Generation and characterization of rat monoclonal antibodies against human serum amyloid A

Scandinavian Journal of Immunology

Volumn 46, Issue 2, 1997, Pages 175-179

  Yamada, T ^a   Hirano, N ^b   Kuroda, T ^c   Okuda, Y ^d   Itoh, Y ^a  

^a JICHI MEDICAL UNIVERSITY   (Japan)

^b EIKEN CHEMICAL CO LTD   (Japan)

^c Niigata Prefectural Senami Hospital   (Japan)

^d Dohgo Spa Hospital   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; SERUM AMYLOID A;

AMYLOIDOSIS; ANTIBODY SPECIFICITY; ANTIGEN ANTIBODY REACTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; HUMAN; PRIORITY JOURNAL;

EID: 0030864042     PISSN: 03009475     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-3083.1997.d01-108.x     Document Type: Article

References (26)

1. Husebekk A, Skogen B, Husby G, Marhaug G. Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo. Scand J Immunol 1985;21:283-7.
2. Husby G, Marhaug G, Dowton B, Sletten K, Sipe JD. Serum amyloid A (SAA): biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid:Int J Exp Clin Invest 1994;1:119-37.
3. Shiroo M, Kawahara E, Nakanishi I, Migita S. Specific deposition of serum amyloid A protein 2 in the mouse. Scand J Immunol 1987; 26:709-16.
4. Badolato R, Wang JM, Murphy WJ et al. Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J Exp Med 1994;180:203-10.
5. Mitchell TI, Coon CI, Brinckerhoff CE. 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. J Clin Invest 1991;87:1177-85.
6. Zimlichman S, Danon A, Nathan I, Moses G, Shaikin-Kestenbaum R. Serum amyloid A, an acute phase protein, inhibits platelet activation. J Lab Clin Invest 1990;116:180-6.
7. Kisilevsky R, Lindhorst E, Ancsin JB, Young D, Bagshaw W. Acute phase serum amyloid A (SAA) and cholesterol transport during acute inflammation: A hypothesis. Amyloid:Int J Exp Clin Invest 1996; 3:252-60.
8. kB-like transcription factors. J Biol Chem 1991;266:15192-201.
9. Yamada T, Nomata Y, Sugita O, Okada M. A rapid method for measuring serum amyloid A protein by latex agglutination nephelometric immunoassay. Ann Clin Biochem 1993;30:72-6.
10. Yamada T, Kluve-Beckerman B, Liepnieks JJ, Benson MD. Fibril formation from recombinant serum amyloid A. Biochim Biophys Acta 1994;1226:323-9.
11. Yamada T, Liepnieks JJ, Kluve-Beckerman B, Benson MD. Cathepsin B generates the most common form of amyloid A (AA76) from degradation of serum amyloid A. Scand J Immunol 1995;41:94-7.
12. Geysen HM, Rodda SJ, Mason TJ, Tribbick G, Schoofs PG. Strategies for epitope analysis using peptide synthesis. J Immunol Meth 1987;102:259-74.
13. Schagger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987;166:368-79.
14. Yamada T, Liepnieks JJ, Benson MD, Kluve-Beckerman B. Accelerated amyloid deposition in mice treated with the aspartic protease inhibitor, pepstatin. J Immunol 1996;157:901-7.
15. Marhaug G, Gaudernack G, Bogen B, Husby G. Monoclonal hybridoma antibodies to human amyloid related protein SAA. Clin Exp Immunol 1982;50:390-6.
16. Benditt EP, Hoffman JS, Eriksen N. SAA, an apoprotein of HDL: its structure and function. Ann NY Acad Sci 1982;389:183-9.
17. Yamada T, Kluve-Beckerman B, Liepnieks JJ, Benson MD. Possible involvement of cathepsin D-like acid proteases in degradation of serum amyloid A and protection against amyloid formation. Scand J Immunol 1995;41:570-4.
18. Westermark GT, Engström U, Westermark P. The N-terminal segment of protein AA determines its fibrillogenic properly. Biochem Biophys Res Commun 1992;182:27-33.
19. Patel H, Bramall J, Waters H, de Beer MC, Woo P. Expression of recombinant human serum amyloid A in mammalian cells and demonstration of the region necessary for high-density lipoprotein binding and amyloid fibril formation by site-directed mutagenesis. Biochem J 1996;318:1041-9.
20. Isobe T, Husby G, Sletten K. Characterization of an amyloid protein AA similar to SAA. In: Glenner GG, Costa P, Freitas F, eds. Amyloid and Amyloidosis. Amsterdam: Excerpta Media, 1980: 331-6.
21. Westermark P, Sletten K. A serum AA-like protein as a common constituent of secondary amyloid fibrils. Clin Exp Immunol 1982; 49:725-31.
22. Miura K, Ju S-T, Cohen AS, Shirahama T. Generation and use of site-specific antibodies to serum amyloid A for probing amyloid A development. J Immunol 1990;144:610-13.
23. Kisilevsky R, Narindrasorasak S, Tape C, Tan R, Boudreau L. During AA amyloidogenesis is proteolytic attack on serum amyloid A a pre- or post-fibrillogenic event? Amyloid:Int J Exp Clin Invest 1994;1:174-83.
24. Westermark P. The heterogeneity of protein AA in secondary (reactive) amyloidosis. Biochim Biophys Acta 1982;701:19-22.
25. Moyner K, Sletten K, Husby G, Natvig JB. An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenstrom's macroglobulinemia and amyloidosis. Scand J Immunol 1980;11:549-54.
26. Gal R, Shtrasburg S, Luria M et al. Amyloid goiter: report of the clinical, histological and biochemical features of five cases. Amyloid: Int J Exp Clin Invest 1995;2:119-25.