Serum amyloid A, the major vertebrate acute-phase reactant

European Journal of Biochemistry

Volumn 265, Issue 2, 1999, Pages 501-523

  Uhlar, Clarissa M ^a   Whitehead, Alexander S ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Acute phase response; Amyloidosis; Serum amyloid A; Transcriptional regulation

Indexed keywords

ACUTE PHASE PROTEIN; AMYLOID A PROTEIN; APOLIPOPROTEIN; CHEMOKINE; COLLAGENASE; CYTOKINE; ENZYME; FORMYLMETHIONYLLEUCYLPHENYLALANINE; GELATINASE A; GLUCOCORTICOID; INTERLEUKIN 1; INTERLEUKIN 6; LIPID; MESSENGER RNA; STROMELYSIN; TRANSCRIPTION FACTOR;

ACUTE PHASE RESPONSE; AMYLOIDOSIS; ANTIINFLAMMATORY ACTIVITY; GENE; HOST RESISTANCE; HUMAN; IMMUNE SYSTEM; LIPID METABOLISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INDUCTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; TRANSCRIPTION REGULATION;

ACUTE-PHASE PROTEINS; AMYLOIDOSIS; ANIMALS; APOLIPOPROTEINS; ARTERIOSCLEROSIS; ARTHRITIS, RHEUMATOID; CYTOKINES; GENE EXPRESSION REGULATION; GLUCOCORTICOIDS; HUMANS; INFLAMMATION; SERUM AMYLOID A PROTEIN; SIGNAL TRANSDUCTION; TRANSCRIPTION, GENETIC;

MAMMALIA; VERTEBRATA;

EID: 0033569982     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00657.x     Document Type: Review

References (298)

1. 1. Baumann, H. & Gauldie, J. (1994) The acute phase response. Immunol. Today 15, 74-78.
2. 2. Kushner, I. (1982) The phenomenon of the acute phase response. Ann. N.Y. Acad. Sci. 389, 39-48.
3. 3. Cassatella, M.A. (1995) The production of cytokines by polymorphonuclear neutrophils. Immunol. Today 16, 21-26.
4. 4. Steel, D.M. & Whitehead, A.S. (1994) The major acute phase reactants: C-reactive protein, serum amyloid P component and serum amyloid A protein. Immunol. Today 15, 81-88.
5. 5. Gabay, C. & Kushner, I. (1999) Acute-phase proteins and other systemic responses to inflammation. N. Engl. J. Med. 340, 448-454.
6. 6. Aggarwal, B.B. & Natarajan, K. (1996) Tumor necrosis factors: developments during the last decade. Eur. Cytokine Netw. 7, 93-124.
7. 7. Besedofsky, H., Del Ray, A., Sorkin, E. & Dinarello, C.A. (1986) Immunoregulatory feedback between interleukin-1 and glucocorticoid hormones. Science 233, 652-654.
8. 8. Naitoh, Y., Fukata, J., Tominaga, T., Nakai, Y., Tamai, S., Mori, K. & Imura, H. (1988) Interleukin-6 stimulates the secretion of adrenocorticotrophic hormone in conscious, freely-moving rats. Biochem. Biophys. Res. Commun. 155, 1459-1463.
9. 9. Campos, S.P. & Baumann, H. (1992) Insulin is a prominent modulator of the cytokine-stimulated expression of acute-phase plasma protein genes. Mol. Cell Biol. 12, 1789-1797.
10. 10. Husby, G., Marhaug, G., Dowton, B., Sletten, K. & Sipe, J.D. (1994) Serum amyloid A (SAA): biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid: Int. J. Exp. Clin. Invest. 1, 119-137.
11. 11. Hoffman, J.S. & Benditt, E.P. (1982) Changes in high density lipoprotein content following endotoxin administration in the mouse: formation of serum amyloid protein-rich subfractions. J. Biol. Chem. 257, 10510-10517.
12. 12. Marhaug, G. (1983) Three assays for the characterization and quantitation of human serum amyloid A. Scand. J. Immunol. 18, 329-338.
13. 13. Eriksen, N. & Benditt, E.P. (1980) Isolation and characterization of the amyloid-related apoprotein (SAA) from human high density lipoprotein. Proc. Natl Acad. Sci. USA 77, 6860-6864.
14. 14. Coetzee, G.A., Strachan, A.F., van der Westhuyzen, D.R., Hoppe, H.C., Jeenah, M.S. & DeBeer, F.C. (1986) Serum amyloid A-containing human high density lipoprotein 3: density, size and apolipoprotein composition. J. Biol. Chem. 261, 9644-9651.
15. 15. Whitehead, A.S., DeBeer, M.C., Steel, D.M., Rits, M., Lelias, J.M., Lane, W.S. & DeBeer, F.C. (1992) Identification of novel members of the serum amyloid A protein (SAA) superfamily as constitutive apolipoproteins of high density lipoprotein. J. Biol. Chem. 267, 3862-3867.
16. 16. de Beer, M.C., Kindy, M.S., Lane, W.S. & de Beer, F.C. (1994) Mouse serum amyloid A protein (SAA5) structure and expression. J. Biol. Chem. 269, 4661-4667.
17. 17. de Beer, M.C., Yaun, T., Kindy, M.S., Asztalos, B.F., Roheim, P.S. & de Beer, F.C. (1995) Characterization of constitutive human serum amyloid A protein (SAA4) as an apolipoprotein. J. Lipid Res. 36, 526-534.
18. 18. Uhlar, C.M., Burgess, C.J., Sharp, P.M. & Whitehead, A.S. (1994) Evloution of the serum amyloid A (SAA) protein superfamily. Genomics 19, 228-234.
19. 19. Uhlar, C.M., Black, I.L., Shields, D.C., Brack, C.M., Schreiber, D. & Whitehead, A.S. (1996) Wallaby serum amyloid A protein: cDNA cloning, sequence and evolutionary analysis. Scand. J. Immunol. 43, 271-276.
20. 20. Jensen, L.E., Hiney, M.P., Shields, D.C., Uhlar, C.M., Lindsay, A.J. & Whitehead, A.S. (1997) Acute phase proteins in salmonids: evolutionary analyses and acute phase response. J. Immunol. 158, 384-392.
21. 21. Sellar, G.C., DeBeer, M.C., Lelias, J.M., Snyder, P., Glickman, L., Felsberg, P. & Whitehead, A.S. (1991) Dog serum amyloid A protein: identification of multiple isoforms defined by cDNA and protein analyses. J. Biol. Chem. 266, 3505-3510.
22. 22. Marhaug, G., Husby, G. & Dowton, S.B. (1990) Mink serum amyloid A protein: expression and primary structure based on cDNA sequences. J. Biol. Chem. 265, 10049-10054.
23. 23. Rygg, M., Nordstoga, K., Husby, G. & Marhaug, G. (1993) Expression of serum amyloid A genes in mink during induction of inflammation and amyloidosis. Biochim. Biophys. Acta 1216, 402-408.
24. 24. Foyn Bruun, C., Nordstoga, K., Sletten, K., Husby, G. & Marhaug, G. (1995) Serum amyloid A protein in humans and four animal species: a comparison by two dimensional electrophoresis. Comp. Biochem. Physiol. B 112, 227-234.
25. 25. Ray, B.K. & Ray, A. (1991) Complementary DNA cloning and nucleotide sequence of rabbit serum amyloid A protein. Biochem. Biophys. Res. Commun. 178, 68-72.
26. 26. Ray, B.K. & Ray, A. (1991) Rabbit serum amyloid A gene: cloning, characterization and sequence analysis. Biochem. Biophys. Res. Commun. 180, 1258-1264.
27. 27. Mitchell, T.I., Coon, C.I. & Brinckerhoff, C.E. (1991) 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. 87, 1177-1185.
28. 28. Sletten, K., Husebekk, A. & Husby, G. (1989) The primary structure of equine serum amyloid A (SAA) protein. Scand. J. Immunol. 30, 117-122.
29. 29. Hulten, C., Sletten, K., Foyn Bruun, C. & Marhaug. G. (1997) The acute phase serum amyloid A protein (SAA) in the horse: isolation and characterization of three isoforms. Vet. Immunol. Immunopathol. 57, 215-227.
30. 30. Webb, C.F., Tucker, P.W. & Dowton, S.B. (1989) Expression and sequence analyses of serum amyloid A in the Syrian Hamster. Biochemistry 28, 4785-4790.
31. 31. Gervais, C. & Suh, M. (1990) Serum amyloid A protein-related mRNA expression in Herpes simplex virus type 2-transformed hamster cells. Mol. Cell. Biol. 10, 4412-4414.
32. 32. Rossevatn, K., Andresen, P.K., Sletten, K., Husebekk, A., Husby, G., Nordstoga, K., Johnson, K.H., Westermark, G.T. & Westermark, P. (1992) The complete amino acid sequence of bovine serum amyloid protein A (SAA) and of subspecies of the tissue-deposited amyloid fibril protein A. Scand. J. Immunol. 35, 217-224.
33. 33. Yamamoto, M., Katoh, N. & Adachi, Y. (1998) The presence of two low molecular mass proteins immunologically related to 14 kilodalton serum amyloid A in the lipoprotein fraction and their decreased serum concentrations in calves with experimentally induced pneumonia. J. Vet. Med. Sci. 60, 181-187.
34. 34. Syversen, P.V., Juul, J., Marhaug, G., Husby, G. & Sletten, K. (1994) The primary structure of serum amyloid A protein in sheep: comparison with serum amyloid A in other species. Scand. J. Immunol. 39, 88-94.
35. 35. Harris, A.J., Shaddock, J.G., Manjanatha, M.G., Lisenbey, J.A. & Casciano, D.A. (1998) Identification of differentially expressed genes in aflatoxin B-1-treated cultured primary rat hepatocytes and Fischer 344 rats. Carcinogenesis 19, 1451-1458.
36. 36. Sipe, J.D. & Committee. (1999) Revised nomenclature for serum amyloid A (SAA). Editorial Letter. Amyloid: Int. J. Exp. Clin. Invest. 6, 67-69.
37. 37. Sellar, G.C., Jordan, S.A., Bickmore, W.A., van Fantes, J.A., Heyningen, V. & Whitehead, A.S. (1994) The human serum amyloid A protein (SAA) superfamily gene cluster: mapping to chromosome 11p15.1 by physical and genetic linkage analysis. Genomics 19, 221-227.
38. 38. Sellar, G.C., Oghene, K., Boyle, S., Bickmore, W.A. & Whitehead, A.S. (1994) Organization of the region encompassing the human serum amyloid A (SAA) gene family on chromosome 11p15.1. Genomics 23, 492-495.
39. 39. Junien, C. & Heyningen, V. (1991) Report of the committee on the genetic constitution of chromosome 11. Cytogenet. Cell Genet. 58, 459-554.
40. 40. Taylor, B.A. & Rowe, L. (1984) Genes for serum amyloid A proteins map to chromosome 7 in the mouse. Mol. Gen. Genet. 195, 491-499.
41. 41. Butler, A., Rochelle, J.M., Seldin, M.F. & Whitehead, A.S. (1995) The gene encoding the mouse serum amyloid-A protein, Apo-SAA (5), maps to proximal chromosome-7. Immunogenetics 42, 153-155.
42. 42. Butler, A. & Whitehead, A.S. (1996) Mapping of the mouse serum amyloid A gene cluster by long-range polymerase chain reaction. Immunogenetics 44, 468-474.
43. 1 alleles. Amyloid: Int. J. Exp. Clin. Invest. 1, 255-262.
44. 44. Faulkes, D.J. & Woo, P. (1997) Do alleles at the serum amyloid A locus influence susceptibility to reactive amyloidosis in systemic onset juvenile chronic arthritis? Amyloid: Int. J. Exp. Clin. Invest. 4, 75-79.
45. 45. Lowell, C.A., Potter, D.A., Stearman, R.S. & Morrow, J.F. (1986) Structure of the murine serum amyloid A gene family: gene conversion. J. Biol. Chem. 261, 8442-8452.
46. 46. Lowell, C.A., Stearman, R.S. & Morrow, J.F. (1986) Transcriptional regulation of serum amyloid A gene expression. J. Biol. Chem. 261, 8453-8461.
47. 47. Stearman, R.S., Lowell, C.A., Peltzman, C.G. & Morrow, J.F. (1986) The sequence of a new serum amyloid A gene. Nucleic Acids Res. 14, 797-809.
48. 48. Meek, R.L. & Benditt, E.P. (1986) Amyloid A gene family expression in different mouse tissues. J. Exp. Med. 164, 2006-2017.
49. 49. Meek, R.L., Eriksen, N. & Benditt, E.P. (1989) Serum amyloid A in the mouse. Sites of uptake and mRNA expression. Am. J. Pathol. 135, 411-419.
50. 50. Ramadori, G., Sipe, J.D. & Colten, H.R. (1985) Expression and regulation of the murine serum amyloid A (SAA) gene in extrahepatic sites. J. Immunol. 135, 3645-3647.
51. 51. Meek, R.L., Eriksen, N. & Benditt, E.P. (1992) Murine serum amyloid A3 is a high density apolipoprotein and is secreted by macrophages. Proc. Natl Acad. Sci. USA 89, 7949-7952.
52. 52. Brinckerhoff, C.E., Mitchell, T.I., Karmilowicz, M.J., Kluve-Beckerman, B. & Benson, M.D. (1989) Autocrine induction of collagenase by serum amyloid A-like and β2-microglobulin-like proteins. Science 243, 655-657.
53. 53. Meek, R.L. & Benditt, E.P. (1989) Rat tissues express serum amyloid A protein-related mRNAs. Proc. Natl Acad. Sci. USA. 86, 1890-1894.
54. 54. Sack, G.H. Jr & Talbot, C.C. Jr (1989) The human serum amyloid A (SAA)-encoding gene GSAA1: nucleotide sequence and possible autocrine-collagenase-inducer function. Gene 84, 509-515.
55. 55. Kluve-Beckerman, B., Drumm, M.L. & Benson, M.D. (1991) Nonexpression of the human serum amyloid A three (SAA3) gene. DNA Cell Biol. 10, 651-661.
56. 56. de Beer, M.C., de Beer, F.C., Gerardot, C.J., Cecil, D.R., Webb, N.R., Goodson, M.L. & Kindy, M.S. (1996) Structure of the mouse Saa4 gene and its linkage to the serum amyloid A gene family. Genomics 34, 139-142.
57. 57. Turnell, W.G., Sarra, R., Glover, I.D., Baum, J.O., Caspi, D., Baltz, M.L. & Pepys, M.B. (1986) Secondary structure prediction of human SAA1. Presumptive identification of calcium and lipid binding sites. Mol. Biol. Med. 3, 387-407.
58. 58. Glenner, G.G. (1980) Amyloid deposits and amyloidosis. N. Engl. J. Med. 302, 1283-1292 and 1333-1343.
59. 59. Meeker, A.K. & Sack, G.H. (1998) A fusion protein between serum amyloid A and staphylococcal nuclease: synthesis, purification and structural studies. Proteins 30, 381-387.
60. 60. Husebekk, A., Skogen, B., Husby, G. & Marhaug, G. (1985) Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo. Scand. J. Immunol. 21, 283-287.
61. 61. Tape, C., Tan, R., Nesheim, M. & Kisilevsky, R. (1988) Direct evidence for circulating apoSAA as the precursor of tissue AA amyloid deposits. Scand. J. Immunol. 28, 317-324.
62. 62. Liepnieks, J.J., Kluve-Beckerman, B. & Benson, M.D. (1995) Characterization of amyloid A protein in human secondary amyloidosis: the predominant deposition of serum amyloid A1. Biochim. Biophys. Acta 1270, 81-86.
63. 63. Westermark, G.T., Sletten, K., Grubb, A. & Westermark, P. (1990) AA-amyloidosis. Tissue component-specific association of various protein AA subspecies and evidence of a fourth SAA gene product. Am. J. Pathol. 137, 377-383.
64. 64. Westermark, G.T., Engstrom, U. & Westermark, P. (1992) The N-terminal segment of protein AA determines its fibrillogenic property. Biochem. Biophys. Res. Commun. 182, 27-33.
65. 65. Patel, H., Bramall, J., Waters, H., De Beer, M.C. & Woo, P. (1996) 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. 318, 1041-1049.
66. 66. Husebekk, A., Skogen, B. & Husby, G. (1987) Characterisation of amyloid proteins AA and SAA as apolipoproteins of HDL. Displacement of SAA from the HDL-SAA by ApoAI and ApoAII. Scand. J. Immunol. 25, 375-381.
67. 3+ as a specific probe for time-resolved fluorometric immunoassay. J. Immunol. Methods 182, 131-144.
68. 68. Malle, E., Herz, R., Artl, A., Ibovnik, A., Andreae, F. & Sattler, W. (1998) Mapping of antigenic determinants of purified, lipid-free human serum amyloid A proteins. Scand. J. Immunol. 48, 557-561.
69. 69. Preciado-Patt, L., Levartowsky, D., Prass, M., Hershkoviz, R., Lider, O. & Fridkin, M. (1994) Inhibition of cell ahhesion to glycoproteins of the extracellular matrix by peptides corresponding to serum amyloid A. Eur. J. Biochem. 223, 35-42.
70. 70. Syversen, P.V., Saeter, U., Cunha-Ribeiro, L., Orvim, U.j., Sletten, Kj. Husby, G. & Sakariassen, K.S. (1994) The effect of serum amyloid protein A fragment-SAA25-76 on blood platelet aggregation. Thromb. Res. 76, 299-305.
71. 71. Zimlichman, S., Danon, A., Nathan, I., Mozes, G. & Shainkin-Kestenbaum, R. (1990) Serum amyloid A, an acute phase protein, inhibits platelet activation. J. Lab. Clin. Med. 116, 180-186.
72. 72. Shainkin-Kestenbaum, R., Zimlichman, S., Lis, M., Preciado-Patt, L., Fridkin, M. & Berenheim, J. (1997) Modulation of prostaglandin I2 production from bovine aortic endothelial cells by serum amyloid A and its N-terminal tetradecapeptide. Biomed. Peptide Protein Nucleic Acids 2, 101-106.
73. 73. Kula, R.W., Engel, W.K. & Line, B.P. (1977) Scanning for soft-tissue amyloid. Lancet I, 92-93.
74. 74. Pepys, M.B., Baltz, M., Gomer, K., Davies, A.J.S. & Doenhoff, M. (1979) Serum amyloid P-component is an acute-phase reactant in the mouse. Nature (London) 278, 259-261.
75. 75. Danielsen, B., Sorensen, I.J., Nybo, M., Nielsen, E.H., Kaplan, B. & Svehag, S.E. (1997) Calcium-dependent and -independent binding of the pentraxin serum amyloid P component to glycosaminoglycans and amyloid proteins: enhanced binding at slightly acid pH. Biochim. Biophys. Acta 1339, 73-78.
76. 76. Malle, E., Bollmann, A., Steinmetz, A., Gemsa, D., Leis, H.-J. & Sattler, W. (1997) Serum amyloid A (SAA) protein enhances formation of cyclooxygenase metabolites of activated human monocytes. FEBS Lett. 419, 215-219.
77. 3) to human neutrophils. Int. J. Peptide Protein Res. 48, 503-513.
78. 78. Ancsin, J.B. & Kisilevsky, R. (1999) Laminin interactions important for basement membrane assembly are promoted by zinc and implicate laminin zinc finger-like sequences. J. Biol. Chem. 271, 6845-6851.
79. 79. Morrow, J.F., Stearman, R.S., Peltzman, C.G. & Potter, D.A. (1981) induction of hepatic synthesis of serum amyloid A protein and actin. Proc. Natl Acad. Sci. USA 78, 4718-4722.
80. 80. Bausserman, L.L., Van Saritelli, A.L., Zuiden, P., Gollaher, C.J. & Herbert, P.N. (1987) Degradation of serum amyloid A by isolated perfused rat liver. J. Biol. Chem. 262, 1583-1589.
81. 81. Raynes, J.G. & Cooper, E.H. (1983) Comparison of serum amyloid A protein and C-reactive protein concentrations in cancer and non-malignant disease. J. Clin. Pathol. 36, 798-803.
82. 82. Herbert, P.N., Bernier, D.N., Cullinane, E.M., Edelstein, L., Kantor, M. A. & Thompson, P.D. (1984) High-density lipoprotein metabolism in runners and sedentary men. J. Am. Med. Assoc. 252, 1034-1037.
83. 83. Tape, C. & Kisilevsky, R. (1990) Apolipoprotein A-I and apolipoprotein SAA half-lives during acute inflammation and amyloidogenesis. Biochim. Biophys. Acta 1043, 295-300.
84. 84. Gollaher, C.J. & Bausserman, L.L. (1990) Hepatic cataholism of serum amyloid A during an acute phase response and chronic inflammation. Proc. Soc. Exp. Biol. Med. 194, 245-250.
85. 85. Numerof, R.P., Sipe, J.D., Trehu, E.G., Dinarello, C.A. & Mier, J.W. (1992) Suppression of IL-2-induced SAA gene expression in mice by the administration of an IL-1 receptor antagonist. Cytokine 4, 555-560.
86. 86. Fantuzzi, G., Benigni, F., Sironi, M., Conni, M., Carelli, M., Cantoni, L., Shapiro, L., Dinarello, C.A., Sipe, J.D. & Ghezzi, P. (1995) Cilliary neurotrophic factor (CNTF) induces serum amyloid A3, hypoglycaemia, and anorexia, and potentiates IL-1 induced corticosterone and IL-6 production in mice. Cytokine 7, 150-156.
87. 87. Foyn Bruun, C., Sletten, K. & Marhaug, G. (1998) Mouse serum amyloid A (SAA) proteins isolated by two-dimensional electrophoresis: characterization of isotypes and the effect of separate and combined administrations of cytokines, dexamethasone and lipopolysaccharide (LPS) on serum levels and isotype distribution. Clin. Exp. Immunol. 111, 231-236.
88. 88. Benigni, F., Fantuzzi, G., Sacco, S., Sironi, M., Pozzi, P., Dinarello, C.A., Sipe, J.D., Poli, V., Cappelletti, M., Paonessa, G., Pennica, D., Panayotatos, N. & Ghezzi, P. (1996) Six different cytokines that share GP130 as a receptor subunit, induce serum amyloid A and potentiate the induction of interleukin-6 and the activation of the hypothalamus-pituitary-adrenal axis by interleukin-1. Blood 87, 1851-1854.
89. 89. Colten, H.R. (1992) Tissue-specific regulation of inflammation. J. Appl. Physiol. 72, 1-7.
90. 90. Benditt, E.P. & Meek, R.L. (1989) Expression of the third member of the serum amyloid A gene family in mouse adipocytes. J. Exp. Med. 169, 1841-1846.
91. 91. Marhaug, G., Hackett, B. & Dowton, S.B. (1997) Serum amyloid gene expression in rabbit, mink and mouse. Clin. Exp. Immunol. 107, 425-434.
92. 92. Hill, M.R., Wu, X., Sullivan, M., King, B.O., Webb, C.F. & Gimble, J.M. (1996) Expression of acute phase proteins by bone marrow stromal cells. J. Endotoxin Res. 3, 425-433.
93. 93. Wang, Q., Meyer, T.A., Boyce, ST., Wang, J.J., Sun, X., Tiao, G., Fischer, J.E. & Hasselgren, P.-O. (1998) Endotoxemia in mice stimulates production of complement C3 and serum amyloid A in mucosa of small intestine. Am. J. Physiol. 44, R1584-R1592.
94. 94. Hardardottir, I., Sipe, J., Moser, A.H., Fielding, C.J., Feingold, K.R. & Grunfeld, C. (1997) LPS and cytokines regulate extra hepatic mRNA levels of apolipoproteins during the acute phase response in Syrian hamsters. Biochim. Biophys. Acta 1344, 210-220.
95. 95. Rygg, M., Husby, G. & Marhaug, G. (1993) Differential expression of rabbit serum amyloid A genes in response to various inflammatory agents. Scand. J. Immunol. 38, 417-422.
96. 96. Urieli-Shoval, S., Meek, R.L., Hanson, R.H., Eriksen, N. & Benditt, E.P. (1994) Human serum amyloid A genes are expressed in monocyte/macrophage cell lines. Am. J. Pathol. 145, 650-660.
97. 97. Ray, B.K. & Ray, A. (1997) Involvement of an SAF-like transcription factor in the activation of serum amyloid A gene in monocyte/macrophage cells by lipopolysaccharide. Biochem. J. 36, 4662-4668.
98. 98. Meek, R.L., Urieli-Shoval, S. & Benditt, E.P. (1994) Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: implications for serum amyloid A function. Proc. Natl Acad. Sci. USA 91, 3186-3190.
99. 99. Yamada, T., Kakihara, T., Kamishima, T., Fukuda, T. & Kawai, T. (1996) Both acute phase and constitutive serum amyloid A are present in atherosclerotic lesions. Pathol. Int. 46, 797-800.
100. 100. Steel, D.M., Donoghue, C.F., O'Neill, R.M., Uhlar, C.M. & Whitehead, A.S. (1996) Expression and regulation of constitutive and acute phase serum amyloid A mRNAs in hepatic and non-hepatic cell lines. Scand. J. Immunol. 44, 493-500.
101. 101. Urieli-Shoval, S., Cohen, P., Eisenberg, S. & Matzner, Y. (1998) Widespread expression of serum amyloid A in histologically normal human tissues: predominant localization to the epithelium. J. Histochem. Cytochem. 46, 1377-1384.
102. 102. Taga, T. (1997) GP130 and the interleukin-6 family of cytokines. Annu. Rev. Immunol. 15, 797-819.
103. 103. Ramadori, G., Damme, J., Rieder, H. & Meyer zum Buschenfelde, K.-H. (1988) Interleukin 6, the third mediator of acute-phase reaction, modulates hepatic protein synthesis in human and mouse. Comparison with interleukin 1β and tumor necrosis factor-α. Eur. J. Immunol. 18, 1259-1264.
104. 104. Ganapathi, M.K., May, L.T., Schultz, D., Brabenec, A., Weinstein, J., Sehgal, P.B. & Kushner, I. (1988) Role of interleukin-6 in regulating synthesis of C-reactive protein and serum amyloid A in human hepatoma cell lines. Biochem. Biophys. Res. Commun. 157, 271-277.
105. 105. Ganapathi, M.K., Schultz, D., Mackiewicz, A., Samols, D., Hu, S.-I., Brabanec, A., MacIntyre, S.S. & Kushner, I. (1988) Heterogeneous nature of the acute phase response. Differential regulation of human serum amyloid A, C-reactive protein and other acute phase proteins by cytokines in Hep3B cells. J. Immunol. 141, 564-569.
106. 106. Ganapathi, M.K., Rzewnicki, D., Samols, D., Jiang, S.L. & Kushner, I. (1991) Effect of combinations of cytokines and hormones on synthesis of serum amyloid A and C-reactive protein in Hep3B cells. J. Immunol. 147, 1261-1265.
107. 107. Raynes, J.G., Eagling, S. & McAdam, K.P.W.J. (1991) Acute-phase protein synthesis in human hepatoma cells: differential regulation of serum amyloid A (SAA) and haptoglobin by interleukin-1 and interleukin-6. Clin. Exp. Immunol. 83, 448-491.
108. 108. Steel, D.M. & Whitehead, A.S. (1991) Heterogeneous modulation of acute-phase-reactant mRNA levels by interleukin-1β and interleukin-6 in the human hepatoma cell line PLC/PRF/5. Biochem. J. 277, 477-482.
109. 109. Rokita, H., Loose, L.D., Bartle, L.M. & Sipe, J.D. (1994) Synergism of interleukin 1 and interleukin 6 induces serum amyloid A production while depressing fibrinogen: a quantitative analysis. J. Rheumatol. 21, 400-405.
110. 110. Conti, P., Bartle, L., Barbacane, R.C., Reale, M., Placido, F.C. & Sipe, J. (1995) Synergistic activation of serum amyloid A (SAA) by IL-6 and IL-1 in combination on human Hep 3B hepatoma cell line. Role of PGE2 and IL-1 receptor antagonist. Immunol. Invest. 24, 523-535.
111. 111. Jiang, S.-L., Lozanski, G., Samols, D. & Kushner, I. (1995) Induction of human serum amyloid A in Hep3B cells by IL-6 and IL-1β involves both transcriptional and post-transcriptional mechanisms. J. Immunol. 154, 825-831.
112. 112. Betts, J.C., Cheshire, J.K., Akira, S., Kishimoto, T. & Woo, P. (1993) The role of NF-κB and NF-IL6 transactivating factors in the synergistic activation of human serum amyloid A gene expression by interleukin-1 and interleukin-6. J. Biol. Chem. 268, 25624-25631.
113. 113. Ray, A. & Ray, B.K. (1996) A novel cis-acting element is essential for cytokine-mediated transcriptional induction of the serum amyloid A gene in nonhepatic cells. Mol. Cell Biol. 16, 1584-1594.
114. 114. Uhlar, C.M., Grehan, S., Steel, D.M., Steinkasserer, A. & Whitehead, A.S. (1997) Use of the acute phase serum amyloid A2 (SAA2) gene promoter in the analysis of pro-and anti-inflammatory mediators: differential kinetics of SAA2 promoter induction by IL-1β and TNFα compared to IL-6. J. Immunol. Methods 203, 123-130.
115. 115. Steel, D.M., Roger, J.T., DeBeer, M.C., DeBeer, F.C. & Whitehead, A.S. (1993) Biosynthesis of human acute-phase serum amyloid A protein (A-SAA) in vitro: the roles of mRNA accumulation, poly (A) tail shortening and translational efficiency. Biochem. J. 291, 701-707.
116. 116. Gabay, C., Genin, B., Mentha, G., Iynedjian, P.B., Roux-Lombard, P. & Guerne, P.A. (1995) IL-1 receptor antagonist (IL-IRa) does not inhibit the production of C-reactive protein or serum amyloid A protein by human primary hepatocytes. Differential regulation in normal and tumour cells. Clin. Exp. Immunol. 100, 306-313.
117. 117. Yap, S.H., Moshage, H.J., Hazenberg, B.C.P., Roelofs, H.M.J., Bijzet, J., Limburg, P.C., van Aarden, L.A. & Rijswijk, M.H. (1991) Tumor necrosis factor (TNF) inhibits interleukin (IL)-1 and/or IL-6 stimulated synthesis of C-reactive protein (CRP) and serum amyloid A (SAA) in primary cultures of human hepatocytes. Biochim. Biophys. Acta 1091, 405-408.
118. 118. Fratelli, M., Zinetti, M., Fantuzzi, G., Spina, C., Napoletano, G., Donatiello, G., Ravagnan, R., Sipe, J.D., Casey, C.A. & Ghezzi, P. (1997) Time course of circulating acute phase proteins and cytokines in septic patients. Amyloid: Int. J. Exp. Clin. Invest. 4, 33-97.
119. 119. Castell, J.V., Gomez-Lechon, M.J., David, M., Andus, T., Geiger, T., Trullenque, R., Fabra, R. & Heinrich, P.C. (1989) Interleukin-6 is the major regulator of acute phase protein synthesis in adult human hepatocytes. FEBS Lett. 242, 237-239.
120. 120. Utsunomiya, I., Nagai, S. & Oh-Ishi, S. (1991) Sequential appearance of IL-1 and IL-6 activities in rat carrageenin-induced pleurisy. J. Immunol. 147, 1803-1809.
121. 121. Jarvis, J.N., Wang, W.L., Moore, H.T., Zhao, L. & Xu, C. (1997) In vitro induction of proinflammatory cytokine secretion by juvenile rheumatoid arthritis synovial immune complexes. Arthritis Rheum. 40, 2039-2049.
122. 122. Schindler, R., Mancilla, J., Endres, S., Ghorbani, R., Clark, S.C. & Dinarello, C.A. (1990) Correlations and interactions in the production of interleukin-6 (IL-6), IL-1, and tumor necrosis factor (TNF) in human blood mononuclear cells: IL-6 suppresses IL-1 and TNF. Blood 75, 40-47.
123. 123. Uhlar, C.M. & Whitehead, A.S. (1999) The kinetics and magnitude of the synergistic activation of the serum amyloid A promoter by IL-1β and IL-6 is determined by the order of cytokine addition. Scand. J. Immunol. 49, 399-404.
124. 124. Ikeda, S., Chisuwa, H., Kawasaki, S., Ozawa, J., Hoshii, Y., Yokota, T. & Aoi, T. (1997) Systemic reactive amyloidosis associated with Castleman's disease: serial changes of the concentrations of acute phase serum amyloid A and interleukin 6 in serum. J. Clin. Pathol. 50, 965-967.
125. 125. Haziot, A., Lin, X.Y., Zhang, F. & Goyert, S.M. (1998) Cutting edge: The induction of acute phase proteins by lipopolysaccharide uses a novel pathway that is CD14-independent. J. Immunol. 160, 2570-2572.
126. 126. Fattori, E., Cappelletti, M., Costa, P., Sellitto, C., Cantoni, L., Carelli, M., Faggioni, R., Fantuzzi, G., Ghezzi, P. & Poli, V. (1994) Defective inflammatory response in interleukin 6-deficient mice. J. Exp. Med. 180, 1243-1250.
127. 127. Kopf, M., Baumann, H., Freer, G., Freudenberg, M., Lamers, M., Kishimoto, T., Zinkernagel, R., Bluethmann, H. & Kohler, G. (1994) Impaired immune and acute-phase responses in interleukin-6-deficient mice. Nature (London) 368, 339-342.
128. 128. Fantuzzi, G., Zheng, H., Faggioni, R., Benigni, F., Ghezzi, P., Sipe, J.D., Shaw, A.R. & Dinarello, C.A. (1996) Effect of endotoxin in IL-1 β-deficient mice. J. Immunol. 157, 291-296.
129. 129. Fantuzzi, G., Ku, G., Harding, M.W., Livingston, D.J., Sine, J.D., Kuida, K., Flavell, R.A. & Dinarello, C.A. (1997) Response to local inflammation of IL-1 beta-converting enzyme-deficient mice. J. Immunol. 158, 1818-1824.
130. 130. Bopst, M., Haas, C., Car, B. & Eugster, H.-P. (1998) The combined inactivation of tumor necrosis factor and interleukin-6 prevents induction of the major acute phase proteins by endotoxin. Eur. J. Immunol. 28, 4130-4137.
131. 131. Dinarello, C.A. (1996) Biological basis for interleukin-1 in disease. Blood 87, 2095-2147.
132. 132. Arend, W.P., Malyak, M., Guthridge, C.J. & Gabay, C. (1998) Interleukin-1 receptor antagonist: role in biology. Annu. Rev. Immunol. 16, 27-55.
133. 133. Dripps, D.J., Brandhuber, B.J., Thompson, R.C. & Eisenberg, S.P. (1991) Interleukin-1 (IL-1) receptor antagonist binds to the 80-kDa IL-1 receptor but does not initiate IL-1 signal transduction. J. Biol. Chem. 266, 10331-10336.
134. 134. Dripps, D.J., Verderber, E., Ng, R.K., Thompson, R.C. & Eisenberg, S.P. (1991) Interleukin-1 receptor antagonist binds to the type II interleukin-1 receptor on B cells and neutrophils. J. Biol. Chem. 266, 20311-20315.
135. 135. Granowitz, E.V., Clark, B.D., Vannier, E., Callahan, M.V. & Dinarello, C.A. (1992) Effect of interleukin-1 (IL-1) blockade on cytokine synthesis: I. IL-1 receptor antagonist inhibits IL-1-induced cytokine synthesis and blocks the binding of IL-1 to its type II receptor on human monocytes. Blood 79, 2356-2363.
136. 136. Butcher, C., Steinkasserer, A., Tejura, S. & Lennard, A.C. (1994) Comparison of two promoters controlling expression of secreted or intracellular IL-1 receptor antagonist. J. Immunol. 153, 701-711.
137. 137. Seckinger, P., Lowenthal, J.W., Williamson, K., Dayer, J.M. & MacDonald, H.R. (1987) A urine inhibitor of interleukin 1 activity that blocks ligand binding. J. Immunol. 139, 1546-1549.
138. 138. Mazzei, G.J., Seckinger, P.L., Dayer, J.M. & Shaw, A.R. (1990) Purification and characterization of a 26-kDa competitive inhibitor of interleukin 1. Eur. J. Immunol. 20, 683-689.
139. 139. Haskill, S., Van Martin, G., Le, L., Morris, J., Peace, A., Bigler, C.F., Jaffe, G.J., Hammerberg, C., Sporn, S.A., Fong. S., Arend, W.P. & Ralph, P. (1991) cDNA cloning of an intracellular form of the human interleukin 1 receptor antagonist associated with epithelium. Proc. Natl Acad. Sci. USA 88, 3681-3685.
140. 140. Bertini, R., Sironi, M., Martin-Padura, I., Colotta, F., Rambaldi, S., Bernasconi, S., Ghezzi, P., Haskill, S.J., Liu, D. & Mantovani, A. (1992) Inhibitory effect of recombinant intracellular interleukin 1 receptor antagonist on endothelial cell activation. Cytokine 4, 44-47.
141. 141. Zahedi, K., Seldin, M.F., Rits, M., Ezekowitz, R.A. & Whitehead, A.S. (1991) Mouse IL-1 receptor antagonist protein. Molecular characterization, gene mapping, and expression of mRNA in vitro and in vivo. J. Immunol. 146, 4228-4233.
142. 142. Colotta, F., Dower, S.K., Sims, J.E. & Mantovani, A. (1994) The type II 'decoy' receptor: a novel regulatory pathway for interleukin-1. Immunol. Today 15, 562-566.
143. 143. Grehan, S., Uhlar, C.M., Sim, R.B., Herbert, J. & Whitehead, A.S. (1997) Expression of a biologically active recombinant mouse IL-1 receptor antagonist and its use in vivo to modulate aspects of the acute phase response. J. Immunol. 159, 369-378.
144. 144. Grehan, S., Herbert, J. & Whitehead, A.S. (1997) Down-regulation of the major circulating precursors of proteins deposited in secondary amyloidosis by a recombinant mouse interleukin-1 receptor antagonist. Eur. J. Immunol. 27, 2593-2599.
145. 145. Edbrooke, M.R., Foldi, J., Cheshire, J.K., Li, F., Faulkes, D.J. & Woo, P. (1991) Constitutive and NF-κB-like proteins in the regulation of the serum amyloid A gene by interleukin-1. Cytokine 3, 380-388.
146. 146. Woo, P., Sipe, J., Dinarello, C.A. & Colten, H.R. (1987) Structure of a human serum amyloid A gene and modulation of its expression in transfected L cells. J. Biol. Chem. 262, 15790-15795.
147. 147. Edbrooke, M.R. & Woo, P. (1989) Regulation of human SAA gene expression by cytokines. In Acute Phase Proteins in the Acute Phase Response (Pepys, M., ed.), pp. 21-27. Springer-Verlag, London.
148. 148. Edbrooke, M.R., Burt, D.W., Cheshire, J.K. & Woo, P. (1989) Identification of cis-acting sequences responsible for phorbol ester induction of human serum amyloid A gene expression via a nuclear factor κB-like transcription factor. Mol. Cell. Biol. 9, 1908-1916.
149. 149. Xia, C., Cheshire, J.K., Patel, H. & Woo, P. (1997) Cross-talk between transcription factors NF-κB and C/EBP in the transcriptional regulation of genes. Int. J. Biochem. Cell Biol. 29, 1525-1539.
150. 150. Huang, J.H., Rienhoff, H.Y. & Liao, W.S.-L. (1990) Regulation of mouse serum amyloid A gene expression in transfected hepatoma cells. Mol. Cell Biol. 10, 3619-3625.
151. 151. Li, X., Huang, J.H., Rienhoff, H.Y. Jr & Liao, W.S.-L. (1990) Two adjacent C/EBP-binding sequences that participate in the cell-specific expression of the mouse serum amyloid A3 gene. Mol. Cell Biol. 10, 6624-6631.
152. 152. Huang, J.H. & Liao, W.S.-L. (1994) Induction of the mouse serum amyloid A3 gene by cytokines requires both C/EBP family proteins and a novel consitutive nuclear factor. Mol. Cell Biol. 14, 4475-4484.
153. 153. Shimizu, H. & Yamamoto, K. (1994) NF-κB and C/EBP transcription factor families synergistically function in mouse serum amyloid A gene expression induced by inflammatory cytokines. Gene 149, 305-310.
154. 154. Li, X. & Liao, W.S.-L. (1991) Expression of rat serum amyloid A1 gene involves both C/EBP-like and NFκB-like transcription factors. J. Biol. Chem. 266, 15192-15201.
155. 155. Li, X. & Liao, W.S.-L. (1992) Cooperative effects of C/EBP-like and NFκB-like binding sites on rat serum amyloid A1 gene expression in liver cells. Nucleic Acids Res. 20, 4765-4772.
156. 156. Lu, S.-Y., Rodriguez, M. & Liao, W.S.-L. (1994) YY1 represses rat serum amyloid A1 gene transcription and is antagonized by NF-kB during acute-phase response. Mol. Cell Biol. 14, 6253-6263.
157. 157. Ren, Y.S., Reddy, S., Huang, J. & Liao, W.S.-L. (1997) Repression of serum amyloid A-1 (SAA1) promoter by transcription factor AP-2. FASEB J. 11, A2011.
158. 158. Ray, A. & Ray, B.K. (1994) Serum amyloid A gene expression under acute-phase conditions involves participation of inducible C/EBP-β and C/EBP-γ and their activation by phosphorylation. Mol. Cell Biol. 14, 4324-4332.
159. 159. Ray, A. & Ray, B.K. (1997) Serum amyloid A gene expression level in liver in response to different inflammatory agents is dependent upon the nature of activated transcription factors. DNA Cell Biol. 16, 1-7.
160. 160. Ray, B.K. & Ray, A. (1997) Induction of serum amyloid A (SAA) gene by SAA-activating sequence-binding factor (SAF) in monocyte/macrophage cells. Evidence for a functional synergy between SAF and Sp1. J. Biol. Chem. 272, 28948-28953.
161. 161. Ray, A., Hannink, M. & Ray, B.K. (1995) Concerted participation of NF-kappa B and C/EBP heteromer in lipopolysaccharide induction of serum amyloid A gene expression in liver. J. Biol. Chem. 270, 7365-7374.
162. 162. Ray, A. & Ray, B.K. (1998) Isolation and functional characterization of cDNA of serum amyloid A-activating factor that binds to the serum amyloid A promoter. Mol. Cell Biol. 18, 7327-7335.
163. 163. Ray, A., Schatten, H. & Ray, B.K. (1999) Activation of SP1 and its functional co-operation with serum amyloid A-activating sequence binding factor in synoviocyte cells trigger synergistic action of interleukin-1 and interleukin-6 in serum amyloid gene expression. J. Biol. Chem. 274, 4300-4308.
164. 164. Ray, B.K., Chatterjee, S. & Ray, A. (1999) Mechanism of minimally modified LDL-mediated induction of serum amyloid A gene in monocyte/macrophage cells. DNA Cell Biol. 18, 65-73.
165. 165. Ghosh, S., May, M.J. & Kopp, E.B. (1998) NF-κB and Rel proteins: evoludonarily conserved mediators of immune responses. Annu. Rev. Immunol. 16, 225-260.
166. 166. Poli, V. (1998) The role of C/EBP isoforms in the control of inflammatory and native immunity functions. J. Biol. Chem. 273, 29279-29282.
167. 167. LeClair, K.P., Blanar, M.A. & Sharp, P.A. (1992) The p50 subunit of NF-κB associates with the NF-IL6 transcription factor. Proc. Natl Acad. Sci. USA 89, 8145-8149.
168. 168. Matsusaka, T., Fujikawa, K., Nishio, Y., Mukaida, N., Matsushima, K., Kishimoto, T. & Akira, S. (1993) Transcription factors NF-IL6 and NF-κB synergistically activate transcription of the inflammatory cytokines, interleukin 6 and interleukin 8. Proc. Natl Acad. Sci. USA 90, 10193-10197.
169. 169. Liou, H.-C. & Baltimore, D. (1993) Regulation of the NF-κB/rel transcription factor and IκB inhibitor system. Curr. Opin. Cell Biol. 5, 477-487.
170. 170. Brasier, A.R., Ron, D., Tate, J.E. & Habener, J.F. (1990) A family of constitutive C/EBP-like DNA binding proteins attenuate the IL-1α induced, NF-κB mediated trans-activation of the angiotensinogen gene acute-phase response element. EMBO J. 9, 3933-3944.
171. 171. Hahn, S. (1992) The Yin and the Yang of mammalian transcription. Curr. Opin. Biol. 2, 152-154.
172. 172. Ray, B.K. & Ray, A. (1993) Functional NF-κB element in rabbit serum amyloid A gene and its role in acute phase induction. Biochem. Biophys. Res. Commun. 193, 1159-1167.
173. 173. Alam. T., An, M.R. & Papaconstantinou, J. (1992) Differential expression of three C/EBP isoforms in multiple tissues during the acute phase response. J. Biol. Chem. 267, 5021-5024.
174. 174. Burgess-Beusse, B.L. & Darlington, G.J. (1998) C/EBPα is critical for the neonatal acute-phase response to inflammation. Mol. Cell Biol. 18, 7269-7277.
175. 175. Ron, D. & Habener, J.F. (1992) CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription. Genes Dev. 6, 439-453.
176. 176. Sukenik, S., Henkin, J., Zimlichman, S., Skibin, A., Neuman, L., Pras, M, Horowitz, J. & Shainkin-Kestenbaum, R. (1988) Serum and synovial fluid levels of serum amyloid A protein and C-reactive protein in inflammatory and noninflammatory arthritis. J. Rheumatol. 15, 942-945.
177. 177. Kumon, Y., Loose, L.D., Birbara, C.A. & Sipe, J.D. (1997) Rheumatoid arthritis exhibits reduced acute phase serum amyloid A protein in synovial fluid relative to serum. A comparison with C-reactive protein. J. Rheumatol. 24, 14-19.
178. 178. Migita, K., Kawabe, Y., Tominaga, M., Origuchi, T., Aoyagi, T. & Eguchi, K. (1998) Serum amyloid A protein induces production of matrix metalloproteinases by human synovial fibroblasts. Lab. Invest. 78, 535-539.
179. 179. Strissel, K.J., Girard, M.T., West-Mays, J.A., Rinehart, W.B., Cook, J.R., Brinckerhoff, C.E. & Fini, M.E. (1997) Role of serum amyloid A as an intermediate in the IL-1 and PMA-stimulated signalling pathways regulating expression of rabbit fibroblast collagenase. Exp. Cell Res. 237, 275-287.
180. 180. Barnes, P.J. & Adcock, I. (1993) Anti-inflammatory actions of steroids: molecular mechanisms. Trends Pharmacol. Sci. 14, 436-441.
181. 181. Merkulova, T.I., Merkulov, V.M. & Mitina, R.L. (1997) Glucocorticoid regulation mechanisms and glucocorticoid-controlled gene regulatory regions: description in the TRDD database. Mol. Biol. 31, 605-615.
182. 182. Pratt, W.B. & Toft, D.O. (1997) Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 18, 306-360.
183. 183. Beato, M. (1989) Gene regulation by steroid hormones. Cell 56, 335-344.
184. 184. Ray, A., Zhang, D.H., Siegel, M.D. & Ray, P. (1995) Regulation of interleukin-6 gene expression by steroids. Ann. N.Y. Acad. Sci. 762, 79-87.
185. 185. Schule, R., Muller, M., Kaltschmidt, C. & Renkawitz, R. (1988) Many transcription factors interact synergistically with steroid receptors. Science 242, 1418-1420.
186. 186. Brattsand, R. & Linden, M. (1996) Cytokine modulation by glucocorticoids: mechanisms and actions in cellular studies. Aliment. Pharmacol. Ther. 10, 81-90.
187. 187. Koj, A. (1998) Termination of acute-phase response: role of some cytokines and anti-inflammatory drugs. Gen. Pharmacol. 31, 9-18.
188. 188. Koj, A. (1996) Initiation of acute phase response and synthesis of cytokines. Biochim. Biophys. Acta 1317, 84-94.
189. 189. Jonat, C., Rahmsdorf, H.J., Park, K.K., Cato, A.C., Gebel, S., Ponta, H. & Herrlich, P. (1990) Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell 62, 1189-1204.
190. 190. Lucibello, F.C., Slater, E.P., Jooss, K.U., Beato, M. & Muller, R. (1990) Mutual transrepression of Fos and the glucocorticoid receptor: involvement of a functional domain in Fos which is absent in FosB. EMBO J. 9, 2827-2834.
191. 191. Schule, R., Rangarajan, P., Kliewer, S., Ransone, L.J., Bolado, J., Yang, N., Verma, I.M. & Evans, R.M. (1990) Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor. Cell 62, 1217-1226.
192. 192. Yang-Yen, H.F., Chambard, J.C., Sun, Y.L., Smeal, T., Schmidt, T.J., Drouin, J. & Karin, M. (1990) Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 62, 1205-1215.
193. 193. Scheinman, R.I., Gualberto, A., Jewell, C.M., Cidlowski, J.A. & Baldwin, A.S. Jr (1995) Characterization of mechanisms involved in transrepression of NF-κB by activated glucocorticoid receptor. Mol. Cell Biol. 15, 943-953.
194. 194. Scheinman, R.I., Cogswell, P.C., Lofquist, A.K. & Baldwin, A.S. Jr (1995) Role of transcriptional activation of IκBα in mediation of immunosupression by glucocorticoids. Science 270, 283-286.
195. 195. Auphan, N., DiDonato, J.A., Rosette, C., Helmberg, A. & Karin, M. (1995) Immunosuppression by glucocorticoids: Inhibition of NF-κB activity through induction of IκB synthesis. Science 270, 286-290.
196. 196. Kerppola, T.K., Luk, D. & Curran, T. (1993) Fos is a preferential target of glucocorticoid receptor inhibition of AP-1 activity in vitro. Mol. Cell Biol. 13, 3782-3791.
197. 197. Knudsen, P.J., Dinarello, C.A. & Strom, T.B. (1987) Glucocorticoids inhibit transcriptional and post-transcriptional expression of interleukin 1 in U937 cells. J. Immunol. 139, 4129-4134.
198. 198. Ishida, T., Matsuura, K., Setoguchi, M., Higuchi, Y. & Yamamoto, S. (1994) Enhancement of murine serum amyloid A3 mRNA expression by glucocorticoids and its regulation by cytokines. J. Leukoc. Biol. 56, 797-806.
199. 199. Ito, A., Takii, T., Matsumura, T. & Onozaki, K. (1999) Augmentation of type I IL-1 receptor expression and IL-1 signaling by IL-6 and glucocorticoid in murine hepatocytes. J. Immunol. 162, 4260-4265.
200. 200. Jantzen, H.M., Strahle, U., Gloss, B., Stewart, F., Schmid, W., Boshart, M., Miksicek, R. & Schutz, G. (1987) Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene. Cell 49, 29-38.
201. 201. Grange, T., Roux, J., Rigaud, G. & Pictet, R. (1989) Two remote glucocorticoid responsive units interact cooperatively to promote glucocorticoid induction of rat tyrosine aminotransferase gene expression. Nucleic Acids Res. 17, 8695-8709.
202. 202. Reinhoff, H.Y.J. & Groudine, M. (1988) Regulation of amyloid A gene expression in cultured cells. Mol. Cell. Biol. 8, 3710-3716.
203. 203. Bernstein, P. & Ross, J. (1989) Poly (A), poly (A) binding protein and the regulation of mRNA stability. Trends Biochem. Sci. 14, 373-377.
204. 204. Jackson, R.J. & Standart, N. (1990) Do the poly (A) tail and 3′ untranslated region control mRNA translation? Cell 62, 15-24.
205. 205. Sachs, A.B. (1993) Messenger RNA degradation in eukaryotes. Cell 74, 413-421.
206. 206. Sachs, A. & Wahle, E. (1993) Poly (A) tail metabolism and function in eucaryotes. J. Biol. Chem. 268, 22955-22958.
207. 207. Zahedi, K. & Whitehead, A.S. (1989) Acute phase induction of mouse serum amyloid P component (SAP): correlation with other parameters of inflammation. J. Immunol. 143, 2880-2886.
208. 208. Brissette, L., Young, I., Narindrasorask, S., Kisilevsky, R. & Deeley, R. (1989) Differential induction of the serum amyloid A gene family in response to an inflammatory agent and the amyloid-enhancing factor. J. Biol. Chem. 264, 19327-19332.
209. 209. Lozanski, G., Jiang, S.L., Samols, D. & Kushner, I. (1996) C-reactive protein and serum amyloid A mRNA stability following induction by cytokines. Cytokine 8, 534-540.
210. 210. Couttet, P., Fromont-Racine, M., Steel, D., Pictet, R. & Grange, T. (1997) Messenger RNA deadenylation precedes decapping in mammalian cells. Proc. Natl Acad. Sci. USA 94, 5628-5633.
211. 211. Dowton, S.B., Peters, C.N. & Jestus, J.J. (1991) Regulation of serum amyloid A gene expression in Syrian hamsters by cytokines. Inflammation 15, 391-397.
212. 212. Badolato, R., Wang, J.M., Murphy, W.J., Lloyd, A.R., Michiel, D.F., Bausserman, L.L., Kelvin, D.J. & Oppenheim, J.J. (1994) Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J. Exp. Med. 180, 203-209.
213. 213. Xu, L., Badolato, R., Murphy, W.J., Longo, D.L., Anver, M., Hale, S., Oppenheim, J.J. & Wang, J.M. (1995) A novel biologic function of serum amyloid A. Induction of T lymphocyte migration and adhesion. J. Immunol. 155, 1184-1190.
214. 214. Preciado-Patt, L., Hershkoviz, R., Fridkin, M. & Lider, O. (1996) Serum amyloid A hinds specific extracellular matrix glycoproteins and induces the adhesion of resting CD4+ T cells. J. Immunol. 156, 1189-1195.
215. 215. Patel, H., Fellowes, R., Coade, S. & Woo, P. (1998) Human serum amyloid A has cytokine-like properties. Scand. J. Immunol. 48, 410-418.
216. 216. Olsson, N., Siegbahn, A. & Nilsson, G. (1999) Serum amyloid a induces chemotaxis of human mast cells by activating a pertussis toxin-sensitive signal transduction pathway. Biochem. Biophys. Res. Commun. 254, 143-146.
217. 217. Preciado-Patt, L., Cahalon, L., Hershkovitz, R., Lider, O., Pras, M. & Fridkin, M. (1998) Serum amyloid A complexed with extracellular matrix induces the secretion of tumor necrosis factor-α by human T-lymphocytes. Lett. Peptide Sci. 5, 349-355.
218. 3) to rabbit fibroblasts. Amyloid: Int. J. Exp. Clin. Invest. 2, 83-91.
219. 219. Murphy, P.M. (1994) The molecular biology of leukocyte chemo-attractant receptors. Annu. Rev. Immunol. 12, 593-633.
220. 220. Badolato, R., Johnston, J.A., Wang, J.M., McVicar, D., Xu, L.L., Oppenheim, J.J. & Kelvin, D.J. (1995) Serum amyloid A induces calcium mobilization and chemotaxis of human monocytes by activating a pertussis toxin-sensitive signaling pathway. J. Immunol. 155, 4004-4010.
221. 221. Su, S.B., Gong, W.H., Gao, J.L., Shen, W., Murphy, P.M., Oppenheim, J.J. & Wang, J.M. (1999) A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells. J. Exp. Med. 189, 395-402.
222. 222. Fiore, S., Maddox, J.F., Perez, H.D. & Serhan, C.N. (1994) Identification of a human cDNA encoding a functional high affinity lipoxin A4 receptor. J. Exp. Med. 180, 253-260.
223. 223. Hoffman, J.S. & Benditt, E.P. (1982) Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture. J. Biol. Chem. 257, 10518-10522.
224. 224. Cabana, V.G., Siegel, J.N. & Sabesin, S.M. (1989) Effects of the acute phase response on the concentration and density distribution of plasma lipids and apolipoproteins. J. Lipid Res. 30, 39-49.
225. 225. Berliner, J.A., Navab, M., Fogelman, A.M., Frank, J.S., Demer, L.L., Edwards, P.A., Watson, A.D. & Lusis, A.J. (1995) Atherosclerosis: basic mechanisms - oxidation, inflammation and genetics. Circulation 91, 2488-2496.
226. 226. Van Lenten, B.J., Hama, S.Y., de Beer, F.C., Stafforini, D.M., McIntyre, T.M., Prescott, S.M., La Du, B.N., Fogelman, A.M. & Navab, M. (1995) Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response. Loss of protective effect of HDL against LDL oxidation in aortic wall cell cocultures. J. Clin. Invest. 96, 2758-2767.
227. 227. Kisilevsky, R. & Subrahmanyan, L. (1992) Serum amyloid A changes high density lipoprotein's cellular affinity: a clue to serum amyloid A's principal function. Lab. Invest. 66, 778-785.
228. 228. Steinmetz, A., Hocke, G., Saile, R., Puchois, P. & Fruchart, J.-C. (1989) Influence of Serum Amyloid A on cholesterol esterification in human plasma. Biochim. Biophys. Acta 1006, 173-178.
229. 229. Rosenson, R.S. (1993) Myocardial injury: the acute phase response and lipoprotein metabolism. J. Am. Coll. Cardiol. 22, 933-940.
230. 230. Fyfe, A.L., Rothenberg, L.S., deBeer, F.C., Cantor, R.M., Rotter, J.I. & Lusis, A.J. (1997) Association between serum amyloid A proteins and coronary artery disease: evidence from two distinct arteriosclerotic processes. Circulation 96, 2914-2919.
231. 231. Shainkin-Kestenbaum, R., Zimlichman, S., Lis, M., Lidor, C., Pomerantz, M., Knyszynski, A., Preciado-Patt, L. & Fridkin, M. (1997b) Effect of serum amyloid A, HDL-apolipoprotein, on endothelial cell proliferation. Implication of an enigmatic protein to atherosclerosis. Biomed. Peptide Protein Nucleic Acids 2, 79-84.
232. 232. Kumon, Y., Nakauchi, Y., Kidawara, K., Fukushima, M., Kobayashi, S., Ikeda, Y., Suehiro, T., Hashimoto, K. & Sipe, J.D. (1988) A longitudinal analysis of alteration in lecithin-cholesterol acyltransferase and paraoxonase activities following laparoscopic cholecystectomy relative to other parameters of HDL function and the acute phase response. Scand. J. Immunol. 48, 419-424.
233. 233. Oram, J.F. (1996) Does serum amyloid A mobilize cholesterol from macrophages during inflammation? Amyloid: Int. J. Exp. Clin. Invest. 3, 290-293.
234. 234. de Beer, F.C., de Beer, M.C., van der Westhuyzen, D.R., Castellani, L.W., Lusis, A.J., Swanson, M.E. & Grass, D.S. (1997) Secretory non-pancreatic phospholipase A2: influence on lipoprotein metabolism. J. Lipid Res. 38, 2232-2239.
235. 235. Gonnerman, W.A., Lim, M., Sipe, J.D., Hayes, K.C. & Cathcart, E.S. (1996) The acute phase response in Syrian hamsters elevates apolipoprotein serum amyloid A (apoSAA) and disrupts lipoprotein metabolism. Amyloid: Int. J. Exp. Clin. Invest. 3, 261-269.
236. 236. Kisilevsky, R., Lindhorst, E., Ancsin, J.B., Young, D. & Bagshaw, W. (1996) Acute phase serum amyloid A (SAA) and cholesterol transport during acute inflammation: a hypothesis. Amyloid: Int. J. Exp. Clin. Invest. 3, 252-260.
237. 237. Lindhorst, E., Young, D., Bagshaw, W., Hyland, M. & Kisilevsky, R. (1997) Acute inflammation, acute phase serum amyloid A and cholesterol metabolism in the mouse. Biochim. Biophys. Acta 1339, 143-154.
238. 238. Liang, J.-S. & Sipe, J.D. (1995) Recombinant human serum amyloid A (apoSAAp) binds cholesterol and modulates cholesterol flux. J. Lipid Res. 36, 37-46.
239. 239. Liang, J.-S., Schreiber, B.M., Salmona, M., Phillip, G., Gonnerman, W.A., deBeer, F.C. & Sipe, J.D. (1996) Amino terminal region of acute phase, but not constitutive, serum amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells. J. Lipid Res. 37, 2109-2116.
240. 240. Banka, C.L., Yuan, T., de Beer, M.C., Kindy, M., Curtiss, L.K. & de Beer, F.C. (1995) Serum amyloid A (SAA): influence on HDL-mediated cellular cholesterol efflux. J. Lipid Res. 36, 1058-1065.
241. 241. Andersson, L.-O. (1997) Pharmacology of apolipoprotein A-I. Curr. Opin. Lipidol. 8, 225-228.
242. 242. Fielding, C.J., Shore, V.G. & Fielding, P.E. (1972) A protein cofactor of lecithin cholesterol acyltransferase. Biochem. Biophys. Res. Commun. 46, 1493-1498.
243. 243. Vadas, P., Browning, J., Edelson, J. & Pruzanski, W. (1993) Extracellular phospholipase A2 expression and inflammation: the relationship with associated disease states. J. Lipid Med. 8, 1-30.
244. 244. Menschikowski, M., Kasper, M., Lattke, P., Schiering, A., Schiefer, S., Stockinger, H. & Jaross. W. (1995) Secretory group II phospholipase A2 in human atherosclerotic plaques. Atherosclerosis 118, 173-181.
245. 245. Pruzanski, W., Keystone, E.C., Sternby, B., Bombardier, C., Snow, K.M. & Vadas, P. (1988) Serum phospholipase A2 correlates with disease activity in rheumatoid arthritis. J. Rheumatol. 15, 1351-1355.
246. 246. Pruzanski, W., de Beer, F.C., de Beer, M.C., Stefanski, E. & Vadas, P. (1995) Serum amyloid A protein enhances the activity of secretory non-pancreatic phospholipase A2. Biochem. J. 309, 461-464.
247. 247. Pruzanski, W., Stefanski, E., de Beer, F.C., de Beer, M.C., Vadas, P., Ravandi, A. & Kuksis, A. (1998) Lipoproteins are substrates for human secretory group IIA phospholipase A2: preferential hydrolysis of acute phase HDL. J. Lipid Res. 39, 2150-2160.
248. 248. Aldo-Benson, M.A. & Benson, M.D. (1982) SAA suppression of immune response in vitro: evidence for an effect on T cell-macrophage interaction. J. Immunol. 128, 2390-2392.
249. 249. Benson, M.D. & Aldo-Benson, M. (1979) Effect of purified protein SAA on immune response in vitro: mechanisms of suppression. J. Immunol. 122, 2077-2082.
250. 250. Benson, M.D. & Aldo-Benson, M.A. (1982) SAA suppression of in vitro antibody response. Ann. N.Y. Acad. Sci. 389, 121-125.
251. 251. Peristeris, P., Gaspar, A., Gros, P., Laurent, P., Bernon, H. & Bienvenu, J. (1989) Effects of serum amyloid A protein on lymphocytes, HeLa, and MRC5 cells in culture. Biochem. Cell Biol. 67, 365-370.
252. 252. Shainkin-Kestenbaum, R., Berlyne, G., Zimlichman, S., Sorin, H.R., Nyska, M. & Danon, A. (1991) Acute phase protein, serum amyloid A, inhibits IL-1-and TNF-induced fever and hypothalamic PGE2 in mice. Scand. J. Immunol. 34, 179-183.
253. 253. Dinarello, C.A., Cannon, J.G. & Wolff, S.M. (1988) New concepts on the pathogenesis of fever. Rev. Infect. Dis. 10, 168-189.
254. 254. Blackburn, W.D. Jr, Dohlman, J.G., Venkatachalapathi, Y.V., Pillion, D.J., Koopman, W.J., Segrest, J.P. & Anantharamaiah, G.M. (1991) Apolipoprotein A-I decreases neutrophil degranulation and superoxide production. J. Lipid Res. 32, 1911-1918.
255. 255. Linke, R.P., Bock, V., Valet, G. & Rothe, G. (1991) Inhibition of the oxidative burst response of N-formyl peptide-stimulated neutrophils by serum amyloid-A protein. Biochem. Biophys. Res. Commun. 176, 1100-1105.
256. 256. Gatt, M.E., Urieli-Shoval, S., Preciado-Patt, L., Fridkin, M., Calco, S., Azar, Y. & Matzner, Y. (1998) Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils. J. Lab. Clin. Med. 132, 414-420.
257. 257. Husby, G. (1994) Classification of amyloidosis. Ballières Clin. Rheumatol. 8, 503-511.
258. 258. Parmelee, D.C., Titani, K., Ericsson, L.H., Eriksen, N., Benditt, E.P. & Walsh, K.A. (1982) Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein. Biochemistry 21, 3298-3303.
259. 259. Shiroo, M., Kawahara, E., Nakanishi, I. & Migita, S. (1987) Specific deposition of serum amyloid A protein 2 in the mouse. Scand. J. Immunol. 26, 709-716.
260. 260. Westermark, P. & Sletten, K. (1982) A serum AA-like protein as a common constituent of secondary amyloid fibrils. Clin. Exp. Immunol. 49, 725-731.
261. 261. Ericsson, L.H., Eriksen, N., Walsh, K.A. & Benditt, E.P. (1987) Primary structure of duck amyloid protein A. The form deposited in tissues may be identical to its serum precursor. FEBS Lett. 218, 11-16.
262. 262. Arai, K., Miura, K., Baba, S. & Shirasawa, H. (1994) Transformation from SAA2-fibrils to AA-fibrils in amyloid fibrillogenesis; in vivo observations in murine spleen using anti-SAA and anti-AA antibodies. J. Pathol. 173, 127-134.
263. 263. Kisilevsky, R., Narindrasorasak, S., Tape, C., Tan, R. & Boudreau, L. (1994) During AA amyloidogenesis is proteolytic attack on serum amyloid A a pre-or post-fibrillogenic event? Amyloid: Int. J. Exp. Clin. Invest. 1, 174-183.
264. 264. Elliott-Bryant, R., Liang, J.S., Sipe, J.D. & Cathcart, E.S. (1998) Catabolism of lipid-free recombinant apolipoprotein serum amyloid A by mouse macrophages in vitro results in removal of the amyloid fibril-forming amino terminus. Scand. J. Immunol. 48, 241-247.
265. 265. Yamada, T., Kluve Beckerman, B., Liepnieks, J.J. & Benson, M.D. (1994) Fibril formation from recombinant human serum amyloid A. Biochim. Biophys. Acta 1226, 323-329.
266. 266. Bausserman, L.L. & Herbert, P.N. (1984) Degradation of serum amyloid A and apolipoproteins by serum proteases. Biochemistry 23, 2241-2245.
267. 267. Ancsin, J.B. & Kisilevsky, R. (1997) Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A. J. Biol. Chem. 272, 406-413.
268. 268. Takahashi, M., Yokota, T., Kawano, H., Gondo, T., Ishihara, T. & Uchino, F. (1989) Ultrastructural evidence for intracellular formation of amyloid fibrils in macrophages. Virchows Arch. A 415, 411-419.
269. 269. Miura, K., Ju, S.-T., Cohen, A.S. & Shirahama, T. (1990) Generation and use of site-specific antibodies to serum amyloid A for probing amyloid A development. J. Immunol. 144, 610-613.
270. 270. Shirahama, T., Miura, K., Ju, S.-T., Kisilevsky, R., Gruys, E. & Cohen, A.S. (1990) Amyloid enhancing factor-loaded macrophages in amyloid fibril formation. Lab. Invest. 62, 61-68.
271. 271. Chronopoulos, S., Chan, S.L., Ratcliffe, M.J.H. & Ali-Khan, Z. (1995) Colocalization of ubiquitin and seram amyloid A and ubiquitin-bound AA in the endosomes-lysomes: a double immunogold electron microscopic study. Amyloid: Int. J. Exp. Clin. Invest. 2, 191-194.
272. SAA) by murine macrophages in vitro. A light and electron microscopic investigation. Amyloid: Int. J. Exp. Clin. Invest. 4, 259-273.
273. 273. Rocken, C. & Kisilevsky, R. (1998) Comparison of the binding and endocytosis of high-density lipoprotein from healthy (HDL) and inflamed (HDLSAA) donors by murine macrophages of four different mouse strains. Virchows Arch. 432, 547-555.
274. 2 in endosomes-lysosomes in activated macrophages and their degradation products. Amyloid: Int. J. Exp. Clin. Invest. 4, 40-48.
275. 275. Levin, M., Franklin, E.C., Frangione, B. & Pras, M. (1972) The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J. Clin. Invest. 51, 2773-2776.
276. 276. Baba, S., Takahashi, T., Kasama, T. & Shirasawa, H. (1992) Identification of two novel amyloid A protein subsets coexisting in an individual patient of AA-amyloidosis. Biochim. Biophys. Acta 1180, 195-200.
277. 277. Bell, A.W., Chan, S.L., Marcantonio, D. & Ali-Kahn, Z. (1996) Both murine SAA1 and SAA2 yield AA amyloid in alveolar hydatid cystinfected mice. Scand. J. Immunol. 43, 173-180.
278. 278. Meek, R.L., Hoffman, J.S. & Benditt, E.P. (1986) Amyloidogenesis. One serum amyloid A isotype is selectively removed from the circulation. J. Exp. Med. 163, 499-510.
279. 279. Hoffman, J.S., Ericsson, L.H., Eriksen, N., Walsh, K.A. & Benditt, E.P. (1984) Murine tissue amyloid protein AA. NH2-terminal sequence identity with only one of two serum amyloid protein (Apo SAA) gene products. J. Exp. Med. 159, 641-646.
280. 280. Sipe, J.D., Colten, H.R., Goldberger, G., Edge, M.D., Tack, B.F., Cohen, A.S. & Whitehead, A.S. (1985) Serum amyloid A (SAA): biosynthesis and post-synthetic processing of preSAA and structural variants defined by complementary DNA. Biochemistry 24, 2931-2936.
281. 281. Dwulet, F.E., Wallace, D.K. & Benson, M.D. (1988) Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual. Biochemistry 27, 1677-1682.
282. 282. Kluve-Beckerman, B., Dwulet, F.E. & Benson, M.D. (1988) Human serum amyloid A: three hepatic mRNAs and the corresponding proteins in one person. J. Clin. Invest. 82, 1670-1675.
283. 283. Steinkasserer, A., Weiss, E.H., Schwaeble, W. & Linke, R.P. (1990) Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis. Biochem. J. 268, 187-193.
284. 284. Beach, C.M., deBeer, M.C., Sipe, J.D., Loose, L.D. & deBeer, F.C. (1992) Human serum amyloid A protein: complete amino acid sequence of a new variant. Biochem. J. 282, 615-620.
285. 285. Baba, S., Masago, S.A., Takahashi, T., Kasama, T., Sugimura, H., Tsugane, S., Tsutsui, Y. & Shirasawa, H. (1995) A novel allelic variant of serum amyloid A, SAA1 gamma: genomic evidence, evolution, frequency, and implication as a risk factor for reactive systemic AA-amyloidosis. Hum. Mol. Genet. 4, 1083-1087.
286. 286. Westermark, P., Sletten, K., Westermark, G.T., Raynes, J. & McAdam, K.P. (1996) A protein AA-variant derived from a novel serum AA protein, SAA1-delta, in an individual from Papua New Guinea. Biochem. Biophys. Res. Commun. 223, 320-323.
287. 287. Betts, J.C., Edbrooke, M.R., Thakker, R.V. & Woo, P. (1991) The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells. Scand. J. Immunol. 34, 471-482.
288. 288. Steel, D.M., Sellar, G.C., Uhlar, C.M., Simon, S., DeBeer, F.C. & Whitehead, A.S. (1993) A constitutively expressed serum amyloid A protein gene (SAA4) is closely linked to, and shares structural similarities with, an acute phase serum amyloid A protein gene (SAA2). Genomics 16, 447-454.
289. 289. de Beer, M.C., de Beer, F.C., McCubbin, W.D., Kay, C.M. & Kindy, M.S. (1993) Structural prerequisites for serum amyloid A fibril formation. J. Biol. Chem. 268, 20606-20612.
290. 290. Lavie, G., Zucker-Franklin, D. & Franklin, E.C. (1980) Elastase-type proteases on the surface of human blood monocytes: possible role in amyloid formation. J. Immunol. 125, 175-180.
291. 291. Silverman, S.L., Cathcart, E.S., Skinner. M. & Cohen, A.S. (1982) The degradation of serum amyloid A protein by activated polymorphonuclear leucocytes: participation of granulocytic elastase. Immunology 46, 737-744.
292. 292. Shephard, E.G., de Beer, F.C., de Beer, M.C., Jeenah, M.S., Coetzee, G.A. & van der Westhuyzen, D.R. (1987) Neutrophil association and degradation of normal and acute-phase high-density lipoprotein 3. Biochem. J. 248, 919-926.
293. 293. Skogen, B. & Natvig, J. (1981) Degradation of amyloid proteins by different serum proteases. Scand. J. Immunol. 14, 389-396.
294. 294. Bausserman, L.L., Herbert, P.N., Rodger, R. & Nicolosi, R.J. (1984) Rapid clearance of serum amyloid A from high-density lipoproteins. Biochim. Biophys. Acta 792, 186-191.
295. 295. Mitchell, T.I., Jeffrey, J.J., Palmiter, R.D. & Brinckerhoff, C.E. (1993) The acute phase reactant serum amyloid A (SAA3) is a novel substrate for degradation by the metalloproteinases collagenase and stromelysin. Biochim. Biophys. Acta 1156, 245-254.
296. 296. Yamada, T., Liepnieks, J.J., Kluve-Beckerman, B. & Benson, M.D. (1995) Cathepsin B generates the most common form of amyloid A (76 residues) as a degradation product from serum amyloid A. Scand. J. Immunol. 41, 94-97.
297. 297. Yamada, T., Kluve-Beckerman, B., Liepnieks, J.J. & Benson, M.D. (1995) In vitro degradation of serum amyloid A by cathepsin D and other acid proteases: possible protection against amyloid fibril formation. Scand. J. Immunol. 41, 570-574.
298. 298. Yamada, T., Liepnieks, J., Benson, M.D. & Kluve-Beckerman, B. (1996) Accelerated amyloid deposition in mice treated with the aspartic protease inhibitor, pepstatin. J. Immunol. 157, 901-907.