References
- Frederik II of Hohenstaufen. De arte venandi cum avibus. Bibliotheca Vaticana, Pal. lat 1071; f79v/80v
- Benditt E P, Eriksen N. Chemical classes of amyloid substance. Am J Pathol 1971; 65: 231–249
- Glenner G G. Amyloid deposits and amyloidosis. The β-fibrillosis. N Engl J Med 1980; 302: 1283–1292, (see also 1333–1343)
- Buxbaum J N. The systemic amyloidosis. Curr Opin Rheumatol 2004; 16: 67–75
- Merlini G, Westermark P. The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies. J Intern Med 2004; 255: 159–178
- Jakob W. Spontaneous amyloidosis of mammals. Vet Pathol 1971; 8: 292–306
- Linke R P, Hol P R, Gruys E, Geisel O, Nathrath W B, Trautwein G. Immunohistochemical identification and crossreactions of amyloid-A fibril protein in man and eleven other species. J Comp Pathol 1984; 94: 339–356
- Zschiesche W, Jakob W. Pathology of animal amyloidosis. Pharmacology 1989; 41: 49–83
- Xing Y, Higuchi K. Amyloid fibrils proteins. Mech Age Dev 2002; 123: 1625–l636
- Gruys E. Protein folding pathology in domestic animals. J Zhejiang Univ Sci 2004; 10: 1226–1238
- Puchtler H, Sweat F, Levine M. On the binding of Congo red by amyloid. J Histochem Cytochem 1962; 10: 355–364
- Husby G, Marhaug G, Dowton B, Sletten K, Sipe J D. Serum amyloid A (SAA): biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid Int J Exp Clin Invest 1994; 1: 119–137
- Lachmann H J, Goodman H J, Gilbertson J A, Gallimore J R, Sabin C A, Gillmore J D, Hawkins P N. Natural history and outcome of AA amyloidosis. N Engl J Med 2007; 356: 2361–2371
- Westermark P, Johnson K H, Sletten K, Hayden D W. AA-amyloidosis in dogs: partial amino acid sequence of protein AA and immunohistochemical cross-reactivity with human and cow AA-amyloid. Comp Biochem Physiol 1985; 82: 211–215
- Colbatzky F, Brunnberg L, Linke R P, Geisel O, Hermanns W. AA-like amyloid deposits confined to arthritic joints in two dogs with rheumatoid arthritis. J Comp Pathol 1991; 105: 331–343
- Niewold T A, van der Linde-Sipman J S, Murphy C, Tooten P C, Gruys E. Familial amyloidosis in cats: Siamese and Abyssinian AA-proteins differ in primary sequence and pattern of deposition. Amyloid Int J Exp Clin Invest 1999; 6: 205–209
- Johnson K H, Sletten K, Werdin R E, Westermark G T, O'Brien T D, Westermark P. Amino acid sequence variations in protein AA of cats with high and low incidences of AA amyloidosis. Comp Biochem Physiol 1989; 94: 765–768
- Bergstrom J, Ueda M, Une Y, Sun X, Misumi S, Shoji S, Ando Y. Analysis of amyloid fibrils in the cheetah (Acinonyx jubatus). Amyloid J Protein Fold Disord 2006; 13: 93–98
- Hol P R, Langevrld J P, van Beuningen-Jansen E W, Veerkamp J H, Gruys E. A second component in bovine AA-amyloid fibrils not identical with protein AA is essential for AA-amyloid fibrillogenesis. Scand J Immunol 1984; 20: 53–60
- Tojo K, Tokuda T, Hoshii Y, Fu X, Higuchi K, Matsui T, Kametani F, Ikeda S. Unexpectedly high incidence of visceral AA-amyloidosis in slaughtered cattle in Japan. Amyloid J Protein Fold Disord 2005; 12: 103–108
- Syversen P V, Juul J, Marhaug G, Husby G, Sletten K. The primary structure of serum amyloid A protein in sheep. Comparison with serum amyloid A in other species. Scand J Immunol 1994; 39: 88–94
- Fernandez A, Mensua C, Biescas E, Lujan L. Clinicopathological features in ovine AA amyloidosis. Res Vet Sci 2003; 75: 203–220
- Niewold T A, Murphy C L, Toussaint M J, Solomon A, Gruys E. Chemical typing of porcine systemic amyloid as AA-amyloid. Amyloid J Protein Fold Disord 2005; 12: 164–166
- Sletten K, Husebekk A, Husby G. The amino acid sequence of an amyloid fibril protein AA isolated from the horse. Scand J Immunol 1987; 26: 79–84
- Geisel O, Linke R P. Generalized AA-amyloidosis in two hares (Lepus europaeus) immunohistochemically identified using poly- and monoclonal antibodies. Vet Pathol 1988; 25: 391–393
- Shtrasburg S, Gal R, Gruys E, Perl S, Martin B M, Kaplan B, Koren R, Nyska A, Pras M, Livneh A. An ancillary tool for the diagnosis of amyloid A amyloidosis in a variety of domestic and wild animals. Vet Pathol 2005; 42: 132–139
- Gorevic P D, Greenwald M, Frangione B. The amino acid sequence of duck amyloid A protein. J Immunol 1977; 118: 1113–1118
- Ericsson L H, Eriksen N, Walsh K A, Benditt E P. Primary structure of duck amyloid protein A. The form deposited in tissues may be identical to its serum precursor. FEBS Lett 1987; 218: 11–16
- Guo J T, Aldrich C E, Mason W S, Pugh J C. Characterization of serum amyloid A protein mRNA expression and secondary amyloidosis in the domestic duck. Proc Natl Acad Sci USA 1996; 93: 14548–14553
- Kovacs B M, Szilagy L, Janan J, Rudas P. Serum amyloid A in geese; cloning and expression of recombinant protein. Amyloid J Protein Fold Disord 2005; 121: 109–114
- Landmann W JM, Sletten K, Koch C A, Tooten P C, Gruys E. Chicken joint amyloid protein is of Type AA: characterization of the amyloid protein. Scand J Immunol 1996; 43: 210–230
- Zschiesche W, Linke R P. Immunohistochemical characterization of spontaneous amyloidosis in captive birds as AA-type, using monoclonal and polyclonal anti-AA-antibodies against mammalian amyloid. Acta Histochem 1989; 86: 45–50
- Zoellner A. Untersuchungen zur Amyloidose bei Zoo- und Wildvoegeln, sowie zur histo- und immunohistologischen Charakterisierung des aviaeren Amyloidproteins. Doctoral thesis, Freie Universitaet Berlin, Germany 1997
- Ippen R, Schroeder H-D. Ein Beitrag zu den Erkrankungen der Zoovoegel. Verhandlungsberichte Erkrankungen der Zootiere 1972; 14: 11–27
- Romeis. Mikroskopische Technik. Hrsg. P.Boeck 1989; 17, Auflage
- Linke R P. Highly sensitive diagnosis of amyloid and various amyloid syndromes using Congo red fluorescence. Virchows Arch 2000; 436: 439–448
- Linke R P. Monoclonal antibodies against amyloid fibril protein AA. Production, specificity and use for immunhistochemical localization and classification of AA-type amyloidosis. J Histochem Cytochem 1984; 32: 322–328
- Linke R P, Oos R, Wiegel N, Nathrath W BJ. Classification of amyloidosis: misdiagnosis by way of incomplete immunohistochemistry and how to prevent it. Acta Histochem 2006; 108: 197–208
- Linke R P, Geisel O, Mann K. Equine cutaneous amyloidosis derived from an immunoglobulin lambda-light chain. Immunohistochemical, immunochemical and chemical results. Biol Chem Hoppe Seyler 1990; 372: 835–843
- Platz S J, Breuer W, Geisel O, Linke R P, Hermanns W. Identification of lambda light chain amyloid in eight canine and two feline extramedullary plasmacytomas. J Comp Pathol 1997; 116: 45–54
- Rowland P H, Linke R P. Immunohistochemical characterization of lamda light-chain-derived Amyloid in one feline and five canine plasma cell tumors. Vet Pathol 1994; 31: 390–393
- Linke R P, Heilmann K L, Nathrath W BJ, Eulitz M. Identification of amyloid A protein in a sporadic Muckle-Wells syndrome. N-terminal amino acid sequence analysis after isolation from formalin-fixed tissue. Lab Invest 1983; 48: 698–704
- Hashimoto F, Horigome T, Kanbayashi M, Yoshida K, Sugano H. An improved method for separation of low-molecular-weight polypeptides by electrophoresis in sodium dodecyl sulphate-polyacrylamide gel. Anal Biochem 1983; 129: 192–199
- Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1992; 76: 4350–4354
- Eckerskorn C, Lottspeich F. Internal amino acid sequence analysis of proteins separated by gel electrophoresis after tryptic digestion in polyacrylamide matrix. Chromatographia 1989; 28: 92–94
- Patterson S D. From electrophoretically separated protein to identification: strategies for sequence and mass analysis. Anal Biochem 1994; 221: 1–15
- Edman P, Begg G. A protein sequenator. Eur J Biochem 1967; 1: 80–91
- Altschul S F, Madden T L, Schäffer A A, Zhang J, Zhang Z, Miller W, Lipman D J. ‘Gapped BLAST and PSI-BLAST’: a new generation of protein database search programs. Nucleic Acids Res 1997; 25: 3389–3402
- Ogata F. Quantitative dot-blot enzyme immunoassay for serum amyloid A protein. J Immunol Methods 1989; 116: 131–135
- Pras M, Schubert M, Zucker-Franklin D, Rimon A, Franklin E C. The characterization of soluble amyloid prepared in water. J Clin Invest 1968; 47: 924–933
- Zar J H. Biostatistical analysis. Prentice-Hall Int, Upper Saddle River, NJ 1996
- Rozsal L, Reiczigel J, Majoros G. Quantifying parasites in samples of hosts. J Parasitol 2000; 86: 228–232
- Wright J R, Calkins E, Humphrey R L. Potassium permanganate reaction in Amyloidosis. A histological method to assist in differentiating forms of this disease. Lab Invest 1977; 36: 274–281
- Levin M, Franklin E C, Frangione B, Pras M. The amino acid sequence of major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest 1972; 51: 2773–2776
- Harr K E. Clinical chemistry of companion avian species: a review. Vet Clin Pathol 2002; 31: 140–151
- Papendick R E, Munson L, O'Brien T D, Johnson K H. Systemic AA amyloidosis in captive cheetahs (Acinonyx jubatus). Vet Pathol 1997; 34: 549–556
- Murphy J C, Fox J G, Niemi S M. Nephrotic syndrome associated with renal amyloidosis in a colony of Syrian hamsters. J Vet Med Assoc 1984; 185: 1359–1362
- Hayden D W, Johnson K H, Wolf C B, Westermark P. AA amyloid-associated gastroenteropathy in a horse. J Comp Pathol 1988; 98: 195–204
- Wien T N, Sørby R, Omtvedt L A, Landsverk T, Husby G. Kinetics of glysaminoglycan deposition in splenic AA amyloidosis induced in mink. Scand J Immunol 2004; 60: 600–608
- DiBartola S P, Tarr M J, Webb D M, Giger U. Familial renal amyloidosis in Chinese Shar Pei dogs. J Am Vet Med Assoc 1990; 197: 483–487
- Buxbaum J N, Tagoe C E. The genetics of the amyloidosis. Annu Rev Med 2000; 51: 543–569
- Benson M D. The hereditary amyloidosis. Best Pract Res Clin Rheumatol 2003; 17: 909–927
- Buxbaum J N. The systemic amyloidoses. Curr Opin Rheumatol 2004; 16: 67–75
- Hull K M, Drewe E, Aksentijevich I, Singh H K, Wong K, McDermott E M, Dean J, Powell R J, Kastner D L. The TNF receptor-associated periodic syndrome (TRAPS). Emerging concepts of an autoinflammatory disorder. Medicine 2002; 81: 349–368
- Elliott-Bryant R, Cathcart E S. Amyloid enhancing factor and dietary transmission in accelerated amyloid A amyloidosis. Clin Immunol Immunopathol 1998; 88: 65–69
- Landmark K, Westermark G T, Nyström S, Murphy C L, Solomon A, Westermark P. Transmissibility of systemic amyloidosis by a prion-like mechanism. Proc Natl Acad Sci USA 2002; 99: 6979–6984
- Gruys E. Inflammatory syndrome of footpaths in puppies and AA-amyloidosis. Vet Rec 1996; 138: 264–268
- Gierse S. Die wichtigsten Infektionskrankheiten bei Falken (Falconidae) und die Bedeutung der Beutevögel als Überträger. Germany 2001, Doctoral Thesis, Universitaet Munich
- Snow A D, Willmer J, Kisilevsky R. Sulfated glycoaminoglycans: a common constituent of all amyloids. Lab Invest 1987; 56: 120–123
- Selinger M J, McAdam K P, Kaplan M M, Sipe J D, Vogel S N, Rosenstreich D L. Monokine-induced synthesis of serum amyloid A protein by hepatocytes. Nature 1980; 285: 498–500
- Urieli-Shoval S, Linke R P, Matzner Y. Expression and function of serum amyloid A, a major acute phase protein, in normal and disease states. Curr Opin Hematol 2000; 7: 64–69
- Gilmore J D, Lovat L B, Persey M R, Pepys M B, Hawkins P N. Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein. Lancet 2001; 358: 24–29
- Hampel M R, Wernery U, Kenne J, Linke R P. AA-amyloidosis in hunting falcons in the United Arab Emirates. Poster No. 54 at the Xth International Symposium on Amyloid and Amyloidosis. April, 18–222004. Tours, France