Acute-Phase Proteins and Responses and Their Application in Clinical Chemistry

  • Waliza Ansar
  • Shyamasree Ghosh


The host innate responses to immunological stress initiate with a nonspecific response followed by specific responses. Host homeostasis is affected due to injury, infection, surgery, trauma, neoplastic growth, or immunological disorders and is combated by a prominent systemic reaction of the organism known as acute-phase response (APR). At the tissue injury sites and sites of invasion of microbes, a series of tissue responses are itself initiated. The activation of vascular system and inflammatory cells and release of pro-inflammatory cytokines are the key steps of these responses. These responses are then amplified by the overproduction of cytokines and different inflammatory mediators released in blood circulation. The acute-phase response is also characterized by hepatic secretion of some proteins termed as acute-phase proteins (APP). APR characterized by alteration in blood plasma composition is beneficial to the host in preventing microbial propagation and thus helps in restoring homeostasis. Multifunctional APPs can opsonize the invading microbes and activate the complement system and remove dead cells and free radicals. In this chapter, the changes induced by acute-phase response disruption of host body homeostasis are discussed. In addition, the diagnostic, prognostic, and therapeutic use of APPs in assessing health in animals as well as human patients is also described.


Acute phase protein Acute phase response Inflammation Inflammatory mediators Acute inflammation Chronic inflammation Disease biomarker Cytokine 


  1. Abbas A, Lichtman A, Pillai S (2012) Basic immunology functions and disorders of the immune system, 4th edn. Saunders/Elsevier, Philadelphia, p 40Google Scholar
  2. Abernethy TJ, Avery OT (1941) The occurrence during acute infections of a protein not normally present in the blood. 1. Distribution of the reactive protein in patient’s sera and the effect of calcium on the flocculation reaction with C polysaccharide of Pneumococcus. J Exp Med 73:173–182PubMedPubMedCentralCrossRefGoogle Scholar
  3. Alsemgeest SPM (1994) Blood concentrations of acute-phase proteins in cattle as markers for disease. PhD thesis, Utrecht University, Utrecht, The NetherlandsGoogle Scholar
  4. Alsemgeest SPM, Taverne MAM (1993) Peripartum acute-phase protein serum amyloid-A concentration in plasma of cows and fetuses. Am J Vet Res 54:164–167PubMedGoogle Scholar
  5. Alsemgeest SPM, Kalsbeek HC, Wensing T, Koeman JP, van Ederen AM, Gruys E (1994) Concentrations of serum amyloid-A (SAA) and haptoglobin (Hp) as parameters of inflammatory diseases in cattle. Vet Q 16:21–23PubMedCrossRefGoogle Scholar
  6. Ansar W, Ghosh S (2013) C-reactive protein and the biology of disease. Immunol Res 56(1):131–142. doi: 10.1007/s12026-013-8384-0 PubMedCrossRefGoogle Scholar
  7. Ansar W, Bandyopadhyay SM, Chowdhury S, Habib SH, Mandal C (2006) Role of C-reactive protein in complement mediated hemolysis in Malaria. Glycoconj J 23(3–4):233–240PubMedCrossRefGoogle Scholar
  8. Ansar W, Habib SK, Roy S, Mandal C, Mandal C (2009a) Unraveling the C-reactive protein complement-cascade in destruction of red blood cells: potential pathological implications in Plasmodium falciparum malaria. Cell Physiol Biochem 23(1–3):175–190. doi: 10.1159/000204106. Epub 2009 Feb 18PubMedCrossRefGoogle Scholar
  9. Ansar W, Mukhopadhyay S, Habib SK, Basu S, Saha B, Sen AK, Mandal CN, Mandal C (2009b) Disease-associated glycosylated molecular variants of human C-reactive protein activate complement-mediated hemolysis of erythrocytes in tuberculosis and Indian visceral leishmaniasis. Glycoconj J 26(9):1151–69. doi: 10.1007/s10719-009-9236-y PubMedCrossRefGoogle Scholar
  10. Arnett HA, Viney JL (2010) Gatekeepers of intestinal inflammation. Inflamm Res 59(1):1–14PubMedCrossRefGoogle Scholar
  11. Asai T, Mori M, Okada M, Uruno K, Yazawa S (1999) Elevated serum haptoglobin in pigs infected with porcine reproductive and respiratory syndrome virus. Vet Immunol Immunopathol 70:143–148PubMedCrossRefGoogle Scholar
  12. Badolato R, Johnston JA, Wang JM, McVicar D, Xu LL, Oppenheim JJ, Kelvin DJ (1995) Serum amyloid A induces calcium mobilisation and chemotaxis in human monocytes by activating a pertussis toxin sensitive signaling pathway. J Immunol 155:4004–4010PubMedGoogle Scholar
  13. Balci B, Tinaztepe K, Yilmaz E, Guçer S, Ozen S, Topaloğlu R et al (2002) MEFV gene mutations in familial Mediterranean fever phenotype II patients with renal amyloidosis in childhood: a retrospective clinicopathological and molecular study. Nephrol Dial Transplant 17:1921–1923PubMedCrossRefGoogle Scholar
  14. Ballou SP, Lozanski FB, Hodder S, Rzewnicki DL, Mion LC, Sipe JD, Ford AB, Kushner I (1996) Quantitative and qualitative alterations of acute-phase proteins in healthy elderly persons. Age Ageing 25(3):224–230PubMedCrossRefGoogle Scholar
  15. Bandyopadhyay S, Chatterjee M, Das T, Bandyopadhyay S, Sundar S, Mandal C (2004) Antibodies directed against O-acetylated sialoglycoconjugates accelerate complement activation in Leishmania donovani promastigotes. J Infect Dis 190(11):2010–2019. Epub 2004 Nov 3PubMedCrossRefGoogle Scholar
  16. Baumann H, Gauldie J (1994) The acute phase response. Immunol Today 15:74–80PubMedCrossRefGoogle Scholar
  17. Black S, Kushner I, Samols D (2004) C-reactive protein. J Biol Chem 279(47):48487–48490. Epub 2004 Aug 26PubMedCrossRefGoogle Scholar
  18. Blackburn WD (1994) Validity of acute phase proteins as markers of disease activity. J Rheumatol 21(Suppl 42):9–13Google Scholar
  19. Bode JG, Albrecht U, Häussinger D, Heinrich PC, Schaper F (2012) Hepatic acute phase proteins – regulation by IL-6- and IL-1-type cytokines involving STAT3 and its crosstalk with NF-κB-dependent signaling. Eur J Cell Biol 91(6–7):496–505PubMedCrossRefGoogle Scholar
  20. Boer JP, Creasey AA, Chang A, Abbink JJ et al (1993) Alpha-2-macroglobulin functions as an inhibitor of fibrinolytic, clotting, and neutrophilic proteinases in sepsis: studies using a baboon model. Infect Immun 61(12):5035–5043PubMedPubMedCentralGoogle Scholar
  21. Bonnefoy M, Ayzac L, Ingenbleek Y, Kostka T, Boisson RC, Bienvenu J (1998) Usefulness of the prognostic inflammatory and nutritional index (PINI) in hospitalized elderly patients. Int J Vitam Nutr Res 68:189–195PubMedGoogle Scholar
  22. Burger W, Ewald C, Fennert EM (1998) Increase in C-reactive protein in the serum of piglets (pCRP) following ACTH or corticosteroid administration. J Vet Med B 45:1–6CrossRefGoogle Scholar
  23. Cathcart ES, Shirahama T, Cohen AS (1967) Isolation and identification of a plasma component of amyloid. Biochim Biophys Acta 147:392–393CrossRefGoogle Scholar
  24. Cavaillon JM, Duff G (1999) Cytokines and the cellular mechanism of inflammation. The cytokine network and immune functions. Oxford University Press, New York, pp 251–261Google Scholar
  25. Chamanza R, Toussaint MJM, Hulskamp-Koch C, Fabri TH (2000) Serum amyloid A and transferrin in chicken. A preliminary investigation of using acute-phase variables to assess diseases in chickens. Vet Bull 70:284, abstr. 1601Google Scholar
  26. Cid MC, Grant DS, Hoffman GS, Auerbach R, Fauci AS, Kleinman HK (1993) Identification of haptoglobin as an angiogenic factor in sera from patients with systemic vasculitis. J Clin Invest 91:977–985PubMedPubMedCentralCrossRefGoogle Scholar
  27. Cote N, Trout DR, Hayes MA (1998) Interaction of transforming growth factor-beta-1 with alpha-2-macroglobulin from normal and inflamed equine joints. Can J Vet Res 62:279–286PubMedPubMedCentralGoogle Scholar
  28. Counotte GHM, Toussaint MJM, van Ederen AM, Gruys E (2002) Food safety and acute phase response. Proceedings of the third European Coloquium on acute phase proteins. Department of Veterinary Pathology, Kaap Doorn, ISBN: 90-9015940-de Villiers WJ, Louw JP, Strachan AGoogle Scholar
  29. Das T, Sen A, Kempf T, Pramanik SR, Mandal C, Mandal C (2003) Induction of glycosylation in human C-reactive protein under different pathological conditions. Biochem J 373(Pt 2):345–355PubMedPubMedCentralCrossRefGoogle Scholar
  30. Das T, Mandal C, Mandal C (2004a) Variations in binding characteristics of glycosylated human C-reactive proteins in different pathological conditions. Glycoconj J 20(9):537–543PubMedCrossRefGoogle Scholar
  31. Das T, Mandal C, Mandal C (2004b) Protein A-a new ligand for human C-reactive protein. FEBS Lett 576:107–113PubMedCrossRefGoogle Scholar
  32. Delange J, Langlois M, Ouyang J, Claeys G, De Buyzere M, Wuyts B (1998) Effect of haptoglobin phenotypes on growth of Streptococcus pyogenes. Clin Chem Lab Med 36:691–696Google Scholar
  33. Dinarello CA (1983) Pathogenesis of fever during hemodialysis. Contrib Nephrol 36:90–99PubMedCrossRefGoogle Scholar
  34. Dinarello CA (1984) Interleukin-1 and the pathogenesis of the acute-phase response. N Engl J Med 311:1413–1418PubMedCrossRefGoogle Scholar
  35. Dinarello CA (1989) Interleukin-1 and its biologically related cytokines. Adv Immunol 44:153–205PubMedCrossRefGoogle Scholar
  36. Dinarello CA (1996) Biologic basis for interleukin-1 in disease. Blood 87:2095–2147PubMedGoogle Scholar
  37. Dinarello CA (1997) Cytokines as endogenous pyrogens. In: Mackowiak PA (ed) Fever: basic mechanisms and management, 2nd edn. Lippincott-Raven, Philadelphia, pp 87–116Google Scholar
  38. Doğanavşargil E, Gümüşdiş G (2003) Romatolojik hastalıkların tanısında labaratuar yöntemleri. Klinik Romatoloji El Kitabı:117–118Google Scholar
  39. Dong Q, Wright JR (1996) Expression of C-reactive protein by alveolar macrophages. J Immunol 156:4815–4820PubMedGoogle Scholar
  40. Duffy LK, Bowyer RT, Testa JW, Faro JB (1996) Acute phase proteins and cytokines in Alaskan mammals as markers of chronic exposure to environmental pollutants. Am Fish Soc Symp 18:809–813Google Scholar
  41. Eckersall PD, Young FJ, McComb C, Hogarth CJ, Safi S, Weber A, McDonald T, Nolan AM, Fitzpatrick JL (2001) Acute phase proteins in serum and milk from dairy cows with clinical mastitis. Vet Rec 148:35–41PubMedCrossRefGoogle Scholar
  42. Ferard G, Gaudias J, Bourguignat A, Ingenbleek Y (2002) C-reactive protein to transthyretin ratio for the early diagnosis and follow-up of postoperative infection. Clin Chem Lab Med 40:1334–1338PubMedCrossRefGoogle Scholar
  43. Funke C, King DP, Brotheridge RM, Adelung D, Scott JL (1997) Harbor seal (phoca vitulina) C-reactive protein (C-RP): purification, characterization of specific monoclonal antibodies and development of an immuno- assay to measure serum C-RP concentrations. Vet Immunol Immunopathol 59:151–162PubMedCrossRefGoogle Scholar
  44. Gabay C, Kushner I (1999) Acute-phase proteins and other systemic responses to inflammation. N Engl J Med 340:448–454PubMedCrossRefGoogle Scholar
  45. Glass EJ, Craigmile SC, Springbett A, Preston PM, Kirvar E, Wilkie GM, Eckersall PD, Hall FR, Brown CG (2003) The protozoan parasite, Theileria annulata, induces a distinct acute phase protein response in cattle that is associated with pathology. Int J Parasitol 33:1409–1418PubMedCrossRefGoogle Scholar
  46. Godson DL, Bacaestrada ME, Vankessel AG, Hughes HPA, Morsy MA (1995) Regulation of bovine acute phase responses by recombinant interleukin-1. Can J Vet Res 59:249–255PubMedPubMedCentralGoogle Scholar
  47. Goitsuka R, Ohashi T (1990) IL-6 activity in feline infectious peritonitis. J Immunol 144:3195–3199Google Scholar
  48. Green PJ, Feizi T, Stoll MS, Thiel S, Prescott A, McConville MJ (1994) Recognition of the major cell surface glycoconjugates of Leishmania parasites by the human serum mannan-binding protein. Mol Biochem Parasitol 66:319–328PubMedCrossRefGoogle Scholar
  49. Gruys E (2002) Acute phase proteins in bovine medicine. In: AVMA 2002 convention notes. Proceedings 2002 of the American Veterinary Medical Association, Nashville, pp 317–321Google Scholar
  50. Gruys E, Snel FWJJ (1994) Animal models for reactive amyloidosis. Baillière’s Clin Rheumatol 8:599–611CrossRefGoogle Scholar
  51. Gruys E, Obwolo MJ, Toussaint MJM (1994) Diagnostic significance of the major acute phase proteins in veterinary clinical chemistry: a review. Vet Bull 64:1009–1018Google Scholar
  52. Gruys E, Toussaint MJM, Landman WJM, Tivapasi M, Chamanza R, van Veen L (1999) Infection, inflammation and stress inhibit growth. Mechanisms and non-specific assessment of the processes by acute phase proteins. In: Wensing T (ed) Production diseases in farm animals. 10th international conference, 1998. Wageningen Press, Wageningen, pp 72–87. ISBN: 90-74134-60-2Google Scholar
  53. Gruys E, Toussaint MJM, Niewold TA, Koopmans SJ (2005) Acute phase reaction and acute phase proteins. J Zhejiang Univ Sci B 6(11):1045–1056PubMedPubMedCentralCrossRefGoogle Scholar
  54. Guzel S, Andican G, Seven A, Aslan M, Bolayirli M, Guzel EC et al (2012) Acute phase response and oxidative stress status in familial Mediterranean fever (FMF). Mod Rheumatol 22:431–437PubMedCrossRefGoogle Scholar
  55. Haig DM, McInnes CJ, Thomson J, Wood A, Bunyan K (1998) The orf virus OV 20.0 L gene product is involved in interferon resistance and inhibits an interferon-inducible, double-stranded RNA-dependent kinase. Immunology 93:335–340PubMedPubMedCentralCrossRefGoogle Scholar
  56. Hallquist NA, Klasing KC (1994) Serotransferrin, ovotransferrin and metallothionein levels during an immune response in chickens. Comp Biochem Physiol Biochem Mol Biol 108:375–384PubMedCrossRefGoogle Scholar
  57. Hardardottir I, Grunfeld C, Feingold KR (1994) Effects of endotoxin and cytokines on lipid metabolism. Curr Opin Lipidol 5:207–215PubMedCrossRefGoogle Scholar
  58. Heinrich PC, Castell JV, Andus T (1990) Interleukin-6 and the acute phase response. Biochem J 265:621–636PubMedPubMedCentralCrossRefGoogle Scholar
  59. Heinrich PC, Behrmann I, Müller-Newen G, Schaper F, Graeve L (1998) Interleukin-6-type cytokine signaling through the gp130/Jak/STAT pathway. Biochem J 334:297–314PubMedPubMedCentralCrossRefGoogle Scholar
  60. Hirvonen J, Huszenicza G, Kulcsar M, Pyorala S (1999) Acute-phase response in dairy cows with acute postpartum metritis. Vet Bull 69:1198, abstr. 7665Google Scholar
  61. Höfner MC, Fosbery MW, Eckersall PD, Donaldson AI (1994) Haptoglobin response of cattle infected with foot-andmouth disease virus. Res Vet Sci 57:125–128PubMedCrossRefGoogle Scholar
  62. Hulten C, Sandgren B, Skioldebrand E, Klingeborn B, Marhaug G, Forsberg M (1999) The acute phase protein serum amyloid A (SAA) as an inflammatory marker in equine influenza virus infection. Acta Vet Scand 40:323–333Google Scholar
  63. Hurlimann J, Thorbecke GJ, Hochwald GM (1966) The liver as the site of C-reactive protein formation. J Exp Med 123:365–378PubMedPubMedCentralCrossRefGoogle Scholar
  64. Ingenbleek Y, Bernstein LH (1999a) The nutritionally dependent adaptive dichotomy (NDAD) and stress hypermetabolism. J Clin Ligand Assay 22:259–267Google Scholar
  65. Ingenbleek Y, Bernstein LH (1999b) The stressful condition as a nutritionally dependent adaptive dichotomy. Nutrition 15:305–320PubMedCrossRefGoogle Scholar
  66. Ingenbleek Y, Carpentier YA (1985) A prognostic inflammatory and nutritional index scoring critically ill patients. Int J Vitam Nutr Res 55:91–101PubMedGoogle Scholar
  67. Ingenbleek Y, Young V (1994) Transthyretin (prealbumin) in health and disease: nutritional implications. Annu Rev Nutr 14:495–533PubMedCrossRefGoogle Scholar
  68. Johnson RW (1997) Inhibition of growth by pro-inflammatory cytokines: an integrated view. J Anim Sci 75:1244–1255PubMedGoogle Scholar
  69. Johnson RW, Curtis SE, Dantzer R, Kelley KW (1993a) Central and peripheral prostaglandins are involved in sickness behavior in birds. Physiol Behav 53:127–131PubMedCrossRefGoogle Scholar
  70. Katoh N, Nakagawa H (1999) Detection of haptoglobin in the high-density lipoprotein and the very high-density lipoprotein fractions from sera of calves with experimental pneumonia and cows with naturally occurring fatty liver. J Vet Med Sci 61:119–124PubMedCrossRefGoogle Scholar
  71. Kilicarslan A, Uysal A, Roach EC (2013) Acute phase reactants. Acta Medica 2:2–7Google Scholar
  72. Kilpatrick L, McCawley L, Nachiappan V (1992) Alpha-1-antichymotrypsin inhibits the NADPH oxidase-enzyme complex in phorbol ester-stimulated neutrophil membranes. J Immunol 149:3059–3065PubMedGoogle Scholar
  73. Kimura M, Toth LA, Agostini H, Cady AB, Majde JA, Krueger JM (1995) Comparison of acute phase responses induced in rabbits by lipopolysaccharide and double-stranded RNA. Am J Physiol 36:1596–1605Google Scholar
  74. Kodama H, Arimitsu H (1999) Enhancement of phagocytic and chemokinetic activities of rainbow trout head kidney cells by C-reactive protein. Am J Vet Res 60:240–244PubMedGoogle Scholar
  75. Kraft R, Ruchti C, Burkhardt AH, Cottier H (1992) Pathogenetic principles in the development of gut-derived infectious-toxic shock (GITS) and multiple organ failure. Cur Stud Haematol Blood Transfus 59:204–240CrossRefGoogle Scholar
  76. Kushner I (1988) The acute phase response: an overview. Methods Enzymol 163:373–383PubMedCrossRefGoogle Scholar
  77. Kushner I (1993) Regulation of the acute phase response by cytokines. Perspect Biol Med 36:611–622PubMedCrossRefGoogle Scholar
  78. Kushner I, Gewurz H, Benson MD (1981) C-reactive protein and the acute-phase response. J Lab Clin Med 97(6):739–749PubMedGoogle Scholar
  79. Langhans W (1996) Bacterial products and the control of ingestive behavior: clinical implications. Nutrition 12:303–315PubMedCrossRefGoogle Scholar
  80. Ledue TB, Rifai N (2003) Preanalytic and analytic sources of variations in C-reactive protein measurement: Implications for cardiovascular disease risk assessment. Clin Chem 49:1258–1271PubMedCrossRefGoogle Scholar
  81. Li P, Mold C, Du Clos TW (1994) Sublytic complement attack exposes C-reactive protein binding sites on cell membranes. J Immunol 152(6):2995–3005PubMedGoogle Scholar
  82. Linke RP, 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 176:1100–1105PubMedCrossRefGoogle Scholar
  83. Lippincott’s illustrated reviews: immunology. Paperback: 384 pages. Williams & Wilkins, Lippincott, July 1, 2007. Language: English. ISBN 0-7817-9543-5. ISBN 978-0-7817-9543-2. Page 182Google Scholar
  84. Lippincott’s Illustrated Reviews: Immunology. Paperback: 384 pages. Publisher: Lippincott Williams & Wilkins; (July 1, 2007). 13: 978-0781795432:182Google Scholar
  85. Livneh A (2006) Amyloidosis of familial Mediterraneanfever (FMF): insights to FMF phenotype II. Harefuah 145:743–745PubMedGoogle Scholar
  86. Loeffler DA, Under MC, Zamany M, Harel E, Paul MA, Baumann H, LeWitt PA (1999) Measurement of acute phase proteins in the Rat Brain: contribution of vascular contents. Neurochem Res 24(10):1313–1317PubMedCrossRefGoogle Scholar
  87. Maes M, Bosmans E, Dejongh R, Kenis G, Van-Doolaeghe E, Naels H (1997) Increased serum IL-1 receptor antagonist concentrations in major depression and treatment resistant depression. Cytokines 9:853–858CrossRefGoogle Scholar
  88. Majno G, Joris I (1996) Cells, tissues and disease. Principles of general pathology. Blackwell Science, Cambridge, MA, pp 487–496Google Scholar
  89. McNair J, Kennedy DG, Bryson DG (1997) Evaluation of a competitive immunoassay for the detection of bovine haptoglobin. Res Vet Sci 63:145–149PubMedCrossRefGoogle Scholar
  90. Moldawer LL, Copeland EM 3rd (1997) Proinflammatory cytokines, nutritional support, and the cachexia syndrome: interactions and therapeutic options. Cancer 79(9):1828–1839PubMedCrossRefGoogle Scholar
  91. Morley JJ, Kushner I (1982) Serum C-reactive protein levels in disease. Ann N Y Acad Sci 389:406–418PubMedCrossRefGoogle Scholar
  92. Moshage H (1997) Cytokines and the hepatic acute phase response. J Pathol 181(3):257–266PubMedCrossRefGoogle Scholar
  93. Munford RS (2001) Statins and the acute-phase response. N Engl J Med 344:2016–2018PubMedCrossRefGoogle Scholar
  94. Murata H, Miyamoto T (1993) Bovine haptoglobin as a possible immunomodulator in the sera of transported calves. Br Vet J 149:277–283PubMedCrossRefGoogle Scholar
  95. Nakayama T, Sonoda S, Urano T, Yamada T, Okada M (1993) Monitoring both serum protein A and C-reactive protein as inflammatory markers in infectious diseases. Clin Chem 39:293–297PubMedGoogle Scholar
  96. Panter-Brick C, Lunn PG, Baker R, Todd A (2001) Elevated acute-phase protein in stunted Nepali children reporting low morbidity: different rural and urban profiles. Br J Nutr 85:125–131PubMedCrossRefGoogle Scholar
  97. Paul K, Boutain D, Agnew K, Thomas J, Hitti J (2008) The relationship between racial identity, income, stress and C-reactive protein among parous women: implications for preterm birth disparity research. J Natl Med Assoc 100(5):540–546PubMedCrossRefGoogle Scholar
  98. Petersen HH, Nielsen JP, Heegaard PMH (2004) Application of acute phase protein measurements in veterinary clinical chemistry. Vet Res 35:163–187PubMedCrossRefGoogle Scholar
  99. Pepys MB, Hirschfield GM (2003) C-reactive protein: a critical update. J Clin Invest 111:1805–1812PubMedPubMedCentralCrossRefGoogle Scholar
  100. Pfeffer A, Rogers KM (1993) Acute phase protein response, food intake, live weight change and lesions following intrathoracic injection of yeast in sheep. Res Vet Sci 55:360–366PubMedCrossRefGoogle Scholar
  101. Pyorala S (2000) Hirvonen’s thesis on acute phase response in dairy cattle. University of Helsinki. ISBN: 951-45-9106-
  102. Sinha S, Mandal C (1996) Microheterogeneity of C-reactive protein in the sera of fish Labeo rohita induced by metal pollutants. Biochem Biophys Res Commun 226(3):681–687PubMedCrossRefGoogle Scholar
  103. Sinha S, Mandal C, Allen AK, Mandal C (2001) Acute phase response of C-reactive protein of Labeo rohita to aquatic pollutants is accompanied by the appearance of distinct molecular forms. Arch Biochem Biophys 396(2):139–150PubMedCrossRefGoogle Scholar
  104. Sipe JD (1995) Acute-phase proteins in osteoarthritis. Semin Arthritis Rheum 25:75–86PubMedCrossRefGoogle Scholar
  105. Skinner JG, Roberts L (1994) Haptoglobin as an indicator of infection in sheep. Vet Rec 134:33–36PubMedCrossRefGoogle Scholar
  106. Smith DJ, Roberts D (1994) Effects of high volume and/or intense exercise on selected blood chemistry parameters. Clin Biochem 27:435–440PubMedCrossRefGoogle Scholar
  107. Srinivasan N, White HE, Emsley J, Wood SP, Pepys MB, Blundell TL (1994) Comparative analyses of pentraxins: Implications for protomer assembly and ligand binding. Structure 2(11):1017–1027PubMedCrossRefGoogle Scholar
  108. Tillett WS, Francis T (1930) Serological reactions in pneumonia with a non-protein somatic fraction of pneumococcus. J Exp Med 52(4):561–571PubMedPubMedCentralCrossRefGoogle Scholar
  109. Tirziu E (2009) Acute-phase proteins in immune response. Lucrări stiinłifice medicină veterinară XLII(1), timisoaraGoogle Scholar
  110. Tohjo H, Miyoshi F, Uchida E, Niiyama M, Syuto B, Moritsu Y, Ichikawa S, Takeauchi M (1995) Polyacrylamide gel electrophoretic patterns of chicken serum in acute inflammation induced by intramuscular injection of turpentine. Poult Sci 74:648–655PubMedCrossRefGoogle Scholar
  111. Toussaint MJM (2000) Acute phase protein in different species measured as a tool to assess animal health. Eur Colloquium Rep 1:1–3Google Scholar
  112. Toussaint MJM, van Ederen AM, Gruys E (1995) Implication of clinical pathology in assessment of animal health and in animal production and meat inspection. Comp Haematol Int 5:149–157CrossRefGoogle Scholar
  113. Toussaint MJM, van Ederen AM, Hulskamp-Koch CAM, Gruys E (1997) Measurement of acute phase proteins in porcine blood as a tool for clinical pathology in pigs. Comp Haematol Int 7:182Google Scholar
  114. Toussaint MJM, Eckersall PD, Alava M, Madec F, Meloen RH, Gruys E (2000a) Acute phase protein assays as tool in assessment of health in pigs. Proceedings of the ISACB congress Toulouse. Vet Med Rev 151:780Google Scholar
  115. Toussaint MJM, Lipperheide C, Eckersall PD, Alava M, Jobert JL, Heegaard PMH, Meloen RH, Madec F (2000b) Assessment of health in pigs by acute phase protein assays. In: Tielen MJM, Voets MT (eds) Proceedings of the Xth international congress on animal hygiene, vol 1. Animal Health Service Centre, Boxtel, pp 139–143. ISBN: 90-71649-04-0Google Scholar
  116. van Miert AS (1995) Pro-inflammatory cytokines in a ruminant model: pathophysiological, pharmacological, and therapeutic aspects. Vet Q 17(2):41–50PubMedCrossRefGoogle Scholar
  117. van Reeth K, Nauwynck H, Pensaert M (1998) Bronchoalveolar interferon-alpha, tumor necrosis factor-alpha, interleukin-1, and inflammation during acute influenza in pigs: a possible model for humans? J Infect Dis 177:1076–1079PubMedCrossRefGoogle Scholar
  118. Werling D, Sutter F, Arnold M, Kun G, Tooten PCJ, Gruys E, Kreuzer M, Langhans W (1996) Characterisation of the acute phase response of heifers to a prolonged low dose infusion of lipopolysaccharide. Res Vet Sci 61:252–257PubMedCrossRefGoogle Scholar
  119. Wigmore SJ, Fearon KC, Maingay JP, Lai PB, Ross JA (1997) Interleukin-8 can mediate acute-phase protein production by isolated human hepatocytes. Am J Physiol 273:720–726Google Scholar
  120. Wu T, Dorn JP, Donahue RP, Sempos CT, Trevisan M (2002) Associations of serum C-reactive protein with fasting insulin, glucose, and glycosylated hemoglobin. Am J Epidemiol 155:65–71PubMedCrossRefGoogle Scholar
  121. Zheng H, Fletcher D, Kozak W, Jiang M, Hofmann KJ, Conn CA, Soszynski D, Grabiec C, Trumbauer ME, Shaw A et al (1995) Resistance to fever induction and impaired acute-phase response in interleukin-1 b-deficient mice. Immunity 3(1):9–19PubMedCrossRefGoogle Scholar

Copyright information

© Springer India 2016

Authors and Affiliations

  • Waliza Ansar
    • 1
  • Shyamasree Ghosh
    • 2
  1. 1.Department of ZoologyBehala CollegeKolkataIndia
  2. 2.National Institute of Science EducationSchool of Biological SciencesBhubaneswarIndia

Personalised recommendations