Protein folding pathology in domestic animals

Journal of Zhejiang University: Science

Volumn 5, Issue 10, 2004, Pages 1226-1238

  Gruys, Erik ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Alzheimer's disease; Amyloid; Amyloid enhancing factor; Extracellular fibrils; Prion; PrP; Spongiform encephalopathy

Indexed keywords

BIREFRINGENCE; ELECTROENCEPHALOGRAPHY; MICROSTRUCTURE; PATHOLOGY; PROTEINS; TISSUE;

ALZHEIMER DISEASE; AMYLOID; AMYLOID ENHANCING FACTOR; AMYLOIDOGENESIS; EXTRACELLULAR FIBRILS; FIBRILLAR MICROANATOMICAL STRUCTURES; PRION; SPONGIFORM ENCEPHALOPATHY;

ANIMAL CELL CULTURE;

AMYLOID;

AMYLOIDOSIS; ANIMAL; ANIMAL DISEASE; CHEMISTRY; DOMESTIC ANIMAL; HUMAN; METABOLISM; PRION; PRION DISEASE; PROTEIN FOLDING; REVIEW;

AMYLOID; AMYLOIDOSIS; ANIMAL DISEASES; ANIMALS; ANIMALS, DOMESTIC; HUMANS; PRION DISEASES; PRIONS; PROTEIN FOLDING;

EID: 10944220882     PISSN: 10093095     EISSN: None     Source Type: Journal    
DOI: 10.1631/jzus.2004.1226     Document Type: Article

References (145)

1. Abramo, F., Colombo, S., Di, L.C., Mortellaro, C.M., 1999. A case of cutaneous asthenia in a kitten. Europ J Vet Pathol, 5:111-113.
2. Aidulis, D., Pegg, D.E., Hunt, C.J., Goffm, Y.A., Vanderkelen, A., van Hoeck, B., Santiago, T., Ramos, T., Gruys, E., Voorhout, W., 2002. Processing of ovine cardiac valve allografts: 1. Effects of preservation method and mechanical properties. Cell Tis Bank, 3:79-89.
3. Almond, F., Pattison, J., 1997. Human BSE. Nature, 389:437-438.
4. Barral, J.M., Broadley, S.A., Schaffar, G., Hartl, F.U., 2004. Roles of molecular chaperones in protein misfolding diseases. Semin Cell Dev Biol, 15:17-29.
5. Bastiari, F.O., Hart, M.N., Cancilla, P.A., 1981. Additional evidence of spiroplasma in Creutzfeldt-Jakob disease. Lancet, 8221:660.
6. Belt, P.B.G., Muileman, I.H., Schreuder, B.E.C., Bos-de Ruijter, J., Gielkens, A.L.J., Smits, M., 1995. Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie. J Gen Virol, 76:509-517.
7. Benditt, E.P., Eriksen, N., 1971. Chemical classes of amyloid substance. Am J Pathol, 65:231-252.
8. Benditt, E.P., Eriksen, N., Hanson, R.H., 1979. Amyloid protein SAA is an apooprotein of mouse plasma high density lipoprotein. Proc Natl Acad Sci USA, 76:4092-4096.
9. Benditt, E.P., Hoffman, J.S., Eriksen, N., Parmelee, B.C., Walsh, K.A., 1982. SAA, an apoprotein of HDL: its structure and function. Ann New York Acad Sci, 389:183-189.
10. Breuer, W., Geisel, O., Linke, R.P., Hermanns, W., 1994. Light microscopic, ultrastructural, and inmmunohistochemical examinations of calcifying epithelial odontogenic tumors (CEOT) in a dog and a cat. Vet Pathol, 31:415-420.
11. Brown, P.J., Young, R.D., Cripps, P.J., 1993. Abnormalities of collagen fibrils in a rabbit with a connective-tissue defect similar to Ehlers-Danlos syndrome. Res Vet Sci, 55:346-350.
12. Brown, K.L., Stewart, K., Ritchie, D.L., Mabbott, N.A., Williams, A., Fraser. H., Morrison, W.I., Bruce, M.E., 1999. Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells. Nat Med, 5:1308-1312.
13. Bruce, M.E., McConnell, I., Fraser, H., Dickinson, A.G., 1991. The disease characteristics of different strains of scrapie in Sine congenic mouse lines: implications for the nature of the agent and host control of pathogenesis. J Gen Virol, 72:595-603.
14. Bruce, M.E., Will, R.G., Ironside, J.W., McConnell, I., Drummond, D., Suttie, A., McCardie, L., Chree, A., Hope, J., Birkett, C., Cousens, S., Fraser, H., Bostock, C.J., 1997. Transmissions tp mice indicate that 'new variant' CJD is caused by the BSE agent. Nature, 389:498-501.
15. Buxbaum, J.N., 2004. The systemic amyloidoses. Curr Opin Rheumatol, 16:67-75.
16. Carver, J.A., Rekas, A., Thorn, D.C., Wilson, M.R., 2003. Small heat-shock proteins and clusterin: intra- and extracellualr molecular chaperones with a common mechenism of action and function? IUBMB Life, 55:661-668.
17. Cohen, A.S., 1966. Preliminary chemical analysis of partially purified amyloid fibrils. Lab Invest, 15:66-83.
18. Cohen, A.S., Calkins, E., 1959. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature, 183:1202-1203.
19. Cohen, A.S., Weiss, L., Calkins, E., 1958. A study of the fine structure of the spleen in experimental amyloidosis of the rabbit. Clin Res, 6:237.
20. Collinge, J., 1999. Variant Creutzfeldt-Jakob disease. Lancet, 354:317-322.
21. Collinge, J., Sidle, K.C., Meads, J., Ironside, J., Hill, A.F., 1996. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature, 383:685-90.
22. Collins, S., Boyd, A., Fletcher, A., Byron, K., Harper, C., McLean, C.A., Masters, C.L., 2000. Novel prion protein gene mutation in an octogenarian with Creutzfeldt-Jakob disease. Arch Neurol, 57:1058-1063.
23. De Lorenzi, E., Giorgetti, S., Grossi, S., Merlini, G., Caccialanza, G., Bellotti, V., 2004. Pharmaceutical strategies against amyloidosis: old and new drugs in targeting a protein misfolding disease. Curr Med Chem, 11:1065-1084.
24. Dobson, C.M., 2004. Principles of protein folding, misfolding and aggregation. Sem Cell Dev Biol, 15:3-16.
25. Dubois, J., Ismail, A.A., Chan, S.L., AliKhan, Z., 1999. Fourier transform infrared spectroscopic investigation of temperature- and pressure-induced diaggregation of amyloid A. Scan J Immunol, 49:376-380.
26. Eanes, E.D., Glenner, G.G., 1968. X-ray diffraction studies of amyloid filaments. J Histochem Cytochem, 16:673-677.
27. Ehlers, B., Diringer, H., 1984. Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen. J Gen Virol, 65:1325-1330.
28. Elliott-Bryant, R., Cathcart, E.S., 1998. Amyloid enhancing factor and dietary transmission in accelerated amyloid A amyloidosis. Clin Immunol Immunopathol, 88:65-69.
29. Farrington, M., Wreghitt, T., Matthews, I., Scarr, D., Sutehall, G., Hunt, C.J., Santiago, T., Gruys, E., Voorhout, W., Ramos, T., Pegg, D.E., 2002. Processing of cardiac valve allografts: 2. Effects of antimicrobial treatment on sterility, structure and mechanical properties. Cell Tiss Bank, 3:91-103.
30. Friedreich, N., Kekule, A., 1859. Zur Amyloidfrage. Virchows Arch Path Anat Klin Med, 16:50-65.
31. Gandy, S., DeMattos, R.B., Lemere, C.A., Heppner, F.L., Leverone, J., Aguzzi, A., Ershler, W.B., Dai, J., Fraser, P., Hyslop, P.S., Holtzman, D.M., Walker, L.C., Keller, E.T., 2004. Alzheimer A beta vaccination of rhesus monkeys (Macaca mulatto). Alzheimer Dis Assoc Disord, 18:44-46.
32. Gardner, D.G., Dubielzig, R.R., McGee, E.V., 1994. The so-called calcifying epithelial odontogenic tumour in dogs and cats (amyloid-producing odontogenic tumour). J Comp Pathol, 111:221-230.
33. Glenner, G.G., 1980. Amyloid deposits and amyloidosis: the beta-fibrilloses (two parts). New Engl J Med, 302: 1283-1292;1333-1343.
34. Glenner, G.G., 1981. The bases of the staining of amyloid fibers: their physicochemical nature and the mechanism of their dye-substrate interaction. Prog Histochem Cytochem, 13:1-37.
35. Glenner, G.G., Wong, C.W., 1984. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun, 16:885-890.
36. Glenner, G.G., Eanes, E.D., Bladen, H.A., Linke, R.P., Termine, J.D., 1974. β-Pleated sheet fibrils. A comparison of native amyloid with synthetic protein fibrils. J Histochem Cytochem, 22:1141-1158.
37. Goedegebuure, S.A., 1987. Spontaneous primary myopathies in domestic animals: a review. Vet Quart, 9:155-157.
38. Goedegebuure, S.A., Hartman, W., Hoebe, H.P., 1983. Dystrophy of the diaphragmatic muscles in adult Meuse-Rhine-Yssel cattle: electromyographical and histological findings. Vet Pathol, 20:32-48.
39. Goffin, Y.A., Black, M.M., Lawford, P.V., 1990. The stability and performance of bioprosthetic heart valves. Curr Perspect Implant Dev, 2:65-120.
40. Goffin, Y.A.H., Henriques de, G.R., Szombathelyi, T., Toussaint, M.J.M., Gruys, E., 1997. Morphologic study of homograft valves before and after cryopreservation and after short-tem implantation in patients. Cardiovasc Pathol, 6:35-42.
41. Gonnerman, W.A., Elliott-Bryant, R., Carreras, I., Sipe, J.D., Cathcart, E.S., 1995. Linkage of protection against amyloid fibril formation in the mouse to a single, autosomal dominant gene. J Exp Med, 181:2249-2252.
42. Gruys, E., 1988. Pathologische anatomic van nutszoogdieren. Deel X. Pathologic van het schaap en de geit, vervolg. Dier-en-Arts, 3:92-100 (in Dutch).
43. Gruys, E., 1995. First workshop and clinic on neuropathology in geriatric dogs and cats. Wiesbaden, Germany May 4-5, 1995. Amyloid Int J Exp Clin Invest, 2:280-283.
44. Gruys, E., Castano, M., 1977. Parallel intraylysosomal amyloid fibrils, a possible result of phagocytosis. Vet Pathol, 14:407-419.
45. Gruys, E., Snel, F.W.J.J., 1994. Animal models for reactive amyloidosis. Baillieres Clin Rheumatol, 8:599-611.
46. Gruys, E., Timmermans, H.J., van Ederen, A.M., 1979. Deposition of amyloid in the liver of hamsters: an enzyme-histochemical and electron-microscopical study. Lab Anim, 13:1-9.
47. Gruys, E., Obwolo, M.J., Toussaint, M.J.M., 1994. Diagnostic significance of the major acute phase proteins in veterinary clinical chemistry: a review. Vet Bull 64:1009-1018.
48. Gruys, E., Tooten, P.C.J., Kuijpers, M.H.M., 1996. Lung, ileum and heart are predilection sites for AApoAII amyloid deposition in CD-1 Swiss mice used for toxicity studies, pulmonary amyloid indicates AApoAII. Lab Anim, 30:28-34.
49. Guijarro, J.I., Sunde, M., Jones, J.A., Campbell, I.D., Dobson, C.M., 1998. Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci USA, 95:4224-4228.
50. Heppner, F.L., Gandy, S., McLaurin, J., 2004. Current concepts and future prospects for Alzheimer disease vaccines. Alzheimer Dis Assoc Disord, 18:38-43.
51. Higuchi, K., Kogishi, K., Wang, J., Chen, X., Chiba, T., Matsushita, T., Hoshii, Y., Kawano, H., Ishihara, T., Yokota, T., Hosokawa, M., 1998. Fibrillization in mouse senile amyloidosis is fibril conformation dependent. Lab Invest, 78:1535-1542.
52. Hill, A.F., Desbruslais, M., Joiner, S., Sidle, K.C.L., Gowland, I., Collinge, J., Doey, L.J., Lanton, P., 1997. The same prion strain causes vCJD and BSE. Nature, 389:448-450.
53. Hoi, P.R., van Beuningen-Jansen, E.W., Gruys, E., 1983. Reaggregation of Bovine Amyloid Protein AA. In: Tribe, C.R., Bacon, P.A. (Eds.), Amyloidosis EARS. Wright and Sons, Bristol, p.158-163.
54. Hoi, P.R., van Ederen, A.M., Snel, F.W.J.J., Langeveld, J.P.M., Veerkamp, J.H., Gruys, E., 1985. Activities of lysosomal enzymes and levels of serum amyloid A (SAA) in blood plasma of hamsters during casein induction of AA-amyloidosis. Br J Exp Pathol, 66:279-292.
55. Hunter, N., Goldmann, W., Foster, J.D., Cairns, D., Smith, G., 1997. Natural scrapie and PrP genotype: case-control studies in British sheep. Vet Rec, 141:137-140.
56. Hurshman, A.R., White, J.T., Powers, E.T., Kellt, J.W., 2004. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry, 43:7365-7381.
57. Inouye, H., Bond, J., Baldwin, M.A., Ball, H.L., Prusiner S.B., Kirschner, D.A., 2000. Structural changes in a hydrophobic domain of the prion protein induced by hydration and by Ala > Val and Pro > Leu substitutions. J Mol Biol, 300:1283-1296.
58. INC (International Nomenclature Committee), 1998a. Part 1. Nomenclature of amyloid fibril proteins. Amyloid Int J Exp Clin Invest, 6:63-66.
59. INC (International Nomenclature Committee), 1998b. Part 2. Revised nomenclature for serum amyloid A (SAA). Amyloid Int J Exp Clin Invest, 6:67-70.
60. Janson, J., Ashley, R.H., Harrison, D., Mclntyre, S., Butler, P.C., 1999. The mechanism of islet amyloid polypep-tide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes, 48:491-498.
61. Jones, T.C., Hunt, R.D., King, N.W., 1997. Veterinary Pathology. Williams and Wilkins, Baltimore, p.850.
62. Kimberlin, R.H., 1982. Scapie agent: prions or virinos? Nature, 297:107-108.
63. Kisilevsky, R., Gruys, E., Shirahama, T., 1995. Does amyloid enhancing factor exist? Is AEF a single biological entity? Amyloid Int J Exp Clin Invest, 2:128-133.
64. Kisilevsky, R., Lemieux, L., Boudreau, L., Dun-Sheng, Y., Fraser, P., 1999. New clothes for amyloid enhancing factor (AEF): silk as AEF. Amyloid Int J Exp Clin Invest, 6:98-106.
65. Kisilevsky, R., Szarek, W.A., Ancsin, J.B., Elimova, E., Marone, S., Bhat, S., Berkin, A., 2004. Inhibition of amyloid A amyloidogenesis in vivo and in tissue culture by 4-deoxy analogues of peracetylated 2-acetamido-2deoxy-α- and β-D-glucose. Am J Pathol, 164:2127-2137.
66. Kluve-Beckerman, B., Liepnieks, W.L., Benson, M.D., 1999. A cell culture system for the study of amyloid pathogenesis. Amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A. Am J Pathol, 155:123-133.
67. Koolbergen, D.R., Hazekamp, M.G., Kurvers, M., de Heer, E., Cornelisse, C.J., Huysmans, H.A., Bruijn, J.A., 1998. Tissue chimerism in human cryopreserved homograft valve explants demonstrated by in situ hybridization. Ann Thorac Surg, 66(6):S225-S232.
68. Landman, W.J.M., 1998. Amyloid Arthropathy in Chickens. PhD-thesis, Utrecht University, Utrecht (ISBN 90-393-1667-8).
69. Landman, W.J.M., Gruys, E., 1998. Amyloid arthropathy in an Indian peafowl. Vet Rec, 142:90-91.
70. Lazo, N.D., Downing, D.T., 1998. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry, 37:1731-1735.
71. Liang, J., Elliott-Bryant, R., Hajri, T., Sipe, J.D., Cathcart, E.S., 1998. A unique amyloidogenic apolipoprotein serum amyloid A (apoSAA) isoform expressed by the amyloid resistant CE/J mouse strain exhibits higher affinity for macrophages than apoSAAl and apoSAA2 expressed by amyloid susceptible CBA/J mice. Biochim Biophys Acta, 1394:121-126.
72. Li, L., Darden, T.A., Bartolotti, L., Kominos, D., Pedersen, L.G., 1999. An atomic model for the pleated beta-sheet structure of Ap amyloid protofilaments. Biophys J, 76:2871-2878.
73. Linke, R.P., 2000. Highly sensitive diagnosis of amyloid and various amyloid syndromes using Congo red fluorescence. Virchows Arch A Pathol Anat, 436:439-448.
74. Linke, R.P., Nathrath, W.B.L., Wilson, P.D., 1983. Immuno-electron microscopic identification and classification of amyloid in tissue sections by the postern-bedding protein-A gold method. Ultrastruct Pathol, 4:1-7.
75. Livneh, A., Drenth, J.P., Klasen, I.S., Langevitz, P., George, J., Shelton, D.A., Gumucio, D.L., Pras, E., Kastner, D.L., Pras, M., van der Meer, J.W., 1997. Familial Mediterranean fever and hyperimmunoglobulinemia D syndrome: two diseases with distinct clinical, serologic, and genetic features. J Rheumatol, 24:1558-1563.
76. Lopez de la Paz, M., Serrano, L., 2004. Sequence determinants of amyloid fibril formation. Proc Natl Acad Sci USA, 101:87-92.
77. Lundmark, K., Westermark, G.T., Nystrom, S., Murphy, C.L., Solomon, A., Westermark, P., 2002. Transmissibility of systemic amyloidosis by a prion-like mechanism. Proc Natl Acad Sci USA, 100:6979-684.
78. MacRaild, C.A., Stewart, C.R., Mok, Y.F., Gunzburg, M.J., Perugini, M.A., Lawrence, L.J., Tirtaatmadja, V., Cooper-White, J.J., Hewlett, G.J., 2004. Non-fibrillar components of amyloid deposits mediate the self-association and tangling of amyloid fibrils. J Biol Chem, 279:21038-21045.
79. Magnus, J.H., 1991. Isolation and Characterization of Amyloid Associated Glycosaminoglycans and Proteoglycans from Human Tissues. PhD-thesis, University of Tromso, Tromso (ISBN 82-7589-014-4).
80. Magy, N., Liepnieks, J.J., Benson, M.D., Kluve-Beckerman, B., 2003. Amyloid-enhancing factor mediates amyloid formation on fibroblasts via a nidus/template mechanism. Arthr Rheum, 48:1430-1437.
81. Ma, Z., Westermark, G.T., Johnson, K.H., O'Brien, T.D., Westermark, P., 1998. Quantitative immunohisto-chemical analysis of islet amyloid polypeptide (IAPP) in normal, impaired glucose tolerant, and diabetic cats. Amyloid Int J Exp Clin Invest, 5:255-261.
82. McDonald, T.L., Larson, M.A., Mack, D.R., Weber, A., 2001. Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum. Vet Immunol Immunopathol, 83:203-211.
83. Mihara, M., Shiina, M., Nishimoto, N., Yoshizaki, K., Kishimoto, T., Akamatsu, K., 2004. Anti-interleukin-6 receptor antibody inhibits murine AA-amyloidosis. J Rheumatol, 31:1132-1138.
84. Miller, S.R., Sekijima, Y., Kelly, J.W., 2004. Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants. Lab Invest, 84:545-552.
85. Minor, R.R., 1980. Collagen metabolism. Am J Pathol, 98:227-277.
86. Muller, W.E., Koch, S., Eckert, A., Hartmann, H., Scheuer, K., 1995. β-Amyloid peptide decreases membrane fluidity. Brain Res., 674:133-136.
87. Neves, J., Abecassis, M., Santiago, T., Ramos, T., Melo, J., Gruys, E., Hulskamp-Koch, C., Ultee, A., Verkaar, E.L.C., Lenstra, J.A., Goffin, Y.A., Vanderkelen, A., van Hoeck, B., Hunt, C.J., Pegg, D.E., 2002. Processing of ovine cardiac valve allografts: 3. Implantation following antimicrobial treatment and preservation. Cell Tiss Bank, 3:105-119.
88. Niewold, T.A., 1990. Pathogenesis of AA-amyloidosis. PhD-thesis, Utrecht University, Utrecht (ISBN 90-9003814-0).
89. Niewold, T.A., Hoi, P.R., van Andel, A.C., Lutz, E.T.G., Gruys, E., 1987. Enhancement of amyloid induction by amyloid fibril fragments in hamster. Lab Invest, 56:544-9.
90. Niewold, T.A., Flores, L.J.M., van den Heuvel, L.P.W.J., Ultee, A., Tooten, P.C.J., Veerkamp, J.H., 1991. Characterization of proteoglycans and glycosamino-glycans in bovine renal AA-type amyloidosis. Virchows Arch B Cell Pathol, 60:321-328.
91. Niewold, T.A., Murphy, C.L., Hulskamp-Koch, C.A.M., Tooten, P.C.J., Gruys, E., 1999a. Casein related amyloid, characterization of a new and unique amyloid protein isolated from bovine corpora amylacea. Amyloid Int J Exp Clin Invest, 6:244-249.
92. Niewold, T.A., van der Linde-Sipman, J.S., Murphy, C.L., Tooten, P.C.J., Gruys, E., 1999b. Familial amyloidosis in cats: Siamese and Abyssinian AA proteins differ in primary sequence and pattern of deposition. Amyloid Int J Exp Clin Invest, 6:205-209.
93. Ovelgonne, J.H., Landman, W.J.M., van den Boogaard, A.E.J.M., Tooten, P.C.J., Gielkens, A.L.J., Peeters, B.P., Gruys, E., 1999. Two Breeds of Chicken with Different Susceptibility to An Amyloidogenic Strain of Enterococcus Faecalis Appear to Have Identical SAAs. In: Kyle, R.A., Gertz, M.A. (Eds.), Amyloid and Amyloidosis 1998. Parthenon, New York, p.390-392.
94. Papaioannou, N., Tooten, P.C.J., Van Ederen, A.M., Bohl, J.R.E., Rofina, J., Tsangaris, T., Gruys, E., 2001. Immunohistochemical investigation of the brain of aged dogs. I. Detection of neurofibrillary tangles and of 4-hydroxynonenal protein, an oxidative damage product, in senile plaques. Amyloid J Prot Fold Dis, 8:11-21.
95. Parry, H.B., 1983. In: Oppenheimer, D.R. (Ed.), Scrapie Disease in Sheep. Academic Press London, ISBN 0-12-545750-2.
96. Pearson, G.R., Wyatt, J.M., Gruffydd-Jones, T.J., Hope, J., Chong, A., Higgins, R.J., Scott, A.C., Wells, G.A., 1992. Feline spongiform encephalopathy: fibril and PrP studies. Vet Rec, 131:307-10.
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. Vet Pathol, 34:271-278.
98. Permanne, B., Adessi, C., Saborio, G.P., Fraga, S., Frossard, M.J., Van Dorpe, J., Dewachter, I., Banks, W.A., Van Leuven, F., Soto, C., 2002. Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide. FASEB J, 16:860-862.
99. Phipps-Yonas, H., Pinard, G., Ali-Khan, Z., 2004. Humoral proinflammatory cytokine and SAA generation profiles and spatio-temporal relationship between SAA and lysosomal cathepsin B and D in murine splenic monocytoid cells during AA amyloidosis. Scand J Immunol, 59:168-176.
100. Platz, S.J., Breuer, W., Geisel, O., Linke, R.P., Hermanns, W., 1997. Identification of lambda light chain amyloid in eight canine and two feline extramedullary plas-macytomas. J Comp Pathol, 116:45-54.
101. Pras, M., Schubert, M., Zucker-Franklin, D., Rimon, A., Franklin, E.C., 1968. The characterization of soluble amyloid prepared in water. J Clin Invest, 47:924-933.
102. Priola, S.A., 1999. Prion protein and species barriers in the transmissible spongiform encephalopathies. Biomed Pharmacother, 53:27-33.
103. Prusiner, S.B., 1982. Novel proteinaceous infectious particles cause scrapie. Science, 216:136-144.
104. Prusiner, S.B., McKinley, M.P., Bowman, K.A., Bolton, D.C., Bendheim, P.E., Groth, D.F., Glenner, G.G., 1983. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell, 35:349-358.
105. Ramos-Vara, J.A., Miller, M.A., Pace, L.W., Linke, R.P., Common, R.S., Watson, G.L., 1998. Intestinal multi-nodular A-lambda amyloid deposition associated with extramedullary plasmocytoma in 3 dogs. Clinicopathological and immunohistochemical studies. J Comp Pathol, 119:239-249.
106. Ren, Y., Reddy, S.A., Liao, W.S., 1999. Purification and identification of a tissue-specific represser involved in serum amyloid Al gene expression. J Biol Chem, 274:37154-37160.
107. Rijkers, D.T., Hoppener, J.W., Posthuma, G., Lips, C.J., Liskamp, R.M., 2002. Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides. Chemistry, 8:4285-4291.
108. Roertgen, K.E., Lund, E.M., O'Brien, T.D., Westermark, P., Hayden, D.W., Johnson, K.H., 1995. Apolipoprotein Al-derived pulmonary vascular amyloid in aged dogs. Am J Pathol, 147:1311-1317.
109. Rofina, J.E., Papaioannou, N., Van Andel, I., Van Ederen, A.M., Gossens, M., Secreve, M., Van der Meer, I., Toussaint, M.J.M., Terlou, M., Gruys, E., 2001a. Cerebrovascular Amyloidosis May Cause A Decrease of Blood Supply Leading to Oxidative Damage and Formation of Amyloid Plaques in the Aged Canine Brain. In: Bely, M., Apathy, A. (Eds.), Amyloid and Amyloidosis IX. Apathy, Budapest, Hungary, p.445-447.
110. Rofina, I.E., Van der Meer, I., Goossens, M., Secreve, M., Van Ederen, A.M., Schilder, M., Gruys, E., 2001b. Preliminary inquiry to assess behavior changes in aging pet dogs. In: Bely, M., Apathy, A. (Eds.), Amyloid and Amyloidosis IX. Apathy, Budapest, Hungary, p. 464-466.
111. Rofina, I.E., Van Andel, I., Van Ederen, A.M., Papaioannou, N., Yamaguchi, H., Gruys, E., 2003. Canine counterpart of senile plaques near capillaries but lack of spatial relationship with activated microglia and macro-phages. Amyloid J Prot Fold Dis, 10:86-96.
112. Romhanyi, G., 1971. Selective differentiation between amyloid and connective tissue structures based on thew collagen specific topo-optical staining reaction with Congo red. Virchows Arch A Pathol Anat, 354:209-222.
113. Romhanyi, G., 1972. Differences in ultrastructural organization of amyloid as revealed by sensitivity or resistance to induced proteolysis. Virchows Arch A Pathol Anat, 357:29-52.
114. Schreuder, B.E.C., 1998. Epidemiological Aspects of Scrapie and BSE Including A Risk Assessment Study. PhD-thesis, Utrecht University, Utrecht (ISBN 90-393-1636-8).
115. Scott, M.R., Will, R., Ironside, J., Nguyen, H.O., Tremblay, P., DeArmond, S.J., Prusiner, S.B., 1999. Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions. Proc Natl Acad Sci USA, 96:15137-15142.
116. Seelig, J., Lehrmann, R., Terzi, E., 1995. Domain formation induced by lipid-ion and lipid-peptide interactions. Mol Membr Biol, 12:51-57.
117. Shtrasburg, S., Pras, M., Brezniak, N., Dolitzki, M., Livneh, A., 1999. Pregnancy and amyloidogenesis: I. Offspring of amyloidotic mice are not predisposed to amyloidosis. J Lab Clin Med, 134:168-172.
118. Skoumalova, A., Rofina, J., Schwippelova, Z., Gruys, E., Wilhelm, J., 2003. The role of free radicals in canine counterpart of senile dementia of the Alzheimer type. Exp Gerontol, 38:711-719.
119. Snow, A.D., Willmer, J., Kisilevsky, R., 1987. Sulfated glycosaminoglycans: a common constituent of all amyloids? Lab Invest, 56:120-123.
120. Snow, A.D., Kinsella, M.G., Parks, E., Sekiguchi, R.T., Miller, J.D., Kimata, K., Wight, T.N., 1995. Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease. Arch Biochem Biophys, 320:84-95.
121. Spiro, D., 1959. The structural basis of proteinuria in man. Electron microscopic studies of renal biopsy specimens from patients with lipid nephrosis, amyloidosis and subacute and chronic glomerulopathies. Am J Pathol, 35:47-74.
122. Tagoe, C.E., French, D., Gallo, G., Buxbaum, J.N., 2004. Amyloidogenesis is neither accelerated nor enhanced by injections of preformed fibrils in mice transgenic for wild-type human transthyretin: the question of infectivity. Amyloid Prot Fold Disord, 11:21-26.
123. Takahashi, Y., Mihara, H., 2004. Construction of a chemically and conformationally self-replicating system of amyloid-like fibrils. Bioorg Medicin Chem, 12:693-699.
124. Taniyama, H., Kitamura, A., Kagawa, Y., Hirayama, K., Yoshino, T., Kamiya, S., 2000. Localized amyloidosis in canine mammary tumors. Vet Pathol, 37:104-107.
125. Tekin, M., Yalcinkaya, F., Cakar, N., Akar, N., Misirlioglu, M., Tastan, H., Turner, N., 2000. MEFV mutations in multiplex families with familial Mediterranean fever: is a particular genotype necessary for amyloidosis? Clin Genet, 57:430-434.
126. Telling, G.C., 2000. Prion protein genes and prion diseases: studies in transgenic mice. Neuropathol Appl Neurobiol, 26:209-20.
127. Torrent, J., Alvarez-Martinez, M.T., Harricane, M.C., Heitz, F., Liautard, J.P., Balny, C., Lange, R., 2004. High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation. Biochemistry, 43:7162-7170.
128. Van Andel, A.C.J., Hoi, P.R., Van der Maas, J.H., Lutz, E.T.G., Krabbendam, H., Gruys, E., 1986. Reaggregation of Bovine Amyloid A Fibril Components to Beta-pleated Sheet Fibrillar Structures. In: Glenner, G.G., Osserman, E.F., Benditt, E.P., Calkins, E., Cohen, A.S., Zucker-Franklin, D. (Eds.), Amyloidosis. Plenum Press, New York, p.39-48.
129. Van Andel, A.C.J., Gruys, E., Kroneman, J., Veerkamp, J., 1988a. Amyloid in the horse: a report of nine cases. Equine Vet J, 20:277-285.
130. Van Andel, A.C.J., Niewold, T.A., Lutz, E.T.G., Van der Maas, J.H., Limburg, P., Gruys, E., 1988b. Fourier Transform Infrared Spectroscopy of Air-dried Heavy Water Suspended AA and AL Amyloid Fibril Preparations of Different Species. In: Isobe, T., Araki, S., Uchino, F., Kito, S., Tsubura, E. (Eds.), Amyloid and Amyloidosis. Plenum Press, New York, p.45-50.
131. Van de Kaa, C.A., Hol, P.R., Huber, J., Linke, R.P., Kooiker, C.J., 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 A Pathol Anat, 408:649-664.
132. Van der Linde-Sipman, J.S., Niewold, T.A., Tooten, P.C., de Neijs-Backer, M., Gruys, E., 1997. Generalized AA-amyloidosis in Siamese and Oriental cats. Vet Immunol Immunopathol, 56:1-10.
133. Van Keulen, L.J.M., Schreuder, B.E.C., Meloen, R.H., Poelen-van den Berg, M., Mooij-Harkes, G., Vromans, M.E.W., Langeveld, J.P.M., 1995. Immunohisto-chemical detection and localization of prion protein in brain tissue of sheep with natural scrapie. Vet Pathol, 32:299-308.
134. Van Nostrand, W.E., Melchor, J.P., Ruffini, L., 1998. Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. J Neurochem, 70:216-223.
135. Ventura, S., Zurdo, J., Narayanan, S., Parreno, M., Mangues, R., Reif, B., Chiti, F., Giannoni, E., Dobson, C.M., Aviles, F.X., Serrano, L., 2004. Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc Natl AcadSci USA, 101:7258-7263.
136. Virchow, R., 1854. Ueber eine im Gehirn und Ruckenmark des Menschen aufgefundene Substanz mit der chemischen Reaction der Cellulose. Virchows Arch Path AnatKlin Med, 6:135-138; 268-271.
137. WHO-IUIS Nomenclature sub-committee, 1993. Nomenclature of amyloid and amyloidosis. Bull World Health Org, 71:105-108.
138. Wilesmith, J.W., Wells, G.A., Cranwell, M.P., Ryan, J.B., 1988. Bovine spongeform encephalopathy: epidemiological. Vet Rec, 123:638-644.
139. Wilesmith, J.W., Ryan, J.B., Atkinson, M.J., 1991. Bovine spongiform encephalopathy: epidemiological studies on the origin. Vet Rec, 128:199-203.
140. Wimley, W.C., Hristova, K., Ladokhin, A.S., Silvestro, L., Axelsen, P.H., White, S.H., 1998. Folding of beta sheet membrane proteins: a hydrophobic hexapeptide model. J Mol Biol, 277:1091-1110.
141. Wisniewski, H.M., Sigurdarson, S., Rubenstein, R., Kascsak, R.J., Carp, R.I., 1996. Mites as vectors for scrapie. Lancet, 347:1114.
142. Wright, J.R., Calkins, E., Humphrey, R.L., 1977. Potassium permanganate reaction in amyloidosis. Lab Invest, 36:274-281.
143. Xing, Y., Nakamura, A, Chiba, T., Kogishi, K., Matsushita, T., Li, F., Guo, Z., Hosokawa, M., Mori, M., Higuchi, K., 2001. Transmission of mouse senile amyloidosis. Lab Invest, 81:493-499.
144. Yu, J., Guo, J.T., Zhu, H., Kindy, M.S., 2000. Amyloid formation in the rat: adenoviral expression of mouse serum amyloid A proteins. Amyloid Int J Exp Clin Invest, 7:32-40.
145. Zekarias, B., Landman, W.J.M., Tooten, P.C.J., Gruys, E., 2000. Leukocyte responses in two breeds of layer chicken that differ in susceptibility to induced amyloid arthropathy. Vet Immunol Immunopathol, 77:55-69.