Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene

Nature Medicine

Volumn 3, Issue 8, 1997, Pages 855-859

  Botto, Marina ^a   Hawkins, Philip N ^a   Bickerstaff, Maria C M ^a   Herbert, Jeff ^a   Bygrave, Anne E ^a   McBride, Alan ^a   Hutchinson, Winston L ^a   Tennent, Glenys A ^a   Walport, Mark J ^a   Pepys, Mark B ^a  

^a HAMMERSMITH HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID P COMPONENT;

AMYLOIDOSIS; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; GENE DELETION; GENE TARGETING; MOUSE; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN DETERMINATION;

AMYLOID; AMYLOIDOSIS; ANIMALS; CASEINS; DISEASE MODELS, ANIMAL; GENE DELETION; GLYCOPROTEINS; HUMANS; MALE; MICE; MICE, INBRED C57BL; SERUM AMYLOID P-COMPONENT; SILVER NITRATE;

ANIMALIA;

EID: 0030757182     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0897-855     Document Type: Article

References (41)

1. Pepys, M.B. Amyloidosis. in Samter's Immunologic Diseases. (eds. Frank, M.M., Austen, K.F., Claman, H.N. & Unanue, E.R.) 637-655 (Little, Brown and Co., Boston, 1994).
2. Glenner, G.G. Amyloid deposits and amyloidosis - the β-fibrilloses. I. N. Engl. J. Med. 302, 1283-1292 (1980).
3. Glenner, G.G. Amyloid deposits and amyloidosis - the β-fibrilloses. II. N. Engl. J. Med. 302, 1333-1343 (1980).
4. Blake, C.C.F. & Serpell, L.C. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 4, 989-998 (1996).
5. Pepys, M.B. et al. Amyloid P component. A critical review. Amyloid: Int. J. Exp. Clin. Invest. (in the press).
6. Hawkins, P.N. & Pepys, M.B. Imaging amyloidosis with radiolabelled SAP. Eur. J. Nucl. Med. 22, 595-599 (1995).
7. Hind, C.R.K., Collins, P.M., Caspi, D., Baltz, M.L. & Pepys, M.B. Specific chemical dissociation of fibrillar and non-fibrillar components of amyloid deposits. Lancet ii, 376-378 (1984).
8. Pepys, M.B. Amyloid P component: Structure and properties. in Amyloidosis. (eds. Marrink, J. & van Rijswijk, M.H.) 43-50 (Martinus Nijhoff, Dordrecht, the Netherlands, 1986).
9. Pepys, M.B. et al. Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. Proc. Natl. Acad. Sci. USA 91, 5602-5606 (1994).
10. Tennent, G.A., Lovat, L.B. & Pepys, M.B. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer's disease and systemic amyloidosis. Proc. Natl. Acad. Sci. USA 92, 4299-4303 (1995).
11. Hawkins, P.N., Tennent, G.A., Woo, P. & Pepys, M.B. Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis. Clin. Exp. Immunol. 84, 308-316 (1991).
12. 2+-binding region of human serum amyloid P component and other pentraxins. Protein Sci. 1, 700-709 (1992).
13. Hutchinson, W.L., Noble, G.E., Hawkins, P.N. & Pepys, M.B. The pentraxins, C-reactive protein and serum amyloid P component, are cleared and catabolized by hepatocytes in vivo. J. Clin. Invest. 94, 1390-1396 (1994).
14. Nelson, S.R. et al. Serum amyloid P component in chronic renal failure and dialysis. Clin. Chim. Acta 200, 191-200 (1991).
15. Cathcart, E.S., Wollheim, F.A. & Cohen, A.S. Immunoassay of P-component in amyloidotic sera. Proc. Soc. Exp. Biol. Med. 125, 1123-1125 (1967).
16. Hawkins, P.N., Wootton, R. & Pepys, M.B. Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis. J. Clin. Invest. 86, 1862-1869 (1990).
17. Baltz, M.L. et al. Differences in the acute phase responses of serum amyloid P component (SAP) and C3 to injections of casein or bovine serum albumin in amyloid-susceptible and resistant mouse strains. Clin. Exp. Immunol. 39, 355-360 (1980).
18. Coe, J.E. & Ross, M.J. Amyloidosis and female protein in the Syrian hamster: Concurrent regulation by sex hormones. J. Exp. Med. 171, 1257-1267 (1990).
19. Snel, F. et al. Experimental amyloidosis in the hamster: Correlation between hamster female protein levels and amyloid deposition. Clin. Exp. Immunol. 76, 296-300 (1989).
20. Janigan, D.T. Experimental amyloidosis: Studies with a modified casein method, casein hydrolysate and gelatin. Am. J. Pathol. 47, 159-171 (1965).
21. Benson, M.D., Scheinberg, M.A., Shirahama, T., Cathcart, E.S. & Skinner, M. Kinetics of serum amyloid protein A in casein-induced murine amyloidosis. J. Clin. Invest. 59, 412-417 (1977).
22. 131I-serum amyloid P component. Arthritis Rheum. 30, 1303-1306 (1987).
23. 123I-labeled serum amyloid P component. J. Exp. Med. 167, 903-913 (1988).
24. Vigushin, D.M., Pepys, M.B. & Hawkins, P.N. Comparison of histology with SAP scintigraphy for evaluation of amyloidosis. in Amyloid and Amyloidosis 1993. (eds. Kisilevsky, R. et al.) 685-687 (Parthenon Publishing, Pearl River, NY, 1994).
25. Tan, S.Y., Pepys, M.B. & Hawkins, P.N. Treatment of amyloidosis. Am. J. Kidney Dis. 26, 267-285 (1995).
26. Kisilevsky, R., Gruys, E. & Shirahama, T. Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity? Amyloid: Int. J. Exp. Clin. Invest. 2, 128-133 (1995).
27. Ganowiak, K., Hultman, P., Engstrom, U., Gustavsson, A. & Westermark, P. Fibrils from synthetic amyloid-related peptides enhance development of experimental AA amyloidosis in mice. Biochem. Biophys. Res. Commun. 199, 306-312 (1994).
28. Booth, D.R. et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787-793 (1997).
29. Hawkins, P.N. & Pepys, M.B. A primed state exists in vivo following histological regression of amyloidosis. Clin. Exp. Immunol. 81, 325-328 (1990).
30. Hawkins, P.N. et al. Serum amyloid P component scintigraphy and turnover studies for diagnosis and quantitative monitoring of AA amyloidosis in juvenile rheumatoid arthritis. Arthritis Rheum. 36, 842-851 (1993).
31. Coria, F. et al. Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis. Lab. Invest. 58, 454-458 (1988).
32. Duong, T., Pommier, E.G. & Scheibel, A.B. lmmunodetection of the amyloid P component in Alzheimer's disease. Acta Neuropathol. 78, 429-437 (1989).
33. Kalaria, R.N., Galloway, P.C. & Perry, G. Widespread serum amyloid P immunoreactivity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders. Neuropathol. Appl. Neurobiol. 17, 189-201 (1991).
34. Kitamoto, T., Tateishi, J., Hikita, K., Nagara, H. & Takeshita, I. A new method to classify amyloid fibril proteins. Acta Neuropathol. 67, 272-278 (1985).
35. Fricker, J. From mechanisms to drugs in Alzheimer's disease. The Lancet 349, 480 (1997).
36. Games, D. et al. Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature 373, 523-527 (1995).
37. Hsiao, K. et al. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 274, 99-102 (1996).
38. Collinge, J. et al. Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature 378, 779-783 (1995).
39. Axelrad, M.A., Kisilevsky, R., Willmer, J., Chen, S.J. & Skinner, M. Further characterisation of amyloid-enhancing factor. Lab. Invest. 47, 139-146 (1982).
40. Pepys, M.B., Baltz, M., Gomer, K., Davies, A.J.S. & Doenhoff, M. Serum amyloid P-component is an acute-phase reactant in the mouse. Nature 278, 259-261 (1979).
41. Pepys, M.B. Isolation of serum amyloid P component (protein SAP) in the mouse. Immunology 37, 637-641 (1979).