Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene (original) (raw)
References
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). Google Scholar
Glenner, G.G. Amyloid deposits and amyloidosis — the β-fibrilloses. I. N. Engl. j. Med.302, 1283–1292 (1980). ArticleCAS Google Scholar
Glenner, G.G. Amyloid deposits and amyloidosis — the β-fibrilloses. II. N. Engl. J. Med.302, 1333–1 343 (1980). ArticleCAS Google Scholar
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. Structure4, 989–998 (1996). ArticleCAS Google Scholar
Pepys, M.B. et al. Amyloid P component. A critical review. Amyloid: Int. J. Exp. Clin. Invest. (in the press).
Hawkins, P.N. & Pepys, M.B. Imaging amyloidosis with radiolabelled SAP. Eur. J. Nucl. Med.22, 595–599 (1995). ArticleCAS Google Scholar
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. Lancetii, 376–378 (1984). Article Google Scholar
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). Chapter Google Scholar
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. USA91, 5602–5606 (1994). ArticleCAS Google Scholar
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. USA92, 4299–4303 (1995). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
Kinoshita, C.M. et al. A protease-sensitive site in the proposed Ca2+-binding region of human serum amyloid P component and other pentraxins. Protein Sci.1, 700–709 (1992). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
Nelson, S.R. et al. Serum amyloid P component in chronic renal failure and dialysis. Clin. Chim. Acta200, 191–200 (1991). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
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). CASPubMedPubMed Central Google Scholar
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). ArticleCAS Google Scholar
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). CASPubMedPubMed Central Google Scholar
Janigan, D.T. Experimental amyloidosis: Studies with a modified casein method, casein hydrolysate and gelatin. Am. J. Pathol.47, 159–171 (1965). CASPubMedPubMed Central Google Scholar
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). ArticleCAS Google Scholar
Caspi, D. et al. Imaging of experimental amyloidosis with 131l-serum amyloid P component. Arthritis Rheum.30, 1303–1306 (1987). ArticleCAS Google Scholar
Hawkins, P.N., Myers, M.J., Epenetos, A.A., Caspi, D. & Pepys, M.B. Specific localization and imaging of amyloid deposits in vivo using 123l-labeled serum amyloid P component. J. Exp. Med.167, 903–913 (1988). ArticleCAS Google Scholar
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). Google Scholar
Tan, S.Y., Pepys, M.B. & Hawkins, P.N. Treatment of amyloidosis. Am. J. Kidney Dis.26, 267–285 (1995). ArticleCAS Google Scholar
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). Article Google Scholar
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). ArticleCAS Google Scholar
Booth, D.R. et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature385, 787–793 (1997). ArticleCAS Google Scholar
Hawkins, P.N. & Pepys, M.B. A primed state exists in vivo following histological regression of amyloidosis. Clin. Exp. Immunol.81, 325–328 (1990). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
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). CAS Google Scholar
Duong, T., Pommier, E.C. & Scheibel, A.B. Immunodetection of the amyloid P component in Alzheimer's disease. Acta Neuropathol.78, 429–437 (1989). ArticleCAS Google Scholar
Kalaria, R.N., Galloway, P.G. & Perry, G. Widespread serum amyloid P immunore-activity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders. Neuropathol. Appl. Neurobiol.17, 189–201 (1991). ArticleCAS Google Scholar
Kitamoto, T., Tateishi, J., Hikita, K., Nagara, H. & Takeshita, I. A new method to classify amyloid fibril proteins. Acta Neuropathol.67, 272–278 (1985). ArticleCAS Google Scholar
Fricker, J. From mechanisms to drugs in Alzheimer's disease. The Lancet349, 480 (1997). ArticleCAS Google Scholar
Games, D. et al. Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature373, 523–527 (1995). ArticleCAS Google Scholar
Hsiao, K. et al. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science274, 99–102 (1996). ArticleCAS Google Scholar
Collinge, J. et al. Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature378, 779–783 (1995). ArticleCAS Google Scholar
Axelrad, M.A., Kisilevsky, R., Willmer, J., Chen, S.J. & Skinner, M. Further characterisation of amyloid-enhancing factor. Lab. Invest.47, 139–146 (1982). CASPubMed Google Scholar
Pepys, M.B., Baltz, M., Comer, K., Davies, A.J.S. & Doenhoff, M. Serum amyloid P-component is an acute-phase reactant in the mouse. Nature278, 259–261 (1979). ArticleCAS Google Scholar