Abstract
Acute phase proteins are serum proteins which increase in concentration during the acute phase response to inflammation or infection. The response occurs in all animals, but in different species the response of individual proteins can be significantly different. Of the numerous acute phase proteins which have been identified in humans, a number have been examined in cattle and dogs but usually on an individual basis with little reference to their part in the acute phase response. Biochemical, physiological and clinical investigations into haptoglobin, fibrinogen, α1-proteinase inhibitor, ceruloplasmin, seromucoid and C-reactive protein of cattle and dogs have therefore been reviewed with the emphasis on their role in this response to tissue damage.
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Allen, R. C., Bienvenu, J., Laurent, P. & Suskind, R. M. 1982. Marker proteins in inflammation, (de Gruyter, New York)
Barsanti, J. A., Kristensen, F. & Drumheller, F. B. 1977. Analysis of serum proteins, using agarose electrophoresis in normal dogs and dogs naturally infected with Dirofilaria immitis. Am. J. Vet. Res., 38, 1055–1058.
Beatty, K., Bieth, J. & Travis, J. 1980. Kinetics of association of serine proteinases with native and oxidised α1-proteinase inhibitor and α1-antichymotrypsin. J. Biol. Chem., 255, 3931–3934
Bingley, J. B. & Dick, A. T. 1969. The pH optimum for ceruloplasmin oxidase activity in the plasma of several species of animal. Clin. Chim. Acta., 25, 480–482
Blakeslee, D. & Stone, W. H. 1971. Serum antigens of cattle. III Immunologic assay of cattle haptoglobin. Vox. Sang., 21, 175–182
Bremner, K. C. 1964. Studies on haptoglobin and haemopexin in the plasma of cattle. Aust. J. Exp. Biol. Med. Sci., 42, 643–656
Calabrese, L., Malatesta, F. & Barra, D. 1981. Purification and properties of bovine caeruloplasmin. Biochem. J., 199, 667–673
Caspi, D., Baltz, M. L., Snel, F., Gruys, E., Niv, D., Batt, R., Munn, E. A., Buttress, N. & Pepys, M. B. 1984. Isolation and characterisation of C-reactive protein from the dog. Immunology, 53, 307–313
Coles, E. H. 1986. Veterinary clinical pathology. (W. B. Saunders Co., Philadelphia), 22–23
Conner, J. G., Eckersall, P. D., Doherty, M. & Douglas, T. A. 1986a. Acute phase response and mastitis in the cow. Res. Vet. Sci., 41, 126–128
Conner, J. G., Eckersall, P. D. & Wiseman, A. 1986b. The acute phase response in the cow and dog. Prot. Biol. Fluids, 34, 509–512
Conner, J. G., Eckersall, P. D., Wiseman, A. & Douglas, T. A. 1988a. Bovine acute phase following turpentine injection. Res. Vet. Sci. 44, 82–88
Conner, J. G., Eckersall, P. D., Ferguson, J. & Douglas, T. A. 1988b. The acute phase response in the dog following surgical trauma. Res. Vet. Sci., (in press)
Deldar, A., Naylor, J. M. & Bloom, J. C. 1984. Effects of Escherichia coli on leukocyte and platelet counts, fibrinogen concentrations, and blood clotting in colostrum-fed and colostrum deficient neonatal calves. Am. J. Vet. Res., 45, 670–677
Dillman, R. C. & Coles, E. H. 1966. A canine serum fraction analagous to human C-reactive protein. Am. J. Vet. Res., 27, 1769–1775
Dobryszycka, W., Elwyn, D. H. & Kurral, J. C. 1969. Isolation and chemical composition of canine haptoglobin. Biochim. Biophys. Acta., 175, 220–222
Dooley, D. M., Cote, C. E., Coolbaugh, T. S. & Jenkins, P. L. 1981. Characterization of bovine ceruloplasmin. FEBS Letters, 131, 363–365
Eckersall, P. D., Sullivan, M., Kirkham, D. & Mohammed, N. A. 1985. The acute phase response detected in dogs by conacanavalin A binding. Vet. Res. Comm., 9, 233–238
Goodger, B. V. 1972. Preliminary characterization of the bovine polymeric Hb binding protein and comparison of some properties with human haptoglobins. Aust. J. Exp. Biol. Med. Sci., 50, 11–20
Gordon, A. H. & Koj, A. 1985. The acute phase response to injury and infection. The roles of interleukin 1 and other mediators. Elsevier, Amsterdam
Hol, P. R. & Gruys, E. 1984. Amyloid A proteins in different species. Appl. Pathol., 2, 316–327
Honkanen-Buzalski, T., Katila, T. & Sandholm, M. 1981. Milk α1-antitrypsin activity during clinical and experimental bovine mastitis. Acta. Vet. Scand., 22, 360–368
Honkanen-Buzalski, T. & Sandholm, M. 1981. Trypsin-inhibitors in mastitic milk and colostrum: correlation between trypsin-inhibitor capacity, bovine serum albumin and somatic cell contents. J. Dairy Sci., 48, 213–223
Jacobsson, K. 1955. Studies on the trypsin and plasmin inhibitors in human blood serum. Scand. J. Clin. Lab. Invest. Suppl. 14, 55–102
Kaplan, M. H. & Volanakis, J. E. 1974. Interaction of C-reactive protein complexes with the complement system. I. Consumption of human complement associated with the reaction of C-reactive protein with pneumococcal C-polysaccaride and the choline phosphatides lecithin and sphingomyelin. J. Immunol., 112, 2135–2147
Kohn, J., Hernandez, M. & Riches, P. G. 1978. The value of acute phase reactants in the management of disease. La Ricera, Clin. Lab., 8 (Suppl 1), 61–70
Kohn, J., Whicher, J., Warren, C. & O'Kelly, T. 1980. The use of lectins to measure acute phase proteins in the serum or plasma of man and animals during inflammation and tissue breakdown. FEBS Letters, 109, 257–260
Koj, A. 1974. Acute phase reactants. Their synthesis, turnover and biological significance. In: A. C.Allison, (ed) Structure and function of plasma proteins Vol. I. (Plenum Press, London). 73–131
Laurell, C-B. 1985. Actue phase proteins—a group of protective proteins. Recent Advances in Clinical Biochemistry, 103–124
Liberg, P. 1977. Agarose gel electrophoretic fractionation of serum proteins in adult cattle. Acta. Vet. Scand., 18, 335–348
Liang, C. C. 1957. The formation of complexes between haemoglobins and plasma proteins in a variety of animals. Biochem. J., 66, 552–558
Mattila, T., Saari, S. Vartiala, H. & Sandholm, M. 1984. Milk antitrypsin as a marker of bovine mastitis—correlation with bacteriology. J. Dairy Sci., 68, 114–122
Maudsley, S. 1985. Phylogenetic studies of the C-reactive protein family. (PhD Thesis, University of London)
McSherry, B. J., Horney, F. D. & deGroot, J. J. 1970. Plasma fibrinogen levels in normal and sick cows. Can. J. Comp. Med., 34, 191–197
Makimura, S. & Suzuki, N. 1982. Quantitative determination of bovine serum haptoglobin and its elevation in some inflammatory diseases. Jpn. J. Vet. Sci., 44, 15–21
Minocherri, F. 1965. Aspetto genetico delle aptoglobine di alcune specie animali. Arch. Vet. Ital., 16, 433–447
Neuhaus, O. W. & Sogoian, V. P. 1961. The presence of haptoglobin in synovial fluid. Nature, 192, 558–559
Panndorf, H., Richter, H. & Dittrich, B. 1976. Haptoglobin bei Haussaugetieren V. Arch. Exper. Vet. Med., 30, 193–202
Peeters, H. 1986. Acute phase response. Protides of the biological fluids, 34, 223–690
Pepys, M. B. 1981. C-reactive protein fifty years on Lancet, 1, 653–657
Piercy, D. W. T. 1979. Acute phase responses to experimental Salmonellosis in calves and Colibacillosis in chickens: serum iron and ceruloplasmin. J. Comp. Path., 89, 309–319
Polonovski, M. & Jayle, F. M. 1940. Preparation of a new fraction of the plasma proteins, haptoglobin. C. R. Acad. Sci., 211, 517–519
Richter, H. 1974. Haptoglobin bei haussaugetieren III. Arch. Exper. Vet. Med., 28, 505–519
Richter, H. 1975. Haptoglobin bei haussaugetieren IV. Arch. Exper. Vet. Med., 29, 217–230
Riley, R. F. & Coleman, M. K. 1970. Isolation of C-reactive proteins of man, monkey, rabbit and dog by affinity chromatography on phosphorylated cellulose. Clin. Chim. Acta., 30, 483–496
Riley, R. F. & Zontine, W. 1972. Further observation on the properties of dog C-reactive protein and the C-reactive protein response in the dog. J. Lab. Clin. Med., 80, 698–703
Robey, F. A., Jones, K. D. & Steinberg, A. D. 1985. C-Reactive protein mediates the solubilization of nuclear DNA by complement in vitro. J. Exper. Med., 161, 1344–1356
Sandholm, M., Honkanen-Buzalski, T. & Kangasniemi, R. 1984. Milk trypsin-inhibitor capacity as an indicator of bovine mastitis—a novel principle which can be automated. J. Dairy Res., 51, 1–9
Schultze, H. E., Gollner, I., Heide, K., Schonenberger, M. & Schwick, G. 1955. Zur kenntnis der globuline des menschlichen normalserum. Z. Naturforsch., B: Anorg. Chem. Org. Chem., Biochem., Biophys. Biol., 10B, 463
Shim, B-S., Yoon, C-S., Oh, S-K., Lee, T-H. & Kang, Y-S. 1971. Studies on swine and canine serum haptoglobins. Biochim. Biophys. Acta., 243, 126–136
Spooner, R. L. 1973. Haemoglobin reactive protein in cattle: partial characterisation. Res. Vet. Sci., 14, 90–96
Spooner, R. L. & Millar, J. K. 1971. The measurement of haemoglobin reactive protein as an aid to the diagnosis of acute inflammation. Vet. Rec., 88, 2–4
Sutton, R. H. & Hobman, B. 1975. The value of plasma fibrinogen estimations in cattle: a comparison with total leucocyte and neutrophil counts. N. Z. Vet. J., 23, 21–27
Sutton, R. H. & Johnson, M. 1977. The value of plasma fibrinogen estimations in dogs. A comparison with total leucocyte and neutrophil counts. J. Small Anim. Pract., 18, 277–281
Tillet, W. S. & Francis, T. 1930. Serological reactions in pneumonia with non-protein somatic fraction of pneumococcus. J. Exper. Med., 52, 561–571
Travis, J. & Johnson, D. 1981. Human α1-proteinase inhibitor. Met. in Enzym., 80, 754–765
Travis, J. C. & Sanders, R. G. 1972. Haptoglobin evolution: polymeric forms of HP in the bovidae and cervidae. J. Exp. Zool., 180, 141–148
Volanakis, J. E. & Kaplan, M. H. 1971. Specificity of C-reactive protein for choline phosphate residues of pneumococcal C-polysaccaride. Proc. Soc. Exp. Biol. Med., 236, 612–618
Westermark, P., Johnson, K. H., Sletten, K. & Hayden, D. W. 1985. AA-amyloidosis in dogs: Partial amino acid sequence of protein AA and immunohistochemical cross-reactivity with human and cow. Comp. Biochem. Physiol., 82B, 211–215
Westermark, P., Johnson, K. H., Westermark, G. T., Sletten, K. & Hayden, D. W. 1986. Bovine amyloid protein AA: Isolation and amino acid sequence analysis. Comp. Biochem. Physiol., 85B, 609–614
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Eckersall, P.D., Conner, J.G. Bovine and canine acute phase proteins. Veterinary Research Communications 12, 169–178 (1988). https://doi.org/10.1007/BF00362798
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DOI: https://doi.org/10.1007/BF00362798