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Effect of subclinical mastitis on milk plasminogen and plasmin compared with that on sodium, antitrypsin and N-acetyl-β-D-glucosaminidase

Published online by Cambridge University Press:  01 June 2009

Johan Schaar  and
Hans Funke
Johan Schaar
Affiliation:
Department of Animal Breeding and Genetics, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden
Hans Funke
Affiliation:
Swedish Association for Livestock Breeding and Production, S-631 84 Eskilstuna, Sweden
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Summary

The effect of subclinical mastitis on levels of plasminogen and plasmin in milk from cows in a high-yielding herd was investigated. Comparisons were made with levels of milk Na, antitrypsin and N-acetyl-β-D-glucosaminidase (NAGase). In samples from mastitic quarters plasminogen activity, as measured after activation to plasmin, increased by only 21% and plasmin by 82%, while NAGase increased by 307 %. Plasminogen was the only component that was normally distributed, all other components showed more or less skewed distributions. Plasmin and plasminogen were significantly related to the other components. However, plasminogen plateaued when the other components continued to increase. There was thus no further increase in plasminogen with the severity of inflammation as with the other components. Plasmin showed a similar although less pronounced tendency. Results of treatment of mastitic whey samples with acid suggested that the non-linear increase in plasmin activity was due to interaction with acid-labile proteinase inhibitors. Mastitis led to dissociation of plasminogen and plasmin from the casein micelles. The degree of activation of plasminogen was higher with casein-associated than with soluble plasminogen in both healthy and mastitic milks. Plasmin was very closely related to milk Na, which is a sensitive indicator of epithelial integrity. It is suggested that plasmin contributes to Na leakage into milk by degrading membrane proteins of the epithelial lining. Plasminogen and antitrypsin, which are both plasma proteins, were not identically affected by stage of lactation, indicating nonidentical modes of transport from plasma to milk.

Type
Original Articles
Information
Journal of Dairy Research , Volume 53 , Issue 4 , November 1986 , pp. 515 - 528
Copyright
Copyright © Proprietors of Journal of Dairy Research 1986

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References

REFERENCES

Andrews, A. T. 1983 Breakdown of caseins by proteinases in bovine milks with high somatic cell counts arising from mastitis or infusion with bacterial endotoxin. Journal of Dairy Research 50 57–66CrossRefGoogle ScholarPubMed
Barrett, A. J. & Starkey, P. M. 1973 The interaction of α2-macroglobulin with proteinases. Biochemical Journal 133 709–724Google Scholar
Barry, J. G. & Donnelly, W. J. 1981 Casein compositional studies. II. The effect of secretory disturbance on casein composition in freshly drawn and aged bovine milks. Journal of Dairy Research 48 437–446Google Scholar
Beh, K. J., Watson, D. L. & Lascelles, A. K. 1974 Concentrations of immunoglobulins and albumin in lymph collected from various regions of the body of the sheep. Australian Journal of Experimental Biology and Medical Science 52 81–86Google Scholar
Bengtsson, B., Luthman, J. & Jacobsson, S. -O. 1984 Evaluation of a tissue cage model for use in cattle. Acta Veterinaria Scandinavica 25 480–494CrossRefGoogle ScholarPubMed
Berga, S. E. 1984 Electric potentials and cell-to-cell dye movement in mouse mammary gland during lactation. American Journal of Physiology 247 C20–C25Google Scholar
Berga, S. E. & Neville, M. C. 1985 Sodium and potassium distribution in the lactating mouse mammary gland in vivo. Journal of Physiology 361 219–230CrossRefGoogle ScholarPubMed
Chan, J. Y. S. & Mertz, E. T. 1966 Studies on plasminogen. VI. Activation products of bovine and human plasminogens. Canadian Journal of Biochemistry 44 487–495Google Scholar
Collen, D. 1980 On the regulation and control of fibrinolysis. Thrombosis & Haemostasis 43 77–89Google Scholar
Craven, N. 1983 Generation of neutrophil chemoattractants by phagocytosing bovine mammary macrophages. Research in Veterinary Science 35 310–317Google Scholar
De Koning, P. J., Kaper, J., Rollema, H. S. & Driessen, F. M. 1985 Age-thinning and gelation in unconcentrated and concentrated UHT-sterilized skim milk. Effect of native milk proteinase. Netherlands Milk and Dairy Journal 39 71–87Google Scholar
De Rham, O. & Andrews, A. T. 1982 Qualitative and quantitative determination of proteolysis in mastitic milks. Journal of Dairy Research 49 587 596Google Scholar
Dulin, A. M., Paape, M. J. & Capuco, A. V. 1985 Activity of N-acetyl-β-D-glucosaminidase in milk: contribution by milk somatic cells. Journal of Dairy Science 67 (Suppl. 1) 253Google Scholar
Electricwala, A. & Atkinson, T. 1985 Purification and properties of plasminogen activators from epithelial cells. European Journal of Biochemistry 147 511–516CrossRefGoogle ScholarPubMed
Ganrot, P. O., Laurell, C. -B. & Ohlsson, K. 1970 Concentration of trypsin inhibitors of different molecular size and of albumin and haptoglobin in blood and lymph of various organs in the dog. Acta Physiologica Scandinavica 79 280–286Google Scholar
Grieve, P. A. & Kitchen, B. J. 1985 Proteolysis in milk: the significance of proteinases originating from milk leucocytes and a comparison of the action of leucocyte, bacterial and natural milk proteinases on casein. Journal of Dairy Research 52 101–112Google Scholar
Guidry, A. J., Butler, J. E., Pearson, R. E. & Wbinland, B. T. 1980 IgA, IgG1, IgG2, IgM and BSA in serum and mammary secretion throughout lactation. Veterinary Immunology and Immunopatkology 1 329–341Google Scholar
Honkanen-Buzalski, T., Kangasniemi, R., Atroshi, F. & Sandholm, M. 1981 Effect of lactation stage and number on milk albumin (BSA) and somatic cell count. Zenlralblatt für Veterinärmedizin A 28 760–767Google Scholar
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. Journal of Dairy Research 48 213–223Google Scholar
Jones, P. A. & Werb, Z. 1980 Degradation of connective tissue matrices by macrophages. II. Influence of matrix composition on proteolysis of glycoproteins, elastin, and collagen by macrophages in culture. Journal of Experimental Medicine 152 1527–1536Google Scholar
Kitchen, B. J., Middleton, G. & Salmon, M. 1978 Bovine milk N-acetyl-β-D-glucosaminidase and its significance in the detection of abnormal udder secretions. Journal of Dairy Research 45 15–20Google Scholar
Klastrup, O. & Schmidt Madsen, P. 1974 Scandinavian recommendations concerning investigation of quarter samples for mastitis. Nordisk Veterinärmedicin 26 197–204Google Scholar
Korycka-Dahl, M., Ribadeau-Dumas, B., Chene, N. & Martal, J. 1983 Plasmin activity in milk. Journal of Dairy Science 66 704–711Google Scholar
Lämmle, B., Eichlisberger, R., Marbet, G. A. & Duckert, F. 1979 Amidolytic activity in normal human plasma assessed with chromogenic substrates. Thrombosis Research 16 245–254Google Scholar
Linzell, J. L. & Peaker, M. 1971 The effects of oxytocin and milk removal on milk secretion in the goat. Journal of Physiology 216 717–734CrossRefGoogle ScholarPubMed
Liotta, L. A., Goldfarb, R. H., Brundage, R., Siegal, G. P., Terranova, V. & Garbisa, S. 1981 Effect of plasminogen activator (urokinase), plasmin and thrombin on glycoprotein and collagenous components of basement membrane. Cancer Research 41 4629–4636Google Scholar
Magee, S. C., Geren, C. R. & Ebner, K. E. 1976 Plasmin and the conversion of the molecular forms of bovine milk galactosyltransferase. Biochimica et Biophysica Acta 420 187–194Google Scholar
Mattila, T. 1985 Diagnostic problems in bovine mastitis with special reference to new applications of milk antitrypsin, NAGase and bacterial growth. Thesis. Department of Pharmacology and Toxicology, College of Veterinary Medicine, Helsinki 55, Finland.Google Scholar
Müller, N. & Danckworth, H. -P. 1977 Coagulation factors and components of the fibrinolytic system in lymph and blood after cannulation and blockage resp. of the thoracic duct in dogs. Lymphology, Proceedings of the Vlth International Congress, Prague pp. 189–192Google Scholar
Mullins, D. E. & Rohrlich, S. T. 1983 The role of proteinases in cellular invasiveness. Biochimica et Biophysica Acta 695 177–214Google Scholar
Mussoni, L., Raczka, E., Chmielbwska, J., Donati, M. B. & Latallo, Z. S. 1979 Plasminogen assay in rabbit, rat and mouse plasma using the chromogenic substrate S-2251. Thrombosis Research 15 341–349Google Scholar
Phillippy, B. O. & McCarthy, R. D. 1979 Multi-origins of milk serum albumin in the lactating goat. Biochimica et Biophysica Acta 584 298–303Google Scholar
Pringnitz, D. J., Butler, J. E. & Guidry, A. J. 1985 Quantitation of bovine β2-microglobulin: occurrence in body fluids, on milk fat globules and origin in milk. Molecular Immunology 22 779–786Google Scholar
Reimerdes, E. -H., Klostermeyer, H. & Sayk, E. 1976 Milk proteinases. 7. Fractionation of components of the proteinase inhibitor system in milk. Milchwissenschaft 31 329–334Google Scholar
Richards, R. C. 1984 The use of trypsin to improve the localization of immunoglobulins in semi-thin frozen sections of the mammary gland. Histochemical Journal 16 565–572Google Scholar
Richardson, B. C. 1983 The proteinases of bovine milk and the effects of pasteurization on their activity. New Zealand Journal of Dairy Science and Technology 18 233–245Google Scholar
Richardson, B. C. & Pearce, K. N. 1981 The determination of plasmin in dairy products. New Zealand Journal of Dairy Science and Technology 16 209–220Google Scholar
Rollema, H. S., Visser, S. & Poll, J. K. 1983 Spectrophotometric assay of plasmin and plasminogen in bovine milk. Milchwissenschaft 38 214–217Google Scholar
Saksela, O., Hovi, T. & Vaheri, A. 1985 Urokinase-type plasminogen activator and its inhibitor secreted by cultured human monocyte-macrophages. Journal of Cellular Physiology 122 125–132Google Scholar
Salonen, E. -M., Zitting, A. & Vaheri, A. 1984 Laminin interacts with plasminogen and its tissue-type activator. FEBS Letters 172 29–32Google Scholar
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. Journal of Dairy Research 51 1–9Google Scholar
Sas Institute Inc. 1982 SAS User's Guide: Statistics. Cary, NC: SAS Institute IncGoogle Scholar
Schaar, J. 1985 Plasmin activity and proteose-peptone content of individual milks. Journal of Dairy Research 52 369–378Google Scholar
Sharma, K. K. & Randolph, H. E. 1974 Influence of mastitis on properties of milk. VIII. Distribution of soluble and micellar casein. Journal of Dairy Science 57 19–23Google Scholar
Sheldrake, R. F., Hoare, R. J. T. & McGregor, G. D. 1983 Lactation stage, parity, and infection affecting somatic cells, electrical conductivity, and serum albumin in milk. Journal of Dairy Science 66 542–547Google Scholar
Wiman, B., Mellbring, G. & Rånby, M. 1983 Plasminogen activator release during venous stasis and exercise as determined by a new specific assay. Clinica Acta 127 279–288Google Scholar