Full Text:  <3282>

CLC number: Q95

On-line Access: 

Received: 2005-07-25

Revision Accepted: 2005-08-19

Crosschecked: 0000-00-00

Cited: 0

Clicked: 7650

Citations:  Bibtex RefMan EndNote GB/T7714

-   Go to

Article info.
1. Reference List
Open peer comments

Journal of Zhejiang University SCIENCE B 2005 Vol.6 No.11 P.1045~1056


Acute phase reaction and acute phase proteins


Affiliation(s):  Department of Pathobiology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, the Netherlands; more

Corresponding email(s):   e.gruys@vet.uu.nl

Key Words:  Acute phase protein, Acute phase reaction, Animal health, Assessment, Cytokine, Index, Nutrition

Share this article to: More |Next Article >>>

GRUYS E., TOUSSAINT M.J.M., NIEWOLD T.A., KOOPMANS S.J.. Acute phase reaction and acute phase proteins[J]. Journal of Zhejiang University Science B, 2005, 6(1): 1045~1056.

@article{title="Acute phase reaction and acute phase proteins",
journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

%0 Journal Article
%T Acute phase reaction and acute phase proteins
%J Journal of Zhejiang University SCIENCE B
%V 6
%N 11
%P 1045~1056
%@ 1673-1581
%D 2005
%I Zhejiang University Press & Springer

T1 - Acute phase reaction and acute phase proteins
J0 - Journal of Zhejiang University Science B
VL - 6
IS - 11
SP - 1045
EP - 1056
%@ 1673-1581
Y1 - 2005
PB - Zhejiang University Press & Springer
ER -

A review of the systemic acute phase reaction with major cytokines involved, and the hepatic metabolic changes, negative and positive acute phase proteins (APPs) with function and associated pathology is given. It appears that APPs represent appropriate analytes for assessment of animal health. Whereas they represent non-specific markers as biological effect reactants, they can be used for assessing nutritional deficits and reactive processes, especially when positive and negative acute phase variables are combined in an index. When such acute phase index is applied to separate healthy animals from animals with some disease, much better results are obtained than with single analytes and statistically acceptable results for culling individual animals may be reached. Unfortunately at present no cheap, comprehensive and easy to use system is available for assessing various acute phase proteins in serum or blood samples at the same time. Protein microarray or fluid phase microchip technology may satisfy this need; and permit simultaneous analysis of numerous analytes in the same small volume sample and enable integration of information derived from systemic reactivity and nutrition with disease specific variables. Applying such technology may help to solve health problems in various countries not only in animal husbandry but also in human populations.

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article


[1] Abdalla, S.A., Hiriuchi, H., Furusawa, S., Matsuda, H., 2004. Molecular cloning and characterization of chicken tumor necrosis factor (TNF)-superfamily ligands, CD30L and TNF-related apoptosis inducing ligand (TRAIL). J. Vet. Med. Sci., 66:643-650.

[2] Adler, K.L., Peng, P.H., Peng, R.K., Klasing, K.C., 2001. The kinetics of hemopexin and α1-acid glycoprotein levels induced by injection of inflammatory agents in chickens. Avian. Dis., 45:289-296.

[3] Alava, M.A., Gonzalez-Ramon, N., Heegaard, P., Guzylack, S., Toussaint, M.J.M., Lipperheide, C., Madec, F., Gruys, E., Eckersall, P.D., Lampreave, F., et al., 1997. Pig-MAP, porcine acute phase proteins and standardisation of assays in Europe. Comp. Haematol. Internat., 7:208-213.

[4] Alcorn, J.M., Fierer, J., Chojkier, M., 1992. The acute phase response protects mice from D-galactosamine sensitization to endotoxin and tumor necrosis factor-α. Hepatology, 15:122-129.

[5] Alexander, J.W., MacMillan, B.G., Stinnnett, J.D., Ogle, C., Bozian, R.C., Fischer, J.E., Oakes, J.B., Morris, M.J., Krummel, R., 1980. Beneficial effects of aggressive protein feeding in severely burned children. Ann. Surg., 192:505-517.

[6] Alsemgeest, S.P.M., 1994. Blood Concentrations of Acute-Phase Proteins in Cattle as Markers for Disease. PhD Thesis, Utrecht University, Utrecht, the Netherlands, ISBN: 90-3-0573-0.

[7] Alsemgeest, S.P.M., Taverne, M.A.M., Boosman, R., van der Weyden, G.C., Gruys, E., 1993. Peripartum acute-phase protein serum amyloid-A concentration, in plasma of cows and fetuses. Am. J. Vet. Res., 54:164-167.

[8] Alsemgeest, S.P.M., Kalsbeek, H.C., Wensing, T., Koeman, J.P., van Ederen, A.M., Gruys, E., 1994. Concentrations of serum amyloid-A (SAA) and haptoglobin (Hp) as parameters of inflammatory diseases in cattle. Vet. Quart., 16:21-23.

[9] Baeten, J.M., Richardson, B.A., Bankson, D.D., Wener, M.H., Kreiss, J.K., Lavreys, L., Mandaliya, K., Bwayo, J.J., McClelland, R.S., 2004. Use of serum retinol-binding protein for prediction of vitamin A deficiency: effects of HIV-1 infection, protein malnutrition, and the acute phase response. Am. J. Clin. Nutr., 79:218-225.

[10] Baybutt, H.N., Holsboer, F., 1990. Inhibition of macrophage differentiation and function by cortisol. Endocrinology, 127:476-480.

[11] Blackburn, W.D., 1994. Validity of acute phase proteins as markers of disease activity. J. Rheumatol., 21(Suppl 42):9-13.

[12] Bonnefoy, M., Ayzac, L., Ingenbleek, Y., Kostka, T., Boisson, R.C., Bienvenu, J., 1998. Usefulness of the prognostic inflammatory and nutritional index (PINI) in hospitalized elderly patients. Int. J. Vitam. Nutr. Res., 68:189-195.

[13] Chamanza, R., Toussaint, M.J.M., van Ederen, A.M., van Veen, L., Hulskamp-Koch, C., Fabri, T.H., 1999a. Serum amyloid A and transferrin in chicken. A preliminary investigation of using acute-phase variables to assess diseases in chickens. Vet. Quart., 21:158-162.

[14] Chamanza, R., van Veen, L., Tivapasi, M.T., Toussaint, M.J.M., 1999b. Acute phase proteins in the domestic fowl. World’s Poult. Sci., 55:61-71.

[15] Cooper, E.H., Ward, A.H., 1979. Acute phase reactant proteins as aids to monitoring disease. Invest. Cell Pathol., 2:293-301.

[16] Counotte, G.H.M., Toussaint, M.J.M., van Ederen, A.M., 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: 90-9015940-1.

[17] de Villiers, W.J., Louw, J.P., Strachan, A.F., Etsebeth, S.M., Shephard, E.G.F.C., de Beer, F.C., 1990. C-reactive protein and serum amyloid A protein in pregnancy and labour. Brit. J. Obst. Gynaecol., 97:725-730.

[18] Dinarello, C.A., 1983. Pathogenesis of fever during hemodialysis. Contr. Nephrol., 36:90-99.

[19] Dinarello, C.A., 1989. Interleukin-1 and its biologically related cytokines. Adv. Immunol., 44:153-205.

[20] Disilvestro, R.A., Carlson, G.P., 1992. Inflammation, an inducer of metallothionein, inhibits carbon-tetrachloride-induced hepatotoxicity in rats. Toxicol. Lett., 60:175-181.

[21] Dowton, S.B., Colten, H.R., 1988. Acute phase reactants in inflammation and infection. Sem. Hematol., 25:84-90.

[22] Duffy, L.K., Bowyer, R.T., Testa, J.W., Faro, J.B., 1996. Acute phase proteins and cytokines in Alaskan mammals as markers of chronic exposure to environmental pollutants. Am. Fish. Soc. Symp., 18:809-813.

[23] Duthie, S., Eckersall, P.D., Addie, D.D., Lawrence, C.E., Jarrett, O., 1997. Value of α1-acid glycoprotein in the diagnosis of feline infectious peritonitis. Vet. Rec., 141:299-303.

[24] Eckersall, P.D., Harvey, M.J.A., Ferguson, J.M., Renton, J.P., Nickson, D.A., Boyd, J.S., 1993. Acute phase proteins in canine pregnancy (Canis familiaris). J. Reprod. Fert., 47(Suppl):159-164.

[25] Eckersall, P.D., Young, F.J., McComb, C., Hogarth, C.J., Safi, S., Weber, A., McDonald, T., Nolan, A.M., Fitzpatrick, J.L., 2001. Acute phase proteins in serum and milk from dairy cows with clinical mastitis. Vet. Rec., 148:35-41.

[26] El Beitune, P., Duarte, G., de Morais, E.N., Quintana, S.M., Vannucchi, H., 2003. Vitamin A deficiency and clincial associations: a review. Arch. Latinoam. Nutr., 53:355-363.

[27] El Ghmati, S.M., van Hoeyveld, E.M., van Strijp, J.G., Ceuppens, J.L., Stevens, E.A., 1996. Identification of haptoglobin as an alternative ligand for CD11B/CD18. J. Immunol., 156:2542-2552.

[28] 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., 40:1334-1338.

[29] Funke, C., King, D.P., Brotheridge, R.M., Adelung, D., Scott, J.L., 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., 59:151-162.

[30] Glass, E.J., Craigmile, S.C., Springbett, A., Preston, P.M., Kirvar, E., Wilkie, G.M., Eckersall, P.D., Hall, F.R., Brown, C.G., 2003. The protozoan parasite, Theileria annulata, induces a distinct acute phase protein response in cattle that is associated with pathology. Int. J. Parasitol., 33:1409-1418.

[31] Goff, J.P., Stabel, J.R., 1990. Decreased plasma retinol, α-tocopherol, and zinc concentration during the periparturient period: effect of milk fever. J. Dairy Sci., 73:3195-3199.

[32] Gordon, A.H., Koy, A., 1985. The Acute Phase Response to Injury and Infection. The Roles of Interleukin 1 and Other Mediators. Elsevier, Amsterdam, ISBN: 0444-80648-2.

[33] Gruys, E., 2002. Acute Phase Proteins in Bovine Medicine. In: AVMA 2002 Convention Notes. Proceedings 2002 of the American Veterinary Medical Association. Nashville, p.317-321.

[34] Gruys, E., Snel, F.W.J.J., 1994. Animal models for reactive amyloidosis. Baillière’s Clin. Rheumatol., 8:599-611.

[35] Gruys, E., Obwolo, M.J., Toussaint, M.J.M., 1994. Diagnostic significance of the major acute phase proteins in veterinary clinical chemistry: a review. Vet. Bull., 64:1009-1018.

[36] Gruys, E., Tooten, P.C.J., Kuijpers, M.H.M., 1996. Lung, ileum and heart are predilection sites for AApoAII amyloid deposition in CD-1 Swiss mice used for toxicity studies. Pulmonary amyloid indicates AApoAII. Lab. Anim., 30:28-34.

[37] Gruys, E., Toussaint, M.J.M., Landman, W.J.M., 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, p.72-87. ISBN: 90-74134-60-2.

[38] Hallquist, N.A., Klasing, K.C., 1994. Serotransferrin, ovotransferrin and metallothionein levels during an immune response in chickens. Comp. Biochem. Physiol. Biochem. Mol. Biol., 108:375-384.

[39] Heinrich, P.C., Castell, T.A., Andus, T., 1990. Interleukin-6 and the acute phase response. Biochem. J., 265:621-636.

[40] Heinrich, P.C., Behrmann, I., Müller-Newen, G., Schaper, F., Graeve, L., 1998. Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway. Biochem. J., 334:297-314.

[41] Höfner, M.C., Fosbery, M.W., Eckersall, P.D., Donaldson, A.I., 1994. Haptoglobin response of cattle infected with foot-and-mouth disease virus. Res. Vet. Sci., 57:125-128.

[42] 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., 40:323-333.

[43] 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.

[44] 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.

[45] Ingenbleek, Y., Carpentier, Y.A., 1985. A prognostic inflammatory and nutritional index scoring critically ill patients. Int. J. Vit. Nutrit. Res., 55:91-101.

[46] Ingenbleek, M., Young, V., 1994. Transthyretin (prealbumin) in health and disease: nutritional implications. Ann. Rev. Nutr., 14:495-533.

[47] Ingenbleek, Y., Bernstein, L.H., 1999a. The nutritionally dependent adaptive dichotomy (NDAD) and stress hypermetabolism. J. Clin. Lig. Ass., 22:259-267.

[48] Ingenbleek, Y., Bernstein, L.H., 1999b. The stressful condition as a nutritionally dependent adaptive dichotomy. Nutrition, 15:305-320.

[49] Jacquier-Sarlin, M.R., Fuller, K., Dinx-Xuan, A.T., Richard, M.J., Polla, B.S., 1994. Protective effects of HSP70 in inflammation. Experientia, 50:1032-1038.

[50] Johnson, R.W., 1997. Inhibition of growth by pro-inflammatory cytokines: an integrated view. J. Anim. Sci., 75:1244-1255.

[51] Johnson, R.W., Borell, E., 1994. Lipopolysaccharide-induced sickness behavior in pigs is inhibited by pretreatment with indomethacin. J. Anim. Sci., 72:309-314.

[52] Johnson, R.W., Curtis, S.E., Dantzer, R., Kelley, K.W., 1993a. Central and peripheral prostaglandins are involved in sickness behavior in birds. Physiol. Behav., 53:127-131.

[53] Johnson, R.W., Curtis, S.E., Dantzer, R., Bahr, J.M., Kelley, K.W., 1993b. Sickness behavior in birds caused by peripheral or central injection of endotoxin. Physiol. Behav., 53:343-348.

[54] Kaiser, P., Rothwell, L., Goodchild, M., Bumstead, N., 2004. The chicken proinfllammatory cytokines interleukin-1 beta and interleukin-6: differences in gene structure and genetic location compared with their mammalian orthologues. Anim. Genet., 35:169-175.

[55] Kaiser, P., Poh, T.Y., Rothwell, L., Avery, S., Balu, S., Pathiana, U.S., Hughes, S., Goodchild, M., Morrelll, S., Watson, M., et al., 2005. A genomic analysis of chicken cytokines and chemokines. J. Interferon. Cytokine. Res., 25:467-484.

[56] Kimura, M., Toth, L.A., Agostini, H., Cady, A.B., Majde, J.A., Krueger, J.M., 1995. Comparison of acute phase responses induced in rabbits by lipopolysaccharide and double-stranded RNA. Am. J. Physiol. Reg. Int. Comp. Physiol., 36:1596-1605.

[57] Kisilevsky, R., Gruys, E., Shirahama, T., 1994. Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity? Amyloid: Int. J. Exp. Clin. Invest., 2:128-133.

[58] Knolle, P., Lohr, H., Treichel, U., Dienes, H.P., Lohse, A., Schlaack, J., Gerken, G., 1995. Parenchymal and nonparenchymal liver cells and their interaction in the local immune response. Zeitschr Gastroenterol, 33:613-620.

[59] Koets, A.P., de Schwartz, N., Tooten, P., Kankofer, M., Broekhuijsen-Davies, J.M., Rutten, V.P.M.G., van Leengoed, L.A.M.G., Taverne, M.A.M., Gruys, E., 1998. Release of proinflammatory cytokines related to luteolysis and the periparturient acute phase response in prostaglandin-induced parturition in cows. Theriogenology, 49:797-812.

[60] Kraft, R., Ruchti, C., Burkhardt, A.H., Cottier, H., 1992. Pathogenetic principles in the development of gut-derived infectious-toxic shock (GITS) and multiple organ failure. Cur. Stud. Haematol. Blood Transfus., 59:204-240.

[61] Kushner, I., Gewurz, H., Benson, M.D., 1981. C-reactive protein and the acute-phase response. J. Lab. Clin. Med., 97:739-749.

[62] Landman, W.J.M., Sletten, K., Koch, C.A.M., Tooten, P.C.J., Gruys, E., 1996. Chicken joint amyloid protein is of the SAA-type. I. Characterization of the amyloid protein. Scand. J. Immunol., 43:210-218.

[63] Langhans, W., 1996. Bacterial products and the control of ingestive behavior: clinical implications. Nutrition, 12:303-315.

[64] Lannergard, A., Larsson, A., Kragsbjerg, P., Friman, G., 2003. Correlations between serum amyloid A protein and C-reactive protein in infectious diseases. Scand. J. Clin. Lab. Invest., 63:267-272.

[65] Larson, M.A., Wei, S.H., Weber, A., Mack, D.R., McDonald, T.L., 2003a. Human serum amyloid A3 peptide enhances intestinal MUC3 expression and inhibits EPEC adherence. Biochem. Biophys. Res. Commun., 300:531-540.

[66] Larson, M.A., Wei, S.H., Weber, A., McDonald, T.L., 2003b. Induction of human mammary-associated serum amyloid A3 expression by prolactin or lipopolysaccharide. Biochem. Biophys. Res. Commun., 301:1030-1037.

[67] Larson, M.A., Weber, A., Weber, A.T., McDonald, T.L., 2005. Differential expression and secretion of bovine serum amyloid A3 (SAA3) by mammary epithelial cells stimulated with prolactin or lipopolysaccharide. Vet. Immunol. Immunopathol., 107:255-264.

[68] Le, J., Vilcek, J., 1989. Interleukin 6: a multifunctional cytokine regulating immune reactions and the acute phase protein response. Lab. Invest., 61:588-602.

[69] Leshchinsky, T.V., Klasing, K.C., 2003. Profile of chicken cytokines induced by lipopolysaccharide is modulated by dietary alpha-tocopherol acetate. Poultry Sci., 82:1266-1273.

[70] 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.

[71] Loyer, P., Iiyin, G., Razzak, Z.A., Banchereau, J., Dezier, J.F., Campion, J.P., Guguenguillouzo, C., Guillouzo, A., 1993. Interleukin-4 inhibits the production of some acute-phase proteins by human hepatocytes in primary culture. FEBS Letters, 336:215-220.

[72] Lynagh, G.R., Bailey, M., Kaiser, P., 2000. Interleukin-6 is produced during both murine and avian Eimeria infections. Vet. Immunol. Immunopathol., 76:98-102.

[73] Mack, D.R., McDonald, T.L., Larson, M.A., Wei, S.H., Weber, A., 2003. The conserved TFLK motif of mammary-associated serum amyloid A3 is responsible for up-regulation of intestinal MUC3 mucin expression in vitro. Pediatr. Res., 53:137-142.

[74] Magnus, J.H., Stenstad, T., Husby, G., 1994. Proteoglycans, glycosaminoglycans and amyloid deposition. Baillière’s Clin. Rheumatol., 8:575-597.

[75] Majno, G., Joris, I., 1996. Cells, Tissues and Disease. Principles of General Pathology. Blackwell Science, Cambridge Mass, USA, p.487-496. ISBN: 0-86542-372-5.

[76] Mazur-Gonkowska, B., Koncicki, A., Krasnodebska-Depta, A., 2004. Assessment of acute phase response in turkeys experimentally infected with Escherichia coli or haemorrhagic enteritis virus. Bull. Vet. Inst. Pulawy., 48:19-23.

[77] McDonald, T.L., Larson, M.A., Mack, D.R., Weber, A., 2001. Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum. Vet. Immunol. Immunopathol., 83:203-211.

[78] McGuire, W., Alessandro, U.D., Olaleye, B.O., Thomson, M.C., Langerock, P., Greenwood, B.M., Kwiatkowski, D., 1996. C-reactive protein and haptoglobin in the evaluation of a community-based malaria control programme. Transact. Royal. Soc. Trop. Med. Hyg., 90:10-14.

[79] 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.

[80] Monshouwer, M., Witkamp, R.F., Nijmeijer, S.M., van Leengoed, L.A.M.G., Verheyden, J.H.M., van Miert, A.S.J.P.A.M., 1995a. Infection (Actinobacillus pleuropneumoniae)-mediated suppression of oxidative hepatic drug metabolism and cytochrome P4503A mRNA levels in pigs. Drug. Metabol. Dispos., 23:44-47.

[81] Monshouwer, M., Witkamp, R.F., Nijmeijer, S.M., Pijpers, A., Verheyden, J.H.M., van Miert, A.S.J.P.A.M., 1995b. Selective effects of a bacterial infection (Actinobacillus pleuropneumoniae) on the hepatic clearances of caffeine, antipyrine, paracetamol, and indocyanine green in the pig. Xenobiotica, 25:491-499.

[82] Monshouwer, M., Witkamp, R.F., Nijmeijer, S.M., van Leengoed, L.A.M.G., Vernooy, H.C.M., Verheyden, J.H.M., van Miert, A.S.J.P.A.M., 1996a. A lipopolysaccharide-induced acute phase response in the pig is associated with a decrease in hepatic cytochrome P450-mediated drug metabolism. J. Vet. Pharmacol. Therap., 19:382-388.

[83] Monshouwer, M., Witkamp, R.F., Nijmeijer, S.M., van Amsterdam, J.G., van Miert, A.S.J.P.A.M., 1996b. Suppression of cytochrome P450- and UDP glucuronosyl transferase-dependent enzyme activities by proinflammatory cytokines and possible nitric oxide in primary cultures of pig hepatocytes. Toxicol. Appl. Pharmacol., 137:237-244.

[84] Morgan, E.T., 1997. Regulation of cytochromes P450 during inflammation and infection. Drug. Metabol. Rev., 29:1129-1188.

[85] Morgan, E.T., Thomas, K.B., Swanson, R., Vales, T., Hwang, J., Wright, K., 1994. Selective suppression of cytochrome P-450 gene expression by interleukins 1 and 6 in rat liver. Biochim. Biophys. Acta, 1219:475-483.

[86] Morlese, J.F., Forrester, T., Jahoor, F., 1998. Acute-phase protein response to infection in severe malnutrition. Am. J. Physiol. Endocrinol. Metabol., 38:E112-E117.

[87] Nabuurs, M., 1995. Microbiological, structural and functional changes of the small intestine of pigs at weaning. Pig News Inform., 16:93N-97N.

[88] Nakamura, K., Mitarai, Y., Yoshioka, M., Koizumi, N., Shibahara, T., Nakajima, Y., 1998. Serum levels of interleukin-6, α1-acid glycoprotein, and corticosterone in two-week-old chickens inoculated with Escherichia coli lipopolysaccharide. Poultry. Sci., 77:908-911.

[89] 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., 39:293-297.

[90] Odink, J., Smeets, J.F.M., Visser, I.J.R., Sandman, H., Snijders, J.M.A., 1990. Haematological and clinicochemical profiles of healthy swine and swine with inflammatory processes. J. Anim. Sci., 68:163-170.

[91] Patterson, L.T., Mora, E.C., 1964. Occurrence of a subsyance analogus to C-reactive protein in the blood of the domestic fowl. Tex. Rep. Biol. Med., 22:716-721.

[92] Patterson, L.T., Mora, E.C., 1965. The C-reactive protein response and disease resistance in the domestic fowl. Tex. Rep. Biol. Med., 23:600-606.

[93] Pepys, M.B., 1981. C-reactive protein fifty years on. Lancet., 21:653-656.

[94] Petersen, H.H., Nielsen, J.P., Heegaard, P.M.H., 2004. Application of acute phase protein measurements in veterinary clinical chemistry. Vet. Res., 35:163-187.

[95] Pinelli, E., 1996. Protective Immune Responses against Leishmania in Dogs. PhD Thesis, Utrecht University, Utrecht, the Netherlands, ISBN: 90-9009302-8.

[96] Pue, C.A., Mortensen, R.F., Marsh, C.B., Pope, H.A., Webers, M.D., 1996. Acute phase levels of C-reactive protein enhance IL-1β and IL-1ra production by human blood monocytes but inhibit IL-1β and IL-ra production by alveolar macrophages. J. Immunol., 156:1594-1600.

[97] Pyorala, S., 2000. Hirvonen’s Thesis on Acute Phase Response in Dairy Cattle. University of Helsinki, ISBN: 951-45-9106-2. http://ethesis.helsinki.fi/julkaisut/ela/kliin/hirvonen/.

[98] Reeds, P.J., Fjeld, C.R., Jahoor, F., 1994. Do the differences between the amino acid compositions of acute-phase and muscle proteins have a bearing on nitrogen loss in traumatic states? J. Nutr., 124:906-910.

[99] 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.

[100] Schroedl, W., Fuerll, B., Reinhold, P., Krueger, M., Schuett, C., 2001. A novel acute phase marker in cattle: lipopolysaccharide binding protein (LBP). J. Endotoxin. Res., 7:49-52.

[101] Sehgal, P.B., Grieninger, G., Tosato, G., 1989. Regulation of the acute phase and immune responses: interleukin-6. Ann. New York Acad. Sci., 557:1-583.

[102] Sijben, J.W., Klasing, K.C., Schrama, J.W., Parmentier, H.K., van der Poel, J.J., Savelkoul, H.F., Kaiser, P., 2003. Early in vivo cytokine gene expression in chickens after challenge with Salmonalla typhymirium lipopolysaccharide and modulation by dietary n-3 polyunsaturated fatty acids. Dev. Comp. Immunol., 27:611-619.

[103] Sipe, J.D., 1995. Acute-phase proteins in osteoarthritis. Sem. Arthr. Rheum., 25:75-86.

[104] Smith, D.J., Roberts, D., 1994. Effects of high volume and/or intense exercise on selected blood chemistry parameters. Clin. Biochem., 27:435-440.

[105] Sordillo, L.M., Pighetti, G.M., Davis, M.R., 1995. Enhanced production of bovine tumor necrosis factor-á during the periparturient period. Vet. Immunol. Immunopathol., 49:263-270.

[106] Stephensen, C.B., 1999. Burden of infection on growth failure. J. Nutr., 129(Suppl):534S-538S.

[107] Stephensen, C.B., 2001. Vitamin A, infection, and immune function. Annu. Rev. Nutr., 21:167-192.

[108] Stephensen, C.B., Gildengorin, G., 2000. Serum retinol, the acute phase response, and the apparent misclassification of vitamin A status in the third National Health and Nutrition Examination Survey. Am. J. Clin. Nutr., 72:1170-1178.

[109] Takahashi, K., Ohta, N., Akiba, Y., 1997. Influences of dietary methionine and cysteine on metabolic responses to immunological stress by Escherichia coli lipopolysaccharide injection, and mitogenic response in broiler chickens. Br. J. Nutr., 78:815-821.

[110] Tape, C., Tan, R., Nesheim, M., Kisilevsky, R., 1987. Direct evidence for circulating apoSAA as the precursor of tissue AA amyloid deposits. Scand. J. Immunol., 28:317-324.

[111] Tillett, W.S., Francis, T., 1930. Serological reactions in pneumonia with a non-protein somatic fraction of Pneumococcus. J. Exp. Med., 52:561-571.

[112] 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. Poultry Sci., 74:648-655.

[113] Tohjo, H., Yadatsu, M., Uchida, E., Niiyama, M., Syuto, B., Moritsu, Y., Ichikawa, S., Takeuchi, M., 1996. Polyacrylamide gel electrophoretic serum protein patterns of acute inflammation induced by intramuscular injection of turpentine in young broiler chickens. J. Vet. Med. Sci., 58:267-268.

[114] Toussaint, M.J.M., 2000. Acute phase protein in different species measured as a tool to assess animal health. European Colloquium Report, 1:1-3.

[115] Toussaint, M.J.M., van Ederen, A.M., Gruys, E., 1995. Implication of clinical pathology in assessment of animal health and in animal production and meat inspection. Comp. Haematol. Internat., 5:149-157.

[116] Toussaint, M.J.M., van Ederen, A.M., Hulskamp-Koch, C.A.M., Gruys, E., 1997. Measurement of acute phase proteins in porcine blood as a tool for clinical pathology in pigs. Comp. Haematol. Internat., 7:182.

[117] Toussaint, M.J.M., Eckersall, P.D., Alava, M., Madec, F., Meloen, R.H., Gruys, E., 2000a. Acute phase protein assays as tool in assessment of health in pigs. Proc. ISACB congress Toulouse. Rev. Vet. Med., 151:780.

[118] Toussaint, M.J.M., Lipperheide, C., Eckersall, P.D., Alava, M., Jobert, J.L., Heegaard, P.M.H., Meloen, R.H., Madec, F., 2000b. Assessment of Health in Pigs by Acute Phase Protein Assays. In: Tielen, M.J.M., Voets, M.T. (Eds.), Proceedings of the Xth International Congress on Animal Hygiene, Vol. 1. Animal Health Service Centre, Boxtel, the Netherlands, p.139-143. ISBN: 90-71649-04-0.

[119] Uchida, E., Katoh, N., Takahashi, K., 1993. Appearance of haptoglobin in serum from cows at parturition. J. Vet. Med. Sci., 55:893-894.

[120] Upragarin, N., 2005. In vitro Studies on the Pathogenesis of AA Amyloid Arthropathy in Chicken. PhD Thesis, Utrecht, the Netherlands, ISBN: 90-393-4038-2.

[121] van Gool, J., Boers, W., Sala, M., Ladiges, N.C.J.J., 1984. Glucocorticoids and catecholamines as mediators of acute-phase proteins especially rat α-macrofoetoprotein. Biochem. J., 220:125-132.

[122] van Miert, A.S.J.P.A.M., 1995. Pro-inflammatory cytokines in a ruminant model: pathophysiological, pharmacological, and therapeutic aspects. Vet. Quart., 175:41-50.

[123] 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., 177:1076-1079.

[124] Werling, D., Sutter, F., Arnold, M., Kun, G., Tooten, P.C.J., Gruys, E., 1996. Characterisation of the acute phase response of heifers to a prolonged low dose infusion of lipopolysaccharide. Res. Vet. Sci., 61:252-257.

[125] West, K.P., 2004. Vitamin A deficiency as a preventable cause of maternal mortality in undernourished societies: plausibility and next steps. Int. J. Gynaecol. Obstet., 85:S24-27.

[126] Xie, H., Huff, G.R., Huff, W.E., Balog, J.M., Holt, P., Rath, N.C., 2002. Identification of ovotransferrin as an acute phase protein in chickens. Poultry Sci., 81:112-120.

[127] Yamada, T., Kluve-Beckerman, B., Kuster, W.M., Liepnieks, J.J., Benson, M.D., 1994. Measurement of serum amyloid-A4 (SAA4): its constitutive presence in serum. Amyloid: Int. J. Exp. Clin. Invest., 1:114-118.

[128] 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.

[129] Yamamoto, M., Katoh, N., Yoshikazu, A., 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.

Open peer comments: Debate/Discuss/Question/Opinion



2014-09-01 18:42:54

for my phd thesis


2014-04-09 03:21:27

I need to know more about this subject.

gehad@No address<gehad.donia@yahoo.com>

2013-02-21 16:44:45

iam interesting by this subject


2011-05-04 03:23:18

Useful paper


2010-12-24 18:31:14



2010-12-24 16:20:38

Useful article

Please provide your name, email address and a comment

Journal of Zhejiang University-SCIENCE, 38 Zheda Road, Hangzhou 310027, China
Tel: +86-571-87952276; Fax: +86-571-87952331; E-mail: jzus@zju.edu.cn
Copyright © 2000 - Journal of Zhejiang University-SCIENCE