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Immunoglobulin lambda-light-chain-derived amyloidosis (Aλ) in two horses

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Summary

Tumorous amyloid deposits in the nasal mucosa of two horses differed from generalized AA-amyloidosis with respect to clinical features, organ distribution, and resistance to KMnO4 treatment. Using a panel of antibodies directed against different human amyloid fibril proteins and employing the peroxidase-anti-peroxidase (PAP) technique, we showed the described equine amyloid to be Aλ-type, as demonstrated by immunohistochemical cross-reactivity. Consequently, we identified a second amyloid class in horses and showed that immunoglobulin light-chain-derived amyloid may also be present in animals.

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References

  1. Chai CK, Lerner C (1984) Amyloidosis development in LLC mice. Exp Cell Biol 52: 339–346

    Google Scholar 

  2. Conner MW, Conner BH, Fox JG, Rogers AE. (1983) Spontaneous amyloidosis in outbred CD-1 mice. Surv Synth Pathol Res 1: 67–78

    Google Scholar 

  3. Dill GS, Stookey JL, Whitney GD (1972) Nodular amyloidosis in the trachea of a dog. Vet Pathol 9: 238–242

    Google Scholar 

  4. Geisel O, Linke RP (1988) Generalized AA-amyloidosis in two hares (Lepus europaeus) immunohistochemically identified using poly- and monoclonal antibodies. Vet Pathol 25: 391–393

    Google Scholar 

  5. 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 

  6. Grawitz P (1883) Amyloidose der oberen Luftwege des Pferdes. Virchows Arch [Pathol Anat] 94: 279–289

    Google Scholar 

  7. Hjärre A (1933) Über das Vorkommen der Amyloid-Degeneration bei Tieren. Acta Pathol Microbiol Scand [Suppl] 16: 132–162

    Google Scholar 

  8. Hjärre A (1942) Über Amyloidose bei Tieren mit besonderer Berücksichtigung atypischer Formen. Berl Münch tierärztl Wochenschr 45: 331–334

    Google Scholar 

  9. Husebekk A, Husby G, Sletten K, Marhaug G, Nordstoga K (1986) Characterization of amyloid protein AA and its serum precursor SAA in the horse. Scand J Immunol 23: 703–709

    Google Scholar 

  10. Jacob W (1971) Spontaneous amyloidosis in mammals Vet Pathol 8: 292–306

    Google Scholar 

  11. Karg O, Linke RP, Götz R (1981) Amyloidablagerungen im Respirationstrakt: Falldemonstration. Prax Pneumol 35: 973–975

    Google Scholar 

  12. 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 

  13. 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 

  14. Linke RP (1985) Immunochemical typing of amyloid deposits after microextraction from biopsies. Appl Pathol 3: 18–28

    Google Scholar 

  15. Linke RP, Hol RP, Geisel O (1986) Immunohistochemical identification of generalized AA-amyloidosis in a mountain gazelle (Gazella gazella). Vet Pathol 23: 63–67

    Google Scholar 

  16. Linke RP, Nathrath WBJ, Eulitz M (1986) Classification of amyloid syndromes from tissue section using antibodies against various amyloid fibril proteins: report of 142 cases. In: Glenner GG, Osserman EF, Benditt EP, Calkins E, Cohen AS, Zucker-Franklin D (eds) Amyloidosis. Plenum Press, New York London, pp 599–605

    Google Scholar 

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

    Google Scholar 

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

    Google Scholar 

  19. McAlpine JC, Fuller AP (1964) Localized laryngeal amyloidosis: a report of a case with a review of the literature. J Laryngol Otol 78: 296–314

    Google Scholar 

  20. Pospischil A, Hänichen T, Linke RP (1987): Amyloidbildende Carcinoide der Mamma bei zwei Hündinnen. Tierärztl Umschau 42: 783–788

    Google Scholar 

  21. Puchtler H, Sweat F, Levin M (1962) On the binding of Congo red by amyloid. J Histochem Cytochem 10, 335–364

    Google Scholar 

  22. Scheinberg MA, Cathcart ES, Eastcott JW, Skinner M, Benson M, Shirahama T, Bennett M (1976) The SJL/J mouse: a new model for spontaneous age-associated amyloidosis. Lab Invest 35: 47–54

    Google Scholar 

  23. Stünzi H, Ehrensperger R, Wild P, Leeman W (1975) Systemische Haut- und Unterhautamyloidose beim Pferd. Vet Pathol 12: 405–414

    Google Scholar 

  24. Toygarli SA (1953) Lokale, blastomatöse Amyloidose der Nasenschleimhaut beim Pferd. Deutsch Tierärztl Wochenschr 60: 372–372

    Google Scholar 

  25. Van de Kaa CA, Hol PR, Huber J, Linke RP, Kooiker CJ, Gruys E (1986) Diagnosis of the type of amyloid in paraffin wax embedded tissue sections using antisera against human and animal amyloid proteins. Virchows Arch [Pathol Anat] 408: 649–664

    Google Scholar 

  26. Westermark P, Sletten K, Pitkänen Natvig JB, Lindholm CE (1982) Localized laryngeal amyloidosis: partial characterization of an amyloid fibril protein AL. Mol Immunol 19: 447–450

    Google Scholar 

  27. Westermark P, Wernstedt T, O'Brien TO, Hayden DW, Johnson KG (1987) Islet amyloid in type 2 diabetes mellitus and adult diabetic cats contain a novel putative polypeptide hormone. Am J Pathol 127: 414–417

    Google Scholar 

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

    Google Scholar 

  29. Yonezu T, Higuchi K, Tsunasawa S, Takagi S, Sakiyama F, Takeda T (1986) High homology is present in the primary structures between murine senile amyloid protein (ASSAM) and human apolipoprotein A-II. FEBS Lett 203: 149–152

    Google Scholar 

  30. Zschiesche W, Linke RP (1989) Immunohistochemical characterizatin of spontaneous amyloidosis in captive birds as AA-type, using monoclonal and polyclonal anti-AA antibodies against mammalian amyloid. Acta Histochem (in press)

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Authors and Affiliations

  1. Institut für Immunologie der Universität München, Goethestrasse 31, D-8000, München 2, Germany

    Reinhold P. Linke

  2. Institut für Pathologie, Tierärztliche Hochschule, Bischofshofener Damm 15, D-3000, Hannover, Germany

    Gerhard Trautwein

Authors
  1. Reinhold P. Linke
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  2. Gerhard Trautwein
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Linke, R.P., Trautwein, G. Immunoglobulin lambda-light-chain-derived amyloidosis (Aλ) in two horses. Blut 58, 129–132 (1989). https://doi.org/10.1007/BF00320431

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  • DOI: https://doi.org/10.1007/BF00320431

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