864

    Google Scholar 

  • Eriksen N, Benditt EP (1984) Trauma, high density lipoprotein and serum amyloid protein A. Clin Chem Acta 140:139–149

    Google Scholar 

  • Eriksen N, Ericssen LH, Pearsall N, Lagunoff D, Benditt EP (1976) Mouse amyloid protein AA: homology with non-immunoglobulin protein of human and monkey amyloid substance. Proc Natl Acad Sci USA 73:964–967

    Google Scholar 

  • Franklin EC (1980) Immunopathology of the amyloid diseases. Hosp Pract 15:70–77

    Google Scholar 

  • Franklin EC, Gorevic PD (1980) The amyloid diseases. In: Fougereau M, Dausset J (eds) Progress in immunology IV, vol. 3. Academic Press, New York, pp 1219–1229

    Google Scholar 

  • Fujihara S, Balow JE, Costa JC, Glenner GG (1980) Identification and classification of amyloid in formalin fixed, paraffin-embedded tissue sections by the unlabeled immunoperoxidase method. Lab Invest 43:358–365

    Google Scholar 

  • Glenner GG (1980) Amyloid deposits and amyloidosis. Theβ-fibrilloses. New Engl J Med 302:1283–1292 and 1333–1343

    Google Scholar 

  • Glenner GG, Page DL (1976) Amyloid, amyloidosis and amyloidogenesis. Int Rev Exp Pathol 15:1–92

    Google Scholar 

  • Glenner GG, Harada M, Isersky C, Cuatrecasas P, Page D, Keiser H (1970) Human amyloid protein: diversity and uniformity. Biochem Biophys Res Commun 41:1013–1019

    Google Scholar 

  • Glenner GG, Eanes ED, Bladen HA, Linke RP, Termine JD (1974)β-pleated sheet fibrils; a comparison of native amyloid with synthetic protein fibrils. J Histochem Cytochem 22:1141–1158

    Google Scholar 

  • Glenner GG, Costa PP, de Freitas AF (1980) Amyloid and amyloidosis. Excerpta Medica. Amsterdam

  • Gorevic PD, Greenwald M, Frangione B, Pras M, Franklin EC (1977) The amino acid sequence of duck amyloid A (AA) protein. J Immunol 118:1113–1118

    Google Scholar 

  • Gorevic PD, Levo Y, Frangione B, Franklin EC (1978) Polymorphism of tissue and serum amyloid A (AA and SAA) protein in the mouse. J Immunol 121:138–140

    Google Scholar 

  • Gorevic PD, Cleveland AB, Franklin EC (1982) The biologic significance of amyloid. Ann NY Acad Sci USA 389:380–394

    Google Scholar 

  • Gruys E, Timmermans HJF (1979) Diagnosis of secondary amyloid in bovine renal amyloidosis. Vet Sci Commun 3:21–37

    Google Scholar 

  • Gruys E, Biewenga WJ, Hol PR (1981) Canine glomerular amyloidosis. In: Tribe CR, Bacon PA (eds) Amyloidosis E.A.R.S., John Wright and Sons, Bristol., pp 167–171

    Google Scholar 

  • Hind CR, Tennent GA, Evans DJ, Pepys MB (1983) Demonstration of amyloid A (AA) protein and amyloid P component (AP) in deposits of systemic amyloidosis associated with renal adenocarcinoma. J Pathol 139:159–166

    Google Scholar 

  • Hoffman JS, Benditt EP (1982) Changes in high density lipoprotein content following endotoxin administration in the mouse. Formation of serum amyloid protein rich subfractions. J Biol Chemn 257:10510–10517

    Google Scholar 

  • Hoffman JS, Ericsson LH, Eriksen N, Walsh KA, Benditt EP (1984) Murine tissue amyloid protein AA; NH2-terminal sequence identity with only one of two serum amyloid protein (Apo SAA) gene products. J Exp Med 159:641–646

    Google Scholar 

  • Hol PR, Gruys E (1985) Amyloid A protein in different species. Appl Pathol (in press)

  • Hol PR, Langeveld JPM, van Beuningen-Jansen EW, Veerkamp JH, Gruys E (1984) A second component in bovine AA amyloid fibrils not identical with protein AA is essential for AA amyloid fibrillogenesis. Scand J Immunol 20:53–60

    Google Scholar 

  • Holmes EJ (1977) Crystalloids of prostatic carcinoma: relationship to Bence Jones crystals. Cancer 39:2073–2080

    Google Scholar 

  • Husby G, Natvig JB, Harboe M (1974) The occurence in sera with M-components of different proteins related to amyloid fibrils. Scand J Immunol 3:391–396

    Google Scholar 

  • Isobe T, Osserman EF (1974) Patterns of amyloidosis and their association with Plasma-cell dyscrasia, monoclonal immunoglobulins and Bence Jones proteins. N Engl J Med 290:473–477

    Google Scholar 

  • Isobe T, Tomita M, Matsumoto J, Fujita T (1983) Plasma cell dyscrasia in 105 Japanese patients with systemic amyloidosis. Jpn J Med 22:117–121

    Google Scholar 

  • Linder E, Westermark P (1981) Presence of complement Clg in cardiac amyloid. In: Tribe CR, Bacon PA (eds) Amyloidosis E.A.R.S., John Wright and Sons, Bristol, pp 39–42

    Google Scholar 

  • Linke RP (1982) Immunohistochemical identification and cross reactions of amyloid fibril proteins in senile heart and amyloid in familial polyneuropathy. Lack of reactivity with cerebral amyloid in Alzheimer's disease. Clin Neuropathol 1:172–182

    Google Scholar 

  • Linke RP (1984) Monoclonal antibodies against amyloid fibril protein AA. Production, specificity, and use for immunohistochemical localization and classification of AA type amyloidosis. J Histochem Cytochem 32:322–328

    Google Scholar 

  • Linke RP, Nathrath WB (1982) Immunochemical typing of amyloid from tissue biopsies. Acta Histochem 25:89–93

    Google Scholar 

  • Linke RP, Sipe JD, Pollock PS, Ignaczak TF, Glenner GG (1975) Isolation of a low-molecular weight serum component antigenetically related to an amyloid fibril protein of unknown origin. Proc Natl Acad Sci USA 72:1473–1476

    Google Scholar 

  • Linke RP, Karg O, Nathrath W (1981) Immunochemische Klassifizierung yon Amyloid-Krankheiten an der Biopsie: Mikroextraktion an nativem Material und Immunoperoxidasetechnik an Kryostat- und Paraffingewebeschnitten. Zentrbl Allg Pathol 125:285

    Google Scholar 

  • Linke RP, Heilman KL, Nathrath WBJ, Eulitz M (1983) Identification of amyloid A protein in a sporadic Muckle-Wells syndrome. N-terminal amino acid sequence after isolation from formaline fixed tissue. Lab Invest 48:698–704

    Google Scholar 

  • Linke RP, Nathrath WBJ, Eulitz M (1984a) Classification of amyloid syndromes from tissue sections using antibodies against various amyloid fibril proteins: report of 142 cases. Proceedings IVth Internat Syrup on Amyloid, Nov 9–12, 1984, Harriman, Plenum Press, New York (in press)

    Google Scholar 

  • Linke RP, Hol PR, Gruys E, Geisel O, Nathrath WBJ, Trautwein G (1984b) Immunohistochemical identification and cross reactions of amyloid-A fibril protein in man and eleven other species. J Comp Pathol 94:339–356

    Google Scholar 

  • Linke RP, Hol PR, Geisel O (1985) Immunohistochemical identification of generalized AA-amyloidosis in a mountain Gazelle (Gazella gazella) by cross-reaction using monoclonal and polyclonal anti-AA antibodies (submitted)

  • Marhaug G, Børresen AL, Husby G, Nordstoga K (1984) A comparative study of serum amyloid A protein (SAA) from mink and man. Comp Biochem Physiol 78 B:401–406

    Google Scholar 

  • Nathrath WBJ, Wilson PD, Trejdosiewicz LK (1982) Immunohistochemical demonstration of epithelial and urothelial antigens at the light- and electron microscope levels. Acta Histochem 25:73–82

    Google Scholar 

  • Orfila C, Rakotoazivony J, Segonds A (1983) Immunofluorescence study of non-idiopathic renal amyloidosis. Hum Pathol 14:362–367

    Google Scholar 

  • Osserman EF (1961 a) The plasmacytic dyscrasias: plasma cell myeloma and primary macroglobulineaemia. Am J Med 31:671–675

    Google Scholar 

  • Osserman EF (1961 b) Amyloidosis: tissue proteinosis: gammaloidosis. Ann Intern Med 55:1033–1036

    Google Scholar 

  • Romhanyi G (1971) Selective differentiation between amyloid and connective tissue structures based on the collagen specific topo-optical staining reaction with Congo red. Virchows Arch [Pathol Anat] 354:209–222

    Google Scholar 

  • Romhanyi G (1972) Differences in ultrastructural organization of amyloid as revealed by sensitivity or resistance to induced proteolysis. Virchows Arch [Pathol Anat] 357:29–52

    Google Scholar 

  • Saraiva MJ, Costa PP, Birksen S, Goodman DS (1983) Presence of an abnormal transthyretin (prealbumin) in Portugese patients with familial amyloidotic polyneuropathy. Trans Assoc Am Physicians 96:261–270

    Google Scholar 

  • Shirahama T, Skinner M, Cohen AS (1981) Immunocytochemical identification of amyloid in formalin-fixed paraffin sections. Histochemistry 72:161–171

    Google Scholar 

  • Solomon A, Frangione B, Franklin EC (1982) Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (VI). J Clin Invest 70:453–460

    Google Scholar 

  • Sternberger LA (1979) Immunocytochemistry, Ed 2, John Wiley and Sons, Inc, New York, p 104

    Google Scholar 

  • Stokes G (1976) An improved Congo red method for amyloid. Med Lab Sci 33:79–80

    Google Scholar 

  • Takahashi N, Page D, Inagami T, Tashjia A (1977) Characterization of amyloid associated peptides from medullary thyroid carcinoma. Fed Proc 36:369

    Google Scholar 

  • Tawara S, Nakazato M, Kangawa Matsuo H, Araki S (1983) Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Jap. type). Biochem Biophys Res Commun 116:880–888

    Google Scholar 

  • Van Rijswijk MH, van Heusden CWGJ (1979) The potassium permangangate method. A reliable method for differentiating amyloid AA from other forms of amyloid in routine laboratory practice. Am J Pathol 97:43–58

    Google Scholar 

  • Waalen K, Sletten K, Husby G, Nordstoga K (1980) The primary structure of protein AA in endotoxin-induced amyloidosis of the mink. Eur J Biochem 104:407–412

    Google Scholar 

  • Westermark P (1974) The pancreatic islets in systemic amyloidosis. The occurrence of two different types of amyloid. Virchows Arch [Pathol Anat] 363:179–182

    Google Scholar 

  • Westermark P, Wilander E (1983) Islet amyloid in type 2 (non-insulin-dependent) diabetes is related to insulin. Diabetologia 24:342–346

    Google Scholar 

  • Westermark P, Grimelius L, Polak JM, Hanssen LJ, Van Noorden S, Wilander E, Pearse AGE (1977) Amyloid in polypeptide hormone-producing tumors. Amyloid tumor hormone formation. Lab Invest 37:212–215

    Google Scholar 

  • Westermark P, Sletten K, Eriksson M (1979) Morphologic and Chemical variation of the kidney lesions in amyloidosis secondary to rheumatoid arthritis. Lab Invest 41:427–431

    Google Scholar 

  • Westermark P, Sletten K, Natvig JB (1981) Structure and antigenic behaviour of kappe limmunoglobulin light-chain amyloid proteins. Acta Path Microbiol Scand 89:199–203

    Google Scholar 

  • Westermark P, Pitkanen P, Cornwell GG (1983) Amyloidosis of the seminal vesicles. The distinctive form of senile amyloidosis. In: Tribe CR, Bacon PA (eds) Amyloidosis E.A.R.S., John Wright and Sons, Bristol, p 205

    Google Scholar 

  • Wright JR, Calkins E, Humphrey RL (1977) Potassium permanganate reaction in amyloidosis. A histologic method to assist in differentiating forms of this disease. Lab Invest 36:274–281

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Pathology, State University of Utrecht, Pasteurstraat 2, 3511 HX, Utrecht, The Netherlands

    Christina A. van de Kaa, Johannes Huber & Cees J. Kooiker

  2. Department of Veterinary Pathology, State University of Utrecht, Yalelaan 1, 3508 TD, Utrecht, The Netherlands

    Paul R. Hol & Erik Gruys

  3. Institute of Immunology, University of Munich, D-8000, Munich, Germany

    Reinhold P. Linke

Authors
  1. Christina A. van de Kaa
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Paul R. Hol
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Johannes Huber
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Reinhold P. Linke
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Cees J. Kooiker
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Erik Gruys
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

This study was funded by the Division of Rheumatology, A.Z.U., the Netherlands League against Rheumatism and Sonderforschungsbereich 0207 (Project C6), München

Rights and permissions

Reprints and permissions

About this article

Cite this article

van de Kaa, C.A., Hol, P.R., Huber, J. et al. Diagnosis of the type of amyloid in paraffin wax embedded tissue sections using antisera against human and animal amyloid proteins. Vichows Archiv A Pathol Anat 408, 649–664 (1986). https://doi.org/10.1007/BF00705343

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00705343

Key words

Search

Navigation