Avian amyloidosis

Avian Pathology

Volumn 27, Issue 5, 1998, Pages 437-449

  Landman, W J M ^a   Gruys, E ^b   Gielkens, A L J ^c  

^a GD ANIMAL HEALTH   (Netherlands)

^b UTRECHT UNIVERSITY   (Netherlands)

^c WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ANAS; ANATIDAE; ANSER; ANSERIFORMES; AVES; GALLIFORMES;

EID: 0031756457     PISSN: 03079457     EISSN: None     Source Type: Journal    
DOI: 10.1080/03079459808419367     Document Type: Review

References (139)

1. Ali-Khan, Z., Normand, J., Alizadeh-Khiavi, K., Robitaille, Y. & Chronopoulos, S. (1992). Ubiquitin profile and amyloid enhancing factor activity in Alzheimer and 'normal' human brain extracts. Neuroscience Letters, 139, 24-28.
2. Alizadeh-Khiavi, K., Normand, J., Chronopoulos, S., Ali, A. & Ali-Khan, Z. (1992). Amyloid enhancing factor activity is associated with ubiquitin. Virchows Archiv A Pathological Anatomy and Histopathology, 420, 139-148.
3. Alsemgeest, S.P., Lambooy, I.E., Wierenga, H.K., Dieleman, S.J., Meerkerk, B., Van Ederen, A.M. & Niewold, T.A. (1995). Influence of physical stress on the plasma concentration of serum amyloid-A (SAA) and haptoglobin (Hp) in calves. Veterinary Quarterly, 17, 9-12.
4. Anonymous (1997). Dwerggroei toenemend probleem in Duitsland. Ziektebestrijding wordt steeds complexer. Pluimveehouderij, 22, 3.
5. Axelrad, M.A., Kisilevsky, R. & Beswetherick, S. (1975). Acceleration of amyloidosis by synegeneic spleen cells from normal donors. American Journal of Pathology, 78, 277-284.
6. Baba, S., Masago, S.A., Takahashi, T., Kasama, T., Sugimura, H., Tsugane, S., Tsutsui, Y. & Shirasawa, H. (1995). A novel allelic variant of serum amyloid-A, Saa1-gamma. genomic evidence, evolution, frequency, and implication as a risk factor for reactive systemic AA-amyloidosis. Human Molecular Genetics, 4, 1083-1087.
7. Baker, J.R. (1977). The results of post-mortem examination of 132 wild birds. British Veterinary Journal, 133, 327-333.
8. Baltz, M.L., Caspi, D., Hind, C.R.K., Feinstein, A. & Pepys, M.B. (1986). Isolation and characterization of amyloid enhancing factor (AEF). In G.G. Glenner, E.F. Osserman, E.P. Benditt, E. Calkins, A.S. Cohen & D. Zucker-Franklin (Eds) Amyloidosis (pp. 115-121). New York: Plenum Press.
9. Beekes, M., Baldauf, E., Cassens, S., Diringer, H., Keyes, P., Scott, A.C., Wells, G.A., Brown, P., Gibbs Jr., C.J. & Gajdusek, D.C. (1995). Western blot mapping of disease-specific amyloid in various animal species and humans with transmissible spongiform encephalopathies using a high-yield purification method. Journal of General Virology, 76, 2567-2576.
10. Benditt, E.P. & Eriksen, N. (1964). Starch gel electrophoretic analysis of some proteins extracted from amyloid. Archives of Pathology, 78, 28, 325-330.
11. Benditt, E.P. & Eriksen, N. (1977). Amyloid serum protein SAA is associated with high density lipoprotein from human serum. Proceedings of the National Academy of Sciences of the United States of America, 74, 4025-4028.
12. Betts, J.C., Cheshire, J.K., Akira, S., Kishimoto, T. & Woo, P. (1993) The role of NF-Kappa B and NF-IL6 transactivating factors in the synergistic activation of human serum amyloid A gene expression by interleukin-1 and interleukin-6. Journal of Biological Chemistry, 268, 25624-25631.
13. Booth, D.R., Sunde, M., Bellotti, V., Robinson, C.V., Hutchinson, W.L., Fraser, P.E., Hawkins, P.N., Dobson, C.M., Radford, S.E., Blake, C.C.F. & Pepys, M.B. (1997). Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature, 385, 787-793.
14. Brayton, C. (1992). Amyloidosis, haemochromatosis and atherosclerosis in a roseate flamingo (Phoenicopterus ruber). Annals of the New York Academy of Science, 653, 184-190.
15. Brinckerhoff, C.E., Mitchell, T.I., Karmilowicz, M.J., Kluve-Beckerman, B. & Benson, M.D. (1989). Autocrine induction of collagenase by serum amyloid A-like and β2-microglobulin-like proteins. Science, 243, 655-657.
16. Brisette, L., Young, I., Narindrasorasak, S., Kisilevsky, R. & Deely, R. (1989). Differential induction of the serum amyloid gene family in response to an inflammatory agent and to amyloid enhancing factor. Journal of Biological Chemistry, 264, 19327-19332.
17. Bruun, C.F., Rygg, M., Nordstoga, K., Sletten, K. & Marhaug, G . (1994). Serum amyloid A protein in mink during endotoxin induced inflammation and amyloidogenesis. Scandinavian Journal of Immunology, 40, 337-344.
18. Cathcart, E.S., Carreras, I., Elliot-Bryant, R., Liang, J.S., Gonnerman, W.A. & Sipe, J.D. (1996). Polymorphism of acute phase serum amyloid A isoforms and amyloid resistance in wild-type Mus musculus czech. Clinical Immunology and Immunopathology, 81, 22-26.
19. Charge, S.B., Esiri, M.M., Bethune, C.A., Hansen, B.C. & Clark, A. (1996). Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. Journal of Pathology, 179, 443-447.
20. Cohen, A.S. & Calkins, E. (1959). Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature, 183, 1202-1203.
21. Cooper, J.H. (1974). Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods. Laboratory Investigation, 31, 232-238.
22. Cowan, D.F. (1968a). Avian amyloidosis. II. Incidence and contributing factors in the family Anatidae. Pathologia Veterinaria, 5, 59-66.
23. Cowan, D.F. (1968b). Avian amyloidosis. I. General incidence in zoo birds. Pathologia Veterinaria, 5, 51-58.
24. Cowan, D.F. & Johnson, W.C. (1970). Amyloidosis in the white Pekin duck. I. Relation to social environmental stress. Laboratory Investigation, 23, 551-555.
25. Dahlbäck, K., Wulf, H.C. & Dahlbäck, B. (1993). Vitronectin in mouse skin: immunohistochemical demonstration of its association with cutaneous amyloid. Journal of Investigative Dermatology, 100, 166-170.
26. Dalferes Jr., E.R., Ruiz, H., Radhakrishnamurthy, B., Rigdon, R.H. & Berenson, G.S. (1969). Acid mucopolysaccharides in the liver of Pekin duck with amyloidosis. Proceedings of the Society of Experimental and Biological Medicine, 131, 1382-1385.
27. De Beer, F.C., Baltz, M.L., Holford, S., Feinstein, A. & Pepys, M.B. (1981). Fibronectin and C4-binding protein are selectively bound by aggregated amyloid P component. Journal of Experimental Medicine, 154, 1134-1139.
28. Dren, C.N., Nemeth, I., Sari, I., Ratz, F., Glavits, R. & Somogyi, P. (1988). Isolation of a reticuloendotheliosis-like virus from naturally occurring lymphoreticular tumours of domestic goose. Avian Pathology, 17, 259-277.
29. Drueke, T., Touam, M. & Zingraff, J. (1995). Dialysis associated amyloidosis. Advances in Renal Replacement Therapy, 2, 24-39.
30. Druet, R.L. & Janigan, D.T. (1966). Experimental amyloidosis. Amyloid induction with a soluble protein antigen in intact, bursectomized and thymectomized chickens. American Journal of Pathology, 49, 1103-1123.
31. Eanes, E.D. & Glenner, G.G. (1968). X-ray diffraction studies on amyloid filaments. Journal of Histochemistry and Cytochemistry, 16, 673-677.
32. Ericsson, L.H., Eriksen, N., Walsh, K.A. & Benditt, E.P. (1987). Primary structure of duck amyloid protein A: the form deposited in tissues may be identical to its serum precursor. FEBS Letters, 218, 11-16.
33. Eskens, U., Burski, B. & Geisthoevel, E. (1984). Secondary amyloidosis in white Pekin ducks. Tierärztliche Praxis, 12, 469-475.
34. Frankenberger, B., Lottspeich, F. & Linke, R.P. (1993). The monoclonal antibody mc21 recognizes the invariant region of the amyloid A protein. In R. Kisilevsky (Ed.) Proceedings of the 7th International Symposium on Amyloidosis (pp. 46, M16). Kingston, Ontario: Queen's University.
35. Friedreich, N. & Kékulé, A. (1859). Zur Amyloidfrage. Virchows Archiv A für Pathologische Anatomie und Physiologie und Klinische Medizin, 16, 50-65.
36. Gallo, G., Wisniewski, T., Choi-Miura, N., Ghiso, J. & Frangione, B. (1994). Potential role of apoliprotein-E in fibrillogenesis. American Journal of Pathology, 145, 526-530.
37. Glenner, G.G. (1980). Amyloid deposits and amyloidosis. The β-fibrilloses. New England Journal of Medicine, 302, 1283-1292. 1333-1343.
38. Glomset, J.A. (1968). The plasma lecithins: cholesterol acyltransferase reaction. Journal of Lipid Research, 9, 155-156.
39. Gorevic, P.D., Greenwald, M., Frangione, B., Pras, M. & Franklin, E.C. (1977). The amino acid sequence of duck amyloid A (AA) protein. Journal of Immunology, 118, 1113-1118.
40. Gruys, E. & Snel, F.W.J.J. (1994). Animal models for reactive amyloidosis. In G. Husby (Ed.) Baillière's Clinical Rheumatology, 8:3 (pp. 599-611). London: Baillière Tindall.
41. Guo, J.T., Aldrich, C.E., Mason, W.S. & Pugh, J.C. (1996). Characterization of serum amyloid A protein mRNA expression and secondary amyloidosis in the domestic duck. Proceedings of the National Academy of Sciences of the United States of America, 93, 14548-14553.
42. 2+-mediated association of human serum amyloid P component with heparan sulfate and dermatan sulfate. Journal of Biological Chemistry, 262, 2456-2460.
43. Hardt, F. & Ranlov, P. (1976). Transfer amyloidosis. International Review of Experimental Pathology, 16, 273-334.
44. Hawkins, P.N. & Pepys, M.B. (1990). A primed state exits in vivo following histological regression of amyloidosis. Clinical and Experimental Immunology, 81, 325-328.
45. Hawkins, P.N., Richardson, S., Vigushin, D.M., David, J., Kelsey, C.R., Gray, R.E., Hall, M.A., Woo, P., Lavender, J.P. & Pepys, M.B. (1993). Serum amyloid P component scintigraphy turnover studies for diagnosis and quantitative monitoring of AA-amyloidosis in juvenile rheumatoid arthritis. Arthritis and Rheumatism, 36, 842-851.
46. Hjärre, A. (1933). Ueber das Vorkommen der Amyloiddegeneration bei Tieren. Acta Pathologica Microbiologica Scandinavica Supplementum, 16, 132-162.
47. Hoffman, J.S. & Benditt, E.P. (1982a). Changes in high-density lipoprotein content following endotoxin administration in the mouse. Formation of serum amyloid protein-rich subfractions. Journal of Biological Chemistry, 257, 10510-10517.
48. Hoffman, J.S. & Benditt, E.P. (1982b). Secretion of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture. Journal of Biological Chemistry, 257, 10518-10522.
49. Hoffman, A.M. & Leighton, F.A. (1985). Hemograms and microscopic lesions of herring gulls during captivity. Journal of the American Veterinary Medical Association, 187, 1125-1128.
50. Hol, P.R., Van Andel, A.C.J., Van Ederen, A.M., Draaijer, J. & Gruys, E. (1985). Amyloid enhancing factor in hamster. British Journal of Experimental Pathology, 66, 689-697.
51. Hol, P.R., Snell, F.W.J.J., Niewold, T.A. & Gruys, E. (1986). Amyloid-enhancing factor (AEF) in the pathogenesis of AA-amyloidosis in the hamster. Virchows Archiv B Cell Pathology, 52, 273-281.
52. Husby, G. (1985). Amyloidosis and rheumatoid arthritis. Clinical and Experimental Rheumatology, 3, 173-180.
53. Husby, G. (1994). Classification of amyloidosis. In G. Husby (Ed.) Baillière's Clinical Rheumatology, 8:3 (pp. 503-511). London: Baillière Tindall.
54. Husebekk, A., Skogen, B., Husby, G. & Marhaug, G. (1985). Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo. Scandinavian Journal of Immunology, 21, 283-287.
55. Husebekk, A., Skogen, B. & Husby, G. (1988). High density lipoprotein has different binding capacity for different apolipoproteins. Scandinavian Journal of Immunology, 28, 653-658.
56. Inoue, S., Hultin, P.G., Szarek, W.A. & Kisilevsky, R. (1996). Effect of poly(vinylsulfonate) on murine AA-amyloid: a high-resolution ultrastructural study. Laboratory Investigation, 74, 1081-1090.
57. Karstad, L. & Sileo, L. (1971). Causes of death in captive wild waterfowl in the Kortright waterfowl park: 1967-1970. Journal of Wildlife Diseases, 7, 236-241.
58. Kawahara, E., Shiroo, M., Nakanishi, I. & Migita, S. (1989). The role of fibronectin in the development of experimental amyloidosis. American Journal of Pathology, 134, 1305-1314.
59. Kedar, I., Bleiberg, I. & Sohar, E. (1975). Stimulation of murine amyloidosis by a dialyzable product from pretreated donors. British Journal of Experimental Pathology, 56, 244-246.
60. Kelly, J.W. (1997). Amyloid formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure, 5, 595-600.
61. Kisilevsky, R. (1991). Serum amyloid A (SAA), a protein without a function: Some suggestions with reference to cholesterol metabolism. Medical Hypotheses, 35, 337-341.
62. Kisilevsky, R., Lemieux, L.J., Fraser, P.E., Kong, X., Hultin, P.G. & Szarek, W.A. (1995). Arresting amyloidosis in vivo using small-molecule anionic sulfonates or sulfates: implications for Alzheimer's disease. Nature Medicine, 1, 143-148.
63. Klunk, W.E., Pettegrew, J.W. & Abraham, D.J. (1989). Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet formation. Journal of Histochemistry and Cytochemistry, 37, 1273-1281.
64. Kluve-Beckerman, B. & Song, M. (1995). Genes Encoding Human Serum Amyloid-A Proteins Saa1 and Saa2 Are Located 18 kb Apart in Opposite Transcriptional Orientations. Gene, 159, 289-290.
65. Landman, W.J.M. & Gruys, E. (1998). Amyloid arthropathy in an Indian peafowl. Veterinary Record, 142, 90-91.
66. Landman, W.J.M., Gruys, E. & Dwars, R.M. (1994). A syndrome associated with growth depression and amyloid arthropathy in layers: a preliminary report. Avian Pathology, 23, 461-470.
67. Landman, W.J.M., Sletten, K., Koch, C.A.M., Tooten, P.C.J. & Gruys, E. (1996). Chicken joint amyloid protein is of AA-type. I. Characterisation of chicken amyloid protein. Scandinavian Journal of Immunology, 43, 210-218.
68. Landman, W.J.M., Peperkamp, N.H.M.T., Koch, C.A.M., Tooten, P.C.J., Crauwels, P.A.P. & Gruys, E. (1997). Induction of amyloid arthropathy in chickens. Amyloid: the International Journal of Experimental and Clinical Investigation, 4, 87-97.
69. 2-82 on platelet aggregation. In J.B. Natvig, Ø Førre, G. Husby, A. Husebekk, B. Skogen, K. Sletten & P. Westermark (Eds) Amyloid and Amyloidosis (pp. 129-132). Dordrecht: Kluwer Academic Publishers.
70. Levin, M., Pras, M. & Franklin, E.C. (1973). Immunologic studies of the major nonimmunoglobulin protein of the amyloid. I. Identification and partial characterization of a related serum component. Journal of Experimental Medicine, 138, 373-380.
71. Liepnieks, J.J ., Dwulet, F.E., Benson, M.D., Kluve-Beckerman, B. & Kushner, I. (1991). The primary structure of serum amyloid-A protein in the rabbit: comparison with serum amyloid-A proteins in other species. Journal of Laboratory and Clinical Medicine, 118, 570-575.
72. Ling, Y.S. (1992). Experimental production of amyloidosis in ducks. Avian Pathology, 21, 141-145.
73. Ling, Y.S., Mao, H.P., Zhong, A.C. & Guo, Y.C. (1991). The effects of Escherichia coli and its endotoxin on amyloidosis in ducks. Veterinary Pathology, 28, 519-523.
74. Linke, R.P. (1979). Temperature induced dissociation of serum amyloid protein SAA. Zeitschrift für Immunitätsforschung und Immunobiologie, 155, 255-261.
75. Linke, R.P., Bock, V., Valet, G. & Rothe, G. (1991). Inhibition of the oxidative burst response of N-formyl peptide-stimulated neutrophils by serum amyloid-A protein. Biochemical and Biophysical Research Communications, 176, 1100-1105.
76. Liu, M.R.J. (1985). Survey of duck amyloidosis in culled breeding ducks in Taiwan. Journal of the Chinese Society of Veterinary Science, II, 103-109.
77. Lorenzo, A. & Yankner, B.A. (1996). Amyloid fibril toxicity in Alzheimer's disease and diabetes. Annals of the New York Academy of Sciences, 777, 89-95.
78. Lowel, C.A., Stearman, R.S. & Morrow, J.F. (1986). Transcriptional regulation of serum amyloid A gene expression. Journal of Biological Chemistry, 261, 8453-8461.
79. Lyon, A.W., Narindrasorasak, S., Young, I.D., Anastassiades, T., Couchman, J.R., McCarthy, K.J. & Kisilevsky, R. (1991). Co-deposition of basement membrane components during the induction of murine splenic AA-amyloid. Laboratory Investigation, 64, 785-790.
80. MacDonald, D.W. & Carlson, H.C. (1969). Attempted experimental induction of amyloidosis in chickens. Poultry Science, 48, 71-76.
81. Maestrini, N. & Pascucci, S. (1970). Amyloidosis in guinea fowl. Atti della Società Italiana delle Scienze Veterinarie, 24, 485-486.
82. Magnus, J.H., Husby, G. & Kolset, S.O. (1989). Presence of glycosaminoglycans in purified AA-type amyloid fibrils associated with juvenile rheumatoid arthritis. Annals of the Rheumatic Diseases, 48, 215-219.
83. Magnus, J.H. (1991). Isolation and characterization of amyloid associated glycosaminoglycans and proteoglycans from human tissues. PhD thesis, University of Tromsø.
84. Magnus, J.H., Stenstad, T. & Husby, G. (1994). Proteoglycans, glycosaminoglycans and amyloid deposition. In G. Husby (Ed.) Baillière's Clinical Rheumatology, 8:3 (pp. 575-597). London: Baillière Tindall.
85. Marhaug, G., Hackett, B. & Dowton, S.B. (1997). Serum amyloid A gene expression in rabbit, mink and mouse. Clinical and Experimental Immunology, 107, 425-434.
86. Mason, W.S., Lien, J.M., Petcu, D.J., Coates, L., London, W.T., O'Connell, A., Aldrich, C. & Custer, R.P. (1987). In vivo and in vitro studies on duck hepatitis B virus replication. In W. Robinson, K. Koike & H. Will (Eds) Hepadna Viruses (pp. 3-16). New York: Liss.
87. Maximow, A. (1898). Experimentally induced amyloid degeneration of the liver. Virchows Archiv A für Pathologische Anatomie und Physiologie und für Klinische Medizin, 153, 353-399.
88. McCubbin, W.D., Kay, C.M., Narindrasorasak, S. & Kisilevsky, R. (1988). Circular-dichroism studies on two murine serum amyloid A proteins. Biochemical Journal, 256, 775-783.
89. 3 is a high density apolipoprotein and is secreted by macrophages. Proceedings of the National Academy of Sciences of the United States of America, 89, 7949-7952.
90. Meek, R.L., Urieli-Shovel, S. & Benditt, E.P. (1994). Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: Implications for serum amyloid A function. Proceedings of the National Academy of Sciences of the United States of America, 91, 3186-3190.
91. Miller, D.L., Papayannopoulus, I.A., Styles, J., Bobin, S.A., Lin, Y.Y., Biemann, K. & Iqbal, K. (1993). Peptide compositions of cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Archives of Biochemistry and Biophysics, 301, 41-52.
92. Mitchell, T.I., Coon, C.I. & Brinckerhoff, C.E. (1991). Serum amyloid A (SAA3) produced by rabbit synovial fibroblasts treated with phorbol esters or interleukin 1 induces synthesis of collagenase and is neutralized with specific antiserum. Journal of Clinical Investigation, 87, 1177-1185.
93. Miwata, H., Yamada, T., Okada, M., Kudo, T., Kimura, H. & Morishima, T. (1993). Serum amyloid A protein in acute viral infections. Archives of Disease in Childhood, 68, 210-214.
94. Moriguchi, R., Izawa, H. & Soekawa, M. (1974). Histopathology of spontaneous amyloidosis in ducks. Kitasato Archives of Experimental Medicine, 47, 211-226.
95. Nelson, S.R., Lyon, M., Gallagher, J.T., Johnson, E.A. & Pepys, M.B. (1991). Isolation and characterization of the integral glycosaminoglycan constituents of human amyloid A and monoclonal light-chain amyloid fibrils. Biochemical Journal, 275, 67-73.
96. Niewold, T.A., Hol, P.R., Van Andel, A.C.J., Lutz, E.T.G. & Gruys, E. (1987). Enhancement of amyloid induction by amyloid fibril fragments in hamster. Laboratory Investigation, 56, 544-549.
97. Peperkamp, N.H.M.T., Landman, W.J.M., Tooten, P.C.J., Ultee, A., Voorhout, W.F. & Gruys, E. (1997). Light microscopic, immunohistochemical and electron microscopic features of amyloid arthropathy in chickens. Veterinary Pathology, 34, 271-278.
98. Pepys, M.B., Dyck, R.F., De Beer, F.C., Skinner, M. & Cohen, A.S. (1979). Binding of serum amyluid-P component (SAP) by amyloid fibrils. Clinical and Experimental Inmunology, 38, 284-293.
99. Perez-Villa, F., Campistol, J.M., Ferrando, J. & Botey, A. (1989). Renal amyloidosis secondary to acne conglobata. International Journal of Dermatology, 28, 132-133.
100. Perini, F., Vidal, R., Ghetti, B., Tagliavini, F., Frangione, B. & Prelli, F. (1996). Prp 27-30 is a normal soluble prion protein fragment released by human platelets. Biochemical and Biophysical Research Communications, 223, 572-577.
101. Pras, M., Schubert, M., Zucker-Franklin, D., Rimon, A. & Franklin, E.C. (1968). The characterization of soluble amyloid prepared in water. Journal of Clinical Investigation, 47, 924-933.
102. Prelli, F., Pras, M., Shtrasburg, S. & Frangione, B. (1991). Characterization of high molecular weight amyloid A proteins. Scandinavian Journal of Immunology, 33, 783-786.
103. Putto, A., Ruuskanen, O., Meurman, O., Ekblad, H., Korvenranta, H., Mertsola, J., Peltola, H., Sarkkinen, J., Viljanen, M.K. & Halonen, P. (1986). C-reactive protein in the evaluation of febrile illness. Archives of Disease in Childhood, 61, 24-29.
104. Rakhmanov, A.M. (1958). Amyloidosis in ducks reared and fattened on poultry farms. Veterinary Bulletin, 29, 328.
105. Rigdon, R.H. (1960). Experimental amyloid production in ducks with methylcholanthrene. Texas Reports on Biology and Medicine, 18, 93-102.
106. Rigdon, R.H. (1961). Amyloidosis: spontaneous occurrence in white Pekin ducks. American Journal of Pathology, 39, 369-378.
107. Rigdon, R.H. (1964). Rupture of spleen in ducks with amyloidosis. Archives of Pathology, 78, 66-68.
108. Rigdon, R.H. & Mack, J. (1969). Amyloidosis: age of occurrence and rate of progression: experimental study in the white Pekin duck. Journal of the American Geriatrics Society, 17, 514-521.
109. Sack Jr., G.H. & Talbot Jr., C.C. (1992). The human serum amyloid A locus SAA4 is a pseudogene. Biochemical and Biophysical Research Communications, 183, 362-366.
110. Sato, A., Koga, T., Inoue, M. & Goto, N. (1981). Pathological observations of amyloidosis in swans and other Anatidae. Japanese Journal of Veterinary Science, 43, 509-519.
111. Shainkin-Kestenbaum, R., Levartowsky, D., Zimlichman, S., Fridkin, M. & Pras, M. (1991). Antiplatelet aggregation activity of serum amyloid A (SAA). In J.B. Natvig, Ø. Førre, G. Husby, A. Husebekk, B. Skogen, K. Sletten & P. Westermark (Eds) Amyloid and Amyloidosis (pp. 139-142). Dordrecht: Kluwer Academic Publishers.
112. Shiroo, M., Kawahara, E., Nakanishi, I. & Migita, S. (1987). Specific deposition of serum amyloid A protein 2 in the mouse. Scandinavian Journal of Immunology, 26, 709-716.
113. Shivaprasad, H.L. & Woolcock, P.R. (1995). Necrohaemorrhagic hepatitis in broiler breeders. Proceedings of the 44th Western Poultry Disease Conference, Sacramento, California, 44, 6.
114. Shivaprasad, H.L., Meteyer, C.U. & Jeffrey, J.S. (1991). Amyloidosis in turkeys, presented at the 34th annual meeting, American Association of Veterinary Laboratory Diagnosticians, San Diego, California, 34, 57.
115. Sipe, J.D., De Beer, F.C., Gonnerman, W.A., Cathcart, E.S. & Hayes, K.C. (1993). Syrian and Armenian hamsters differ in serum amyloid A gene expression; the SAA3 subtype is selectively deposited as AA-fibrils. In R. Kisilevsky (Ed.) Proceedings of the 7th International Symposiumon on Amyloidosis (p. 30). Kingston, Ontario, Queen's University.
116. Snow, A.D. & Wight, T.N. (1989). Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses. Neurobiology of Aging, 10, 481-497.
117. Snow, A.D., Willmer, J. & Kisilevsky, R. (1987). A close ultrastructural relationship between sulfated proteoglycans and AA-amyloid fibrils. Laboratory Investigation, 57, 687-698.
118. Snow, A.D., Cummmings, J.A., Ngo, C.T., Yang, W., Nochiin, D., Rimvall, K., Sheardown, M.J. & Judge, M.E. (1995). Further studies implicating the importance of perlecan (a specific heparan sulfate proteoglycan) in an animal model of fibrillar Aβ amyloid deposition in vivo: comparison of Aβ (1-42) versus Aβ (1-40). Society for Neuroscience Abstracts, 21, 1282.
119. Soto, C., Kindy, M.S., Baumann, M. & Frangione, B. (1996). Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochemical and Biophysical Research Communications, 226, 672-680.
120. Syversen, P.V., Sletten, K. & Husby, G. (1990). Evolutionary aspects of protein SAA. In J.B. Natvig, Ø. Førre, G. Husby, A. Husebekk, B. Skogen, K. Sletten & P. Westermark (Eds) Amyloid and Amyloidosis (pp. 111-114). Dordrecht: Kluwer Academic Publishers.
121. Tablante, N.L., Vaillancourt, J.P. & Julian, R.J. (1994). Necrotic, haemorrhagic, hepatomegalic hepatitis associated with vasculitis and amyloidosis in commercial laying hens. Avian Pathology, 23, 725-732.
122. Thompson, K.J., Freund, J., Sommer, H.E. & Walter, A.W. (1947). Immunization of ducks against malaria by means of killed parasites with or without adjuvant. American Journal of Tropical Medicine, 27, 79-105.
123. Turnell, W.G., Sarra, R., Glover, I.D.G., Baum, J., Caspi, D., Baltz, M.L. & Pepys, M.B. (1986a). X-ray scattering from human AA-fibrils re-examined with the aid of secondary prediction. In G.G. Glenner, E.F. Osserman, E.P. Benditt, E. Calkins, A.S. Cohen & D. Zucker-Franklin (Eds) Proceedings of the 4th International Symposium on Amyloidosis. New York, 1984 (pp. 49-55). New York: Plenum Press.
124. Turnell, W.G., Sarra, R., Baum, J.O., Caspi, D., Baltz, M.L. & Pepys, M.B. (1986b). X-ray scattering and diffraction by wet gels of AA-amyloid fibrils. Molecular Biology and Medicine, 3, 409-424.
125. Turnell, W.G., Sarra, R., Glover, I.D., Baum, J.O., Caspi, D., Baltz, M.L. & Pepys, M.B. (1986c). Secondary structure prediction of human SAA1. Presumptive identification of calcium and lipid binding sites. Molecular Biology and Medicine, 3, 387-407.
126. Virchow, R. (1854). Ueber eine im Gehirn und Rückenmark des Menschen aufgefundene Substanz mit der chemischen Reaktion der Cellulose. Virchows Archiv A für Pathologische Anatomie und Physiologie und für Klinische Medizin, 6, 135-138, 268-271, 416-426.
127. Von Rampin, T., Sironi, G. & Gallazi, D. (1989). Amyloidoseepisoden bei Junghennen nach wiederholter Anwendung van antibakteriellen Ölemulsionvakzinen. Deutsche Tierärztliche Wochenschrift, 96, 168-172.
128. Wang, D.H. & Di, B.X. (1992). Pathological study on amyloidosis in chickens. Acta Veterinaria Zootechnica Sinica, 23, 256-261.
129. Werdelin, O. & Ranlov, P. (1966). Amyloidosis in mice produced by transplantation of spleen cells from casein-treated mice. Acta Pathologica et Microbiologica Scandinavica, 68, 1-18.
130. Westermark, P., Shirahama, T., Skinner, M., Brun, A., Cameron, R. & Cohen, A.S. (1982). Immuno-histochemical evidence for the lack of amyloid P-component in some intracerebral amyloids. Laboratory Investigation, 46, 457-460.
131. Westermark, P., Sletten, K., Westermark, G.T., Raynes, J.& McAdam, K.P. (1996). A protein AA-variant derived from a novel serum AA-protein, SAA1 delta, in an individual from Papua New Guinea. Biochemical and Biophysical Research Communications, 223, 320-323.
132. Whitehead, A.S., De Beer, M.C., Steel, D.M., Rits, M., Lelias, J.M., Lane, W.S. & De Beer, F.C. (1992). Identification of novel members of the serum amyloid A protein superfamily as constitutive apolipoproteins of high density lipoprotein. Journal of Biological Chemistry, 267, 3862-3867.
133. Wisniewski, T. & Frangione, B. (1992). Apoliprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neuroscience Letters, 135, 235-238.
134. Yamada, T., Liepnieks, J., Benson, M. & Kluve-Beckerman, B. (1996). Accelerated amyloid deposition in mice treated with the aspartic protease inhibitor, pepstatin. Journal of Immunology, 157, 901-907.
135. Yood, R.A., Skinner, M., Rubinov, A., Talarico, L. & Cohen, A.S. (1983). Bleeding manifestations in 100 patients with amyloidosis. Journal of the American Medical Association, 249, 1322-1324.
136. Zimlichman, S., Danon, A., Natnan, I., Mozes, G. & Shainkin-Kestenbaum, R. (1990). Serum amyloid A, an acute phase protein, inhibits platelet activation. Journal of Laboratory and Clinical Medicine, 116, 180-186.
137. Zschiesche, W. & Jakob, W. (1989). Pathology of animal amyloidosis. Pharmacology and Therapeutics, 41, 49-83.
138. Zschiesche, W. & Linke, R.P. (1986). Zur amyloidose der Zoovögel unter besonderer Berücksichtigung des Wassergeflügels. Erkrankungen der Zootiere, 28, 301-306.
139. Zschiesche, W. & Linke, R.P. (1989). Immunohistochemical characterization of spontaneous amyloidosis in captive birds as AA-type, using monoclonal and polyclonal anti-AA antibodies against mammalian amyloid. Acta Histochemica, 86, 45-50.