Skip to main content
SpringerLink
Log in

Acute-Phase Response and Amyloid

  • Conference paper
Rheumatoid Arthritis

  • 183 Accesses

Abstract

The acute phase is described as a series of events that occur in response to infection or tissue injury. Inflammation, as expressed clinically by the classical tetrad of dolor, calor, rubor et tumor represents the local reaction to such insults to tissue integrity, whereas the acute-phase phenomena reflect the systemic response in this recpect [56]. The ultimate goal of the inflammatory and acute-phase responses is to restore and maintain homeostasis by destruction and elimination of causative agents, limination of the extent of injury, removal of damaged tissue constituents, and repair.

This work was supported by the Norwegian Council for Science and the Humanities, the Norwegian Women’s Public Health Association, and the Norsk Revmatikerforbund.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Anders RF, Nordstoga K, Natvig JB, Husby G (1976) Amyloid-related serum protein SAA in endotoxin-induced amyloidosis of the mink. J Exp Med 143:678–683

    CAS  PubMed  Google Scholar 

  2. Anders RF, Natvig JB, Sletten K, Husby G, Nordstoga K (1977) Amyloid-related serum protein SAA from three animal species: comparison with human SAA. J Immunol 118:229–234

    CAS  PubMed  Google Scholar 

  3. Andersson JK, Mole JE (1982) Large-scale isolation and partial primary structure of human plasma amyloid P-component. Ann NY Acad Sci 389:216–234

    Google Scholar 

  4. Axelrad MA, Kisilevsky R (1980) Biological characterization of amyloid-enhancing factor. In: Glenner GG, Costa PP, de Freitas AF (eds) Amyloid and amyloidosis. Exerpta Medica, Amsterdam pp 527–533

    Google Scholar 

  5. Baltz ML, Caspi D, Evans DJ, Rowe IF, Hind CRK, Pepys MB (1986) Circulating serum amyloid P component is the precursor of amyloid P component in tissue amyloid deposits. Clin Exp Immunol 66:691–700

    CAS  PubMed  Google Scholar 

  6. Baltz ML, Rowe IF, Capsi D, Turnell WG, Pepys MB (1987) Acute-phase high-density lipoprotein in the rat does not contain serum amyloid A protein. Biochem J 242:301–303

    CAS  PubMed  Google Scholar 

  7. Bausserman LL, Saritelli AL, van Zuiden P, Collaher CJ, Herbert PN (1987) Degradation of serum amyloid A by isolated perfused rat liver. J Biol Chem 262:1583–1589

    CAS  PubMed  Google Scholar 

  8. Benditt EP, Eriksen N (1971) Chemical classes of amyloid substance. Am J Pathol 65:231–252

    CAS  PubMed  Google Scholar 

  9. Benditt EP, Eriksen N (1977) Amyloid protein SAA is associated with high-density lipoprotein from human serum. Proc Natl Acad Sci USA 74:4025–4028

    CAS  PubMed  Google Scholar 

  10. Benditt EP, Eriksen M, Hermodsen MA, Ericsson LH (1971) The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences. FEBS Lett 19:169–173

    CAS  PubMed  Google Scholar 

  11. Benditt EP, Cohen AS, Costa PP, Franklin EC, Glenner GG, Husby G, Mandema E, Natvig JB, Ossermann EF, Sohar E, Wegelius O, WEstermark P (1980) Guidelines for Nomenclature. Pp XI–XII in GG Glenner, PP Costa and AF de Freitas (Eds) Amyloid and Amyloidosis. Excerpta Medica, Amsterdam, Oxford, Princeton

    Google Scholar 

  12. Burchett SK, Weaver WM, Westall JA, Larsen A, Kronheim S, Wilson CB (1988) Regulation of tumor necrosis factor/cachetin and IL-1 secretion in human mononuclear phagocytes. J Immunol 140:3473–3481

    CAS  PubMed  Google Scholar 

  13. Castel JV, Gómez-Lechón MJ, David M, Hirano T, Kishimoto T, Heinrich PC (1988) Recombinant human interleukin-6 (IL-6/BSF-2/HSF) regulates the synthesis of acute-phase proteins in human hepatocytes. FEBS Lett 232:347–350

    Google Scholar 

  14. Cerami A, Beutler B (1988) The role of cachectin/TNF in endotoxic shock and cachexia. Immunol Today 1:28–31

    Google Scholar 

  15. Clifton PM, Mackinnon AM, Barter PJ (1985) Effects of serum amyloid A protein (SAA) on composition, size, and density of high-density lipo-proteins in subjects with myocardial infarction. J Lipid Res 26:1389–1398

    CAS  PubMed  Google Scholar 

  16. Coetzee GA, Strachan AF, van der Westhuyzen DR, Hoppe HC, Jeenan MS, de Beer FC (1986) Serum amyloid A-containing human high-density lipoproteins. J Biol Chem 261:9644–9651

    CAS  PubMed  Google Scholar 

  17. Cohen AS (1967) Amyloidosis. N Engl J Med 277:522–530

    CAS  PubMed  Google Scholar 

  18. Cohen AS (1967) Amyloidosis. N Engl J Med 277:574–583

    CAS  PubMed  Google Scholar 

  19. Cohen AS (1967) Amyloidosis. N Engl J Med 277:628–638

    CAS  PubMed  Google Scholar 

  20. Deal CL, Sipe JD, Tatsuta E, Skinner M, Cohen AS (1982) The effect of amyloid enhancing factor (AEF) on the acute — phase serum amyloid A (SAA) and serum amyloid P (SAP) response to silver nitrate. Ann NY Acad Sci 389:439–441

    CAS  Google Scholar 

  21. Dillon V, Woo P, Isenberg D (1989) Amyloidosis in the rheumatic diseases. Ann Rheum Dis 47:696–701

    Google Scholar 

  22. Dinarello CA (1984) Interleukin-1. Rev Infect Dis 6:51–95

    CAS  PubMed  Google Scholar 

  23. Dinarello CA, Mier JW (1987) Lymphokines. N Engl J Med 317:940–945

    CAS  PubMed  Google Scholar 

  24. Dowton SB, Colten HR (1988) Acute-phase reactants in inflammation and infection. Semin Hematol 25:84–90

    CAS  PubMed  Google Scholar 

  25. Edbrooke MR, Burt DW, Cheshire JK, Woo P (1989) Identification of cis-acting sequences responsible for phorbol ester induction of human serum amyloid A gene expression via a nuclear factor kappa B-like transcription factor. Mol Cell Biol 9:1908–1916

    CAS  PubMed  Google Scholar 

  26. Ericsson LH, Eriksen N, Walsh KA, Benditt EP (1987) Primary structure of duck amyloid protein A. FEBS Lett 218:11–16

    CAS  PubMed  Google Scholar 

  27. Fuks A, Zucker-Franklin D (1985) Impaired Kupffer cell function precedes the development of secondary amyloidosis. J Exp Med 161:1013–1028

    CAS  PubMed  Google Scholar 

  28. Ganapathi MK, Schultz D, Mackiewicz A, Samold D, Hu SI, Brabenec A, Macintyre S, Kushner I (1988) Heterogenous nature of the acute-phase response. Differential regulation of human serum amyloid A, C-reactive protein, and other acute-phase proteins by cytokines in Hep 3B cells. J Immunol 141:564–569

    CAS  PubMed  Google Scholar 

  29. Gauldie J, Richards C, Harnish D, Landsorp P, Baumann H (1987) Interferon β2/B-cell stimulatory factor type 2 shares identity with monocyte-derived hepatocyte-stimulating factor (HSF) and regulates the major acute-phase protein response in liver cells. Proc Natl Acad Sci USA 84:7251–7255

    CAS  PubMed  Google Scholar 

  30. Glenner GG (1980) Amyloid deposits and amyloidosis. N Engl J Med 302:1283–1292

    CAS  PubMed  Google Scholar 

  31. Goldberger G, Bing DH, Sipe JD, Rits M, Colton HR (1987) Transcriptional regulation of genes encoding the acute-phase proteins CRP, SAA and C3. J Immunol 138:3967–3971

    CAS  PubMed  Google Scholar 

  32. Hamazaki H (1987) CA2+-mediated association of human serum amyloid P component with heparan sulfate and dermatan sulfate. J Biol Chem 262:1456–1460

    CAS  PubMed  Google Scholar 

  33. Harats N, Kluve-Beckerman B, Skinner M, Paso M, Quinn L, Benson MD (1989) Lack of association of a restriction fragment length polymorphism for serum amyloid P gene with reactive amyloidosis. Arthritis Rheum 32:1325–1327

    CAS  PubMed  Google Scholar 

  34. Hawkins PN, Lavender JP, Myers MJ, Pepys MB (1988) Diagnostic radionuclide imaging of amyloid: biological targeting by circulating human serum amyloid P component. Lancet 1:1413–1418

    CAS  PubMed  Google Scholar 

  35. Hoffman JS, Ericsson LH, Eriksen N, Walsh KA, Benditt EP (1984) Murine tissue amyloid protein AA. NH2-terminal sequence identity with only one of two serum amyloid protein (ApoSAA) gene products. J Exp Med 159:641–646

    CAS  PubMed  Google Scholar 

  36. Hol PR, Snel FWJJ, Niewold TA, Gruys E (1986) Amyloid enhancing factor (AEF) in the pathogenesis of AA-amyloidosis in the hamster. Virchows Arch [B] 52:273–281

    CAS  Google Scholar 

  37. Hoick M, Husby G, Sletten K, Natvig JB (1979) The amyloid P component (protein AP): an integral part of the amyloid substance? Scand J Immunol 10:55–60

    Google Scholar 

  38. Husby G (1980) A chemical classification of amyloid correlation with different clinical types of amyloidosis. Scand J Rheumatol 9:60–64

    CAS  PubMed  Google Scholar 

  39. Husby G (1983) Immunoglobulin-related (AL) amyloidosis. Clin Exp Rheumatol 1:353–358

    CAS  PubMed  Google Scholar 

  40. Husby G (1985) Amyloidosis and rheumatoid arthritis. Clin Exp Rheumatol 3:173–180

    CAS  PubMed  Google Scholar 

  41. Husby G, Natvig JB (1974) A serum component related to non-immunoglobulin amyloid protein AS. A possible precursor of the fibrils. J Clin Invest 53:1054–1061

    CAS  PubMed  Google Scholar 

  42. Husby G, Sletten K (1986) Chemical and clinical classification of amyloidosis 1985. Scand J Immunol 23:253–265

    CAS  PubMed  Google Scholar 

  43. Husby G, Sletten K (1986) Amyloid proteins. In: Marrink J, van Rijswijk MH (eds) Amyloidosis. Nijhoff, Dordrecht, pp 23–24

    Google Scholar 

  44. Husby G, Sletten K, Michaelsen TE, Natvig JB (1972) An alternative nonimmunoglobulin origin of amyloid fibrils. Nature 238:187

    CAS  Google Scholar 

  45. Husby G, Natvig JB, Michaelsen TE, Sletten K, H0St H (1973) Unique amyloid protein subunit common to different types of amyloid fibril. Nature 244:362–364

    CAS  PubMed  Google Scholar 

  46. Husby G, Natvig JB, Sletten K, Nordstoga K, Anders RF (1975) An experimental model in mink for studying the relation between amyloid fibril protein AA and the related serum protein SAA. Scand J Immunol 4:811–816

    CAS  PubMed  Google Scholar 

  47. Husby G, Husebekk A, Marhaug G, Skogen B, Sletten K (1988) Serum amyloid A (SAA): the precursor for protein AA in secondary amyloidosis. Adv Exp Med Biol 243:148–192

    Google Scholar 

  48. 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

    CAS  PubMed  Google Scholar 

  49. Husebekk A, Husby G, Sletten K, Marhaug G (1986) Characterization of amyloid protein AA and its serum precursor SAA in the horse. Scand J Immunol 23:703–709

    CAS  PubMed  Google Scholar 

  50. Husebekk A, Permin H, Husby G (1986) Serum amyloid protein A (SAA) — an indicator of inflammation in AIDS and AIDS-related complex (ARC). Scand J Infect Dis 18:389–394

    CAS  PubMed  Google Scholar 

  51. Husebekk A, Skogen B, Husby G (1987) Characterization of amyloid proteins AA and SAA as apolipoproteins of HDL. Displacement of SAA from the HDL-SAA by apo AI and apo AII. Scand J Immunol 25:375–381

    CAS  PubMed  Google Scholar 

  52. Husebekk A, Skogen B, Husby G (1988) Replacement of SAA from the SAA-HDL complex by Apo AI and Apo AII. Relevance for amyloid formation? In: Jsobe S, Araki F, Uchino S, Kito and E Tsubura (eds) Amyloid and Amyloidosis. Plenum, New York and London, pp 223–228

    Google Scholar 

  53. Husebekk A, Husby G, Sletten K, Skogen B, Nordstoga K (1988) Characterization of bovine amyloid proteins SAA and AA. Scand J Immunol 27:739–743

    CAS  PubMed  Google Scholar 

  54. Isobe T, Husby G, Sletten K (1980) Characterization of an amyloid protein AA similar to SAA. In: Glenner GG, Costa PP, de Freitas AF (eds) Amyloid and amyloidosis. Exerpta Medica, Amsterdam pp 331–336

    Google Scholar 

  55. Kisilevsky R (1987) From arthritis to Alzheimer’s disease: current concepts on the pathogenesis of amyloidosis. Can J Physiol Pharmacol 65:1805–1815

    CAS  PubMed  Google Scholar 

  56. Kluve-Beckerman B, Long GL, Benson MD (1986) DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA). Biochem Genet 24:795–803

    CAS  PubMed  Google Scholar 

  57. Koj A (1974) Acute-phase reactants. In: Alison AC (ed) Structure and function of plasma proteins. Plenum, New York pp 73–132

    Google Scholar 

  58. Kushner I (1982) The phenomenon of the acute-phase response. Ann NY Acad Sci 389:39–48

    CAS  PubMed  Google Scholar 

  59. Kushner I, Mackiewicz A (1987) Acute-phase proteins as disease markers. Dis Markers 5:1–11

    CAS  PubMed  Google Scholar 

  60. Kushner I, Ganapathi MK, Macintyre SS (1989) Regulation of biosynthesis and secretion of human C-reactive protein and serum amyloid A. In: Pepys MB (ed) Acute-phase proteins in the acute-phase response. Springer, Berlin Heidelberg New York, pp 69–83

    Google Scholar 

  61. Lavie G, Zucker-Franklin D, Franklin EC (1978) Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes. J Exp Med 148:1020–1031

    CAS  PubMed  Google Scholar 

  62. Le J, Vilcek J (1987) Tumor necrosis factor and interleukin-1: cytokines with multiple overlapping biological activities. Lab Invest 56:234–248

    CAS  PubMed  Google Scholar 

  63. Levin M, Franklin EC, Frangione B, Pras M (1972) The amino acid sequence of a major non-immunoglobulin component of some amyloid fibrils. J Clin Invest 51:2773–2776

    CAS  PubMed  Google Scholar 

  64. Li JJ, McAdam PW (1984) Human amyloid P component: an elastase inhibitor. Scand J Immunol 20:219–226

    CAS  PubMed  Google Scholar 

  65. Liao WS, Stark GS (1986) Cloning of rat cDNAs for eight acute-phase reactants and kinetics of induction of mRBAs following acute inflammation. Adv Inflamm Res 10:220–222

    Google Scholar 

  66. Linke RP, Heilmann KL, Nathrath WBJ, Eulitz M (1983) Identification of amyloid A protein in a sporadic Muckle-Wells syndrome. N-terminal amino acid sequence after isolation from formalin-fixed tissue. Lab Invest 48:698–704

    CAS  PubMed  Google Scholar 

  67. Lowell A, Potter DA, Stearman RS, Morrow JF (1986) Structure of the murine serum amyloid A gene family. J Biol Chem 261:88442–8452

    Google Scholar 

  68. Lowell CA, Stearman RS, Morrow JF (1986) Transcriptional regulation of serum amyloid A gene expression. J Biol Chem 261:8453–8561

    CAS  PubMed  Google Scholar 

  69. Macintyre S, Samols D, Kushner I (1986) Regulation of C-creative protein secretion by cultured rabbit hepatocytes. Protides Biol Fluids 34:251–254

    CAS  Google Scholar 

  70. Magnus JH, Husby G, Kolset SO (1989) Glycosaminoglycans are present in purified AA-type amyloid fibrils associated with juvenile rheumatoid arthritis. Ann Rheum Dis 48:215–219

    CAS  PubMed  Google Scholar 

  71. Marhaug G (1983) Three assays for the characterization and quantitation of human serum amyloid A. Scand J Immunol 18:329–338

    CAS  PubMed  Google Scholar 

  72. Marhaug G, Sletten K, Husby G (1982) Characterization of amyloid-related serum protein SAA complexed with serum lipoproteins (apo SAA). Clin Exp Immunol 50:382–393

    CAS  PubMed  Google Scholar 

  73. Marhaug G, Permin H, Husby G (1983) Amyloid-related serum protein (SAA) as an indicator of lung infection in cystic fibrosis. Acta Paediatr Scand 72:861–866

    CAS  PubMed  Google Scholar 

  74. Marhaug G, Hårklau L, Olsen B, Husby G, Husebekk A, Wang H (1986) Serum amyloid A protein in acute myocardial infarction. Acta Med Scand 220:303–306

    CAS  PubMed  Google Scholar 

  75. Marhaug G, Østensen M, Husby G, Kolmannskog S, Flaegstad T, Stokland T, Husebekk A (1986) Clinical acute-phase pattern of serum amyloid A. Protides Biol Fluids 34:375–378

    Google Scholar 

  76. Maury CPJ, Teppo A-M, Ahonen J, v Willebrand E (1984) Measurement of serum amyloid A protein concentrations as a test of renal allograft rejection in patients with initially non-functioning grafts. Br Med J 288:340–341

    Google Scholar 

  77. McAdam KPWJ, Elin RJ, Sipe JD, Wolff SM (1978) Changes in human serum amyloid-A and C-reactive protein after etiocholanolene-induced inflammation. J Clin Invest 61:390–394

    CAS  PubMed  Google Scholar 

  78. McAdam KPWJ, Li J, Knowles J, Foss NT, Dinarello CA, Rosenwasser LJ, Selinger MJ, Kaplan MM, Goodman R (1982) The biology of SAA: identification of the inducer, in vitro synthesis, and heterogeneity demonstrated with monoclonal antibodies. Ann NY Acad Sci 389:126–136

    CAS  PubMed  Google Scholar 

  79. Meek RL, Benditt EP (1986) Amyloid A gene family expression in different mouse tissues. J Exp Med 164:2006–2017

    CAS  PubMed  Google Scholar 

  80. Meek RL, Benditt EP (1989) Rat tissues express serum amyloid A protein-related mRNAs. Proc Natl Acad Sci USA 86:1890–1894

    CAS  PubMed  Google Scholar 

  81. Meek RL, Hoffmann JS, Benditt EP (1986) Amyloidogenesis. One serum amyloid A isotype is selectively removed from the circulation. J Exp Med 163:499–510

    CAS  PubMed  Google Scholar 

  82. Moshage HJ, Roelofs HMJ, v Pelt JF, Hazenberg BPC, v Leeuwen MA, Limburg PC, Aarden LA, Yap SH (1988) The effect of interleukin-1, interleukin-6 and its interrelationship on the synthesis of serum amyloid A and C-reactive protein in primary cultures of adult human hepatocytes. Biochem Biophys Ress Commun 155:112–117

    CAS  Google Scholar 

  83. Møyner K, Sleten K, Husby G & Natvig JB (1980) An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenstrø’s macroglobulinaemia and amyloidosis. Scand J Immunol 11:549–554

    PubMed  Google Scholar 

  84. Muckle TJ (1979) The “Muckle-Wells” syndrome. Br J Dermatol 100:87–92

    CAS  PubMed  Google Scholar 

  85. Niewold TA, Hol PR, van Andel ACJ, Lutz ETG, Gruys E (1987) Enhancement of amyloid induction by amyloid fibril fragments in hamster. Lab Invest 56:554–549

    Google Scholar 

  86. Oppenheim JJ, Kovacs EJ, Matusushima K, Durum SK (19869 There is more than one interleukin-1. Immunol Today 7:45–56

    Google Scholar 

  87. Park JS, Rudel LL (1985) Alteration of high-density lipoprotein subfraction distribution with induction of serum amyloid A protein (SAA) in the non-human primate. J Lipid Res 26:82–91

    Google Scholar 

  88. Parmelee DC, Titani K, Ericsson LH, Eriksen N, Benditt EP, Walsh KA (1982) Amino acid sequence of amyloid-related apoprotein (apoSAA) from human high-density lipoprotein. Biochemistry 21:3298–3303

    CAS  PubMed  Google Scholar 

  89. Pepys M, Baltz ML (1983) Acute-phase proteins with special reference to C-reactive protein and related proteins (pentraxins) and serum amyloid A protein. Adv Immunol 34:141–212

    CAS  PubMed  Google Scholar 

  90. Prelli F, Pras M, Frangione B (1987) The degradation and deposition of amyloid AA fibril is tissue specific. Biochemistry 26:8251–8256

    CAS  PubMed  Google Scholar 

  91. Ramadori G, Van Damme J, Rieder H, Meyer zum Büschenfelde KH (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

    CAS  PubMed  Google Scholar 

  92. Rokita H, Shirahama T, Cohen AS, Meek RL, Benditt EP, Sipe J (1987) Differential expression of the amyloid SAA3 gene in liver and peritoneal macrophages of mice undergoing dissimilar inflammatory processes. J Immunol 139:3849–3853

    CAS  PubMed  Google Scholar 

  93. Rosenthal CJ, Sullivan LM (1979) Serum amyloid A to monitor cancer dissemination. Ann Intern med 91:383–390

    CAS  PubMed  Google Scholar 

  94. Sack GH Jr (1988) Serum amyloid (SAA) gene variations in familial Mediterranean fever. Mol Biol Med 5:61–67

    CAS  PubMed  Google Scholar 

  95. Seckinger P, Williamson K, Balavoine J-F, Bach B, Mazzei G, Shaw A, Dayer J-M (1987) A urine inhibitor of interleukin-1 activity affects both interleukin-1 α and -1 β but not tumor necrosis factor α1. J immunol 139:1541–1545

    CAS  PubMed  Google Scholar 

  96. Seckinger P, Isaaz S, Dayer J-M (1988) A human inhibitor of tumor necrosis factor α. J Exp Med 167:1511–1516

    CAS  PubMed  Google Scholar 

  97. Sipe JD, Colten HR, Goldberger G, Edge MD, Tack BF, Cohen AS, Whitehead AS (1985) Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of pre SAA and structural variants by complementary DNA. Biochemistry 24:2931–2935

    CAS  PubMed  Google Scholar 

  98. Skogen B, Natvig JB (1981) Degradation of amyloid proteins by different serine proteases. Scand J Immunol 14:389–396

    CAS  PubMed  Google Scholar 

  99. Skogen B, Børresen AL, Natvig JB, Berg K, Michaelsen TE (1979) High-density lipoproteins as carrier for amyloid-related protein sAA in rabbit serum. Scand J Immunol 10:39–45

    CAS  PubMed  Google Scholar 

  100. Sletten K, Husby G (1974) The complete amino acid sequence of non-immuno-globulin amyloid fibril protein AS in rheumatoid arhritis. Eur J Biochem 41:117–125

    CAS  PubMed  Google Scholar 

  101. Sletten K, Marhaug G, Husby G (1983) The covalent structure of amyloid-related serum protein SAA from two patients with inflammatory disease. Hoppe-Zeyler’s Physiol Chem 364:1039–1046

    CAS  Google Scholar 

  102. Sletten K, Husebekk A, Husby G (1989) The primary structure of equine serum amyloid A (SAA) protein. Scand J Immunol 30:117–122

    CAS  PubMed  Google Scholar 

  103. Snow AD, Willmer J, Kisilevsky R (19879 A close structural relationship between sulfated proteoglycans and AA amyloid fibrils. Lab Invest 57:687–698

    Google Scholar 

  104. Syversen V, Sletten K, Marhaug G, Husby G, Lium B (1987) The amino acid sequence of serum amyloid A (SAA) in mink. Scand J Immunol 26:763–767

    CAS  PubMed  Google Scholar 

  105. 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

    CAS  PubMed  Google Scholar 

  106. Trinchieri G, Perussia B (1985) Immune interferon: a pleiotropic lymphokine with multiple effects. Immunol Today 6:131–136

    CAS  Google Scholar 

  107. Turneil W, Sarra R, Glover ID, Baum JO, Caspi D, Baltz ML, Pepys MD (1986) Secondary structure prediction of human SAA1. Presumptive identification of calcium and lipid binding sites. Mol Biol Med 3:387–407

    Google Scholar 

  108. Turnell W, Sarra R, Baum JO, Caspi D, Baltz ML, Pepys MB (1986) X-ray scattering and diffraction by wet gels of AA amyloid fibrils. Mol Biol Med 3:409–424

    CAS  PubMed  Google Scholar 

  109. Waalen K, Sletten K, Husby G, Nordstoga K (1980) The primary structure of amyloid fibril protein AA in endotoxin-induced amyloidosis of the mink. Eur J Biochem 104:407–412

    CAS  PubMed  Google Scholar 

  110. Wohlgethan JR, Cathcart ES (1980) Amyloid resistance in A/J mice. Studies with a transfer model. Lab Invest 42:663–67

    CAS  PubMed  Google Scholar 

  111. Wong GG, Clark SC (1988) Multiple actions of interleukin-6 within a cytokine network. Immunol Today 9:137–139

    CAS  PubMed  Google Scholar 

  112. Woo P, Sipe J, Dinarello CA, Colten HR (1987) Structure of a human serum amyloid A gene and modulation of its expression in transfected L cells. J Biol Chem 262:15790–15795

    CAS  PubMed  Google Scholar 

  113. Woo P, O’Brien J, Robson M, Ansell BM (1987) A genetic marker for systemic amyloidosis in juvenile arthritis. Lancet 2:767–769

    CAS  PubMed  Google Scholar 

  114. Yamamoto KI, Shiroo M, Migita S (1986) Diverse gene expression for isotypes of murine serum amyloid A protein during acute-phase reaction. Science 232:227–229

    CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Rheumatology, The University Hospital of Tromsø, 9000, Tromsø, Norway

    G. Husby

Authors
  1. G. Husby
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. 2. Medizinische Abteilung Zentrum fü Diagnostik und Therapie rheumatischer Erkrankungen, Krankenhaus der Stadt Wien-Lainz und Ludwig Boltzmann Institut für Rheumatologie und Balneologie, Wolkersbergenstraße 1, A-1130, Wien, Austria

    Josef S. Smolen

  2. Medizinische Klinik III mit Poliklinik und Institut für Klinische Immunologie und Rheumatologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Krankenhausstraße 12, W-8520, Erlangen, Germany

    Joachim R. Kalden

  3. Mathilda and Terence Kennedy Institute of Rheumatology, 6 Bute Gardens, W6 7DW, Hammersmith, London, UK

    Ravinder N. Maini

Rights and permissions

Reprints and permissions

Copyright information

© 1992 Springer-Verlag Berlin Heidelberg

About this paper

Cite this paper

Husby, G. (1992). Acute-Phase Response and Amyloid. In: Smolen, J.S., Kalden, J.R., Maini, R.N. (eds) Rheumatoid Arthritis. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76189-8_22

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-76189-8_22

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-76191-1

  • Online ISBN: 978-3-642-76189-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation