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Look Inside Get Access Find out how to access preview-only content Chapter Amyloid and Amyloidosis pp 75-80 Induced AA Amyloid in Hamster: On the Amyloid Enhancing Factor and Protein AA-Cross Reacting Components of Intermediate Molecular Weight 

Th. A. NiewoldAffiliated withDepartment of Veterinary Pathology, University of Utrecht

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, P. C. J. TootenAffiliated withDepartment of Veterinary Pathology, University of Utrecht



, A. C. J. van Andel



, E. GruysAffiliated withDepartment of Veterinary Pathology, University of Utrecht

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$29.95 / €24.95 / £19.95 * Buy eBook Buy this eBook $99.00 / €90.47 / £64.99* * Final gross prices may vary according to local VAT. * Final gross prices may vary according to local VAT. Get Access Abstract In the pathogenesis of AA-amyloidosis serum amyloid protein A (SAA) and the amyloid enhancing factor (AEF) are thought to play essential roles 1. SAA is an acute phase reactant produced in hepatocytes stimulated by cytokines released by inflammatory cells 2,3. SAA is present in the bloodstream mainly as a part of high density lipoprotein. of its structure, amino acid composition and DNA sequence in several species a great deal is known already. In contrast, it is not known where the AEF is produced or by what cells. Furthermore, its exact chemical nature is unknown. In the experimental murine model AEF has been described as a (glyco-) protein, because of its inactivation by proteolytic enzymes 4,5. However, upto now the AEF resists every attempt to ascribe its activity to one specific protein 5. Moreover, regarding the molecular size of the AEF, different data are given in the literature, depending on varying research groups and the source of the AEF, ranging from 10,000 to over 400,000 dalton4,5,6,7,8 . The suggestion was made that AEF could be a small molecule that is easily complexing with itself or normal tissue components1,8. Page %P

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Supplementary Material (0) References (17) Literature 1. 1. R. Kisilevsky, A. D. Snow, L. Subrahmanyan, L. Boudreau, and R. Tan, What factors are necessary for the induction of AA amyloidosis?, in: Amyloidosis, edited by J. Marrink, and M. H. van Rijswijk, p301. Martinus Nijhoff Publishers, Dordrecht (1986)CrossRef

2. 2. P. R. Hol, F. W. J. J. Snel, and E. Gruys, Hamster SAA-stimulating factor and lymphocyte activating factor are different factors, in: IV th International Symposium of Veterinary Laboratory Diagnosticians, edited by G. H. A. Borst et al, pl32. The Royal Netherlands Veterinary Association, Utrecht ( 1986) 3. 3. K. P. W. J. McAdam, J. Li, J. Knowles, N. T. Foss, C. A. Dinarello, L. J. Rosenwasser, M. J. Selinger, M. M. Kaplan, R. Goodman, P. N. Herbert, L. L. Baussermann, and L. M. Nadler, The biology of SAA: identification of the inducer, in vitro synthesis, and heterogeneity demonstrated with monoclonal antibodies. Ann. N. Y. Acad. Sc. 389:127 (1982)CrossRef 4. 4. M. A. Axelrad, and R. Kisilevsky, Biological characterization of amyloid enhancing factor, in: Amyloid and Amyloidosis, edited by G. G. Glenner, P. P. Costa, A. F. de Freitas, p 527. Excerpta Medica, Amsterdam (1980) 5. 5. M. L. Baltz, D. Caspi, C. R. K. Hind, A. Feinstein, and M. B. Pepys, Isolation and characterization of amyloid enhancing factor (AEF), in: Amyloidosis, edited by G. G. Glenner, E. F. Ossermann, E. P. Benditt, E. Calkins, A. S. Cohen, D. Zucker-Franklin, pll5. Plenum Press, New York (1986) 6. 6. P. R. Hol, A. C. J. van Andel, A. M. van Ederen, J. Draaijer, and E. Gruys, Amyloid enhancing factor in hamster, Br. J. Exp. Pathol. 66:689 (1985) 7. 7. K. Kedar, I. Keizman, J. Bleiberg, and E. Sohar, Stimulation of murine amyloidosis by a dialyzable product from pre-treated donors, Br. J. Exp. Pathol. 56:244 (1975) 8. 8. Th.A. Niewold, P. R. Hol, A. C. J. van Andel, E. T. G. Lutz, and E. Gruys, Enhancement of amyloid induction by amyloid fibril fragments in hamster, Lab. Invest. 56:544 (1987) 9. 9. P. R. Hol, F. W. J. J. Snel, Th. A. Niewold, and E. Gruys, Amyloid-enhancing factor (AEF) in the pathogenesis of AA-amyloidosis in the hamster, Virchows Arch. B. 52:273 (1986)CrossRef 10. 10. J. Varga, M. S. M. Flinn, T. Shirahama, O. G. Rodgers, and A. S. Cohen, The induction of accelerate d murine amyloid with human splenic extract, Virchows Arch. B. 51:177 (1986) CrossRef 11. 11.

M. Pras, M. Schubert, D. Zucker-Franklin, A. Rimon, and E. C. Franklin, The characterization of soluble amyloid in water, J. Clin. Invest. 47:924 (1968)CrossRef 12. 12. P. R. Hol, J. P. M. Langeveld, E. W. van Beuningen-Jansen, J. H. Veerkamp, and E. Gruys, A second component in bovine AA amyloid fibrils not identical wi th protein AA is essential for AA amyloid fibrillogenesis, Scand. J. Immunol. 20:53 (1984)CrossRef 13. 13. G. Stokes, An improved Congo red method for amyloid, Med. Lab. Sci. 33:79 (1976) 14. 14. N. Eriksen, and E. P. Benditt, Protein AA and associated proteins in type -AA amyloid substance, in: Amyloidosis, edited by G. G. Glenner, E. F. Ossermann, E. P. Benditt, E. Calkins, A. S. Cohen, and D. Zucker-Franklin, p3. Plenum Press, New York (1986)CrossRef 15. 15. D. L. Scott, G. Marhaug, and G. Husby, Comparative studies of the high molecular weight amyloid fibril proteins and similar components from normal tissues, Clin. Exp. Immunol. 52: 693 (1983) 16. 16. D. L. Scott, A. Husebekk, and G. Husby, Comparison of a reticulin extract of normal tissue and AA amyloid fibrils. IRCS Med. Sci. 13:378 (1985) 17. 17. A. C. J. van Andel, P. R. Hol, J. H. van der Maas, E. T. G. Lutz, H. Krabbendam, and E. Gruys, Reaggregation of bovine amyloid A fibril components to ß-pleated sheet fibrillar structures, in: Amyloidosis, edited by G. G. Glenner, E. F. Ossermann, E. P. Benditt, E. Calkins, A. S. Cohen, and D. Zucker-Franklin, p39. Plenum Press, New York (1986)CrossRef About this Chapter Title Induced AA Amyloid in Hamster: On the Amyloid Enhancing Factor and Protein AA -Cross Reacting Components of Intermediate Molecular Weight Book Title Amyloid and Amyloidosis Book Part II Pages

pp 75-80 Copyright 1988 DOI 10.1007/978-1-4757-0298-9_13 Print ISBN 978-1-4757-0300-9 Online ISBN 978-1-4757-0298-9 Publisher Springer US Copyright Holder Springer Science+Business Media New York Additional Links 

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Editors 

Takashi Isobe (1)



Shukuro Araki (2)

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Fumiya Uchino (3)

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Shozo Kito (4)

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Eiro Tsubura (5)

Editor Affiliations 

1. Kobe University

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2. Kumamoto University

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3. Yamaguchi University

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4. Hiroshima University

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5. Toneyama National Hospital

Authors 

Th. A. Niewold (6)



P. C. J. Tooten (6)



A. C. J. van Andel (6)



E. Gruys (6)

Author Affiliations 

6. Department of Veterinary Pathology, University of Utrecht, Utrecht, The Netherlands

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