Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-28T06:02:16.095Z Has data issue: false hasContentIssue false

Distribution of plasminogen activator in different fractions of bovine milk

Published online by Cambridge University Press:  01 June 2009

Jeffrey H. White
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05405, USA
Boris Zavizion
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05405, USA
Kristen O'Hare
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05405, USA
James Gilmore
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05405, USA
Ming R. Guo
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05405, USA
Paul Kindstedt
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05405, USA
Ioannis Politis
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05405, USA

Summary

The type and relative amounts of plasminogen activator (PA) in different fractions of bovine milk obtained from 15 Holstein cows were examined. Raw milk was centrifuged to separate skim milk and a somatic cell pellet. PA was mainly localized within the casein fraction, being 42 times that in the serum, and in association with somatic cells. The predominant form of PA in milk casein was isolated from SDS-PAGE gel extracts and had a molecular mass of ∽75 kDa. Its activity was increased 41-fold (P < 0·01) in the presence of fibrin but was unaffected by the presence of amiloride, indicating that it was due to tissue-PA. The predominant forms of PA associated with milk somatic cells were isolated from SDS-PAGE gel extracts and had molecular masses of ∽ 30 and ∽ 50 kDa. The activity of both proteins was unaffected by the presence of fibrin but was dramatically reduced by the presence of amiloride, indicating that they represented urokinase-PA.

Type
Original articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1995

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Andrews, A. T. 1983 Proteinases in normal bovine milk and their action on caseins. Journal of Dairy Research 50 4555.CrossRefGoogle ScholarPubMed
Baldi, A., Politis, I., Bakbano, D. M. & Gorewit, R. C. 1993 Primary characterization and determination of plasminogen activator in bovine milk. Journal of Dairy Science 76 Suppl. 1 92 (Abstr.).Google Scholar
Heegard, C. W., Christensen, T. & Andreasen, P. A. 1993 t-PA binds to casein micelles in bovine milk. Proceedings of Molecular and Cellular Biology of Plasminogen Activation, p. 64Google Scholar
Heegard, C. W., Christensen, T., Rasmussen, M. D., Benfeldt, C., Jensen, N. J., Sejrsen, K., Petersen, T. E. & Andreasen, P. A. 1994 Plasminogen activators in bovine milk during mastitis, an inflammatory disease. Fibrinolysis 8 2230CrossRefGoogle Scholar
Korycka-Dahl, M., Ribadeau Dumas, B., Chene, N. & Martal, J. 1983 Plasmin activity in milk. Journal of Dairy Science 66 704711CrossRefGoogle Scholar
Kristensen, P., Larsson, L. -I, Nielsen, L. S., Grøndahl-Hansen, J., Andreasen, P. A. & Dano, K. 1984 Human endothelial cells contain one type of plasminogen activator. FEBS Letters 168 3337CrossRefGoogle ScholarPubMed
Lu, D. D. & Nielsen, S. S. 1993 Isolation and characterization of native bovine milk plasminogen activators. Journal of Dairy Science 76 33693383CrossRefGoogle Scholar
Markus, G., Hitt, S., Harvey, S. R. & Trisch, G. L. 1993 Casein, a powerful enhancer of the rate of plasminogen activation. Fibrinolysis 7 229236CrossRefGoogle Scholar
Politis, I., Lachancb, E., Block, E. & Turner, J. D. 1989 a Plasmin and plasminogen in bovine milk: a relationship with involution ? Journal of Dairy Science 72 900906CrossRefGoogle ScholarPubMed
Politis, I., Ng Kwai Hang, K. F. & Giroux, R. N. 1989 b Environmental factors affecting plasmin activity in milk. Journal of Dairy Science 72 17131718CrossRefGoogle ScholarPubMed
Politis, I., Zhao, X., Mcbridb, B. W., Burton, J. H. & Turner, J. D. 1991 Plasminogen activator production by bovine milk macrophages and blood monocytes. American Journal of Veterinary Research 52 12081213CrossRefGoogle ScholarPubMed
Saksela, O. 1985 Plasminogen activation and regulation of pericellular proteolysis. Biochimica el Biophysica Acta 823 3565Google ScholarPubMed
Schaar, J. & Funke, H. 1986 Effect of subclinical mastitis on milk plasminogen and plasmin compared with that on sodium, antitrypsin and N-aeety-β-D-glueosaminidase. Journal of Dairy Research 53 515528CrossRefGoogle Scholar
Vassali, J. -D. & Belin, D. 1987 Amiloride selectively inhibits the urokinase-type plasminogen activator. FEBS Letters 214 187191CrossRefGoogle Scholar
Zachos, T., Politis, I., Gorewit, R. C. & Barbano, D. M. 1992 Effect of mastitis on plasminogen activator activity of milk somatic cells. Journal of Dairy Research 59 461467CrossRefGoogle ScholarPubMed
Zammaron, C., Lijnen, H. R. & Collen, D. 1984 Kinetics of the activation of plasminogen by natural and recombinant tissue-type plasminogen activator. Journal of Biological Chemistry 259 20802083CrossRefGoogle Scholar