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Synthesis of plasminogen activator inhibitor 1 by bovine mammary epithelial and myoepithelial cell lines

Published online by Cambridge University Press:  01 June 2009

Boris Zavizion
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05404, USA
Christian W. Heegard
Affiliation:
Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus C, Denmark
Jeffrey White
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05404, USA
Federica Cheli
Affiliation:
Istituto di Nutrizione Animale, Università degli Studi di Milano, I-20133 Milano, Italia
Ioannis Politis
Affiliation:
Department of Animal and Food Sciences, University of Vermont, Burlington, VT 05404, USA

Summary

Conversion of plasminogen to plasmin provides an important source of proteolytic activity in the bovine mammary gland. Plasminogen activator inhibitor 1 (PAI-1) plays a key role in limiting plasminogen activation. The PAI-1 biosynthetic capabilities of various bovine mammary cells were determined. The immortalized epithelial cell lines MAC-T and BME-UV and the myoepithelial cell line BMM-UV were used as model systems. Northern blot analysis indicated that both epithelial and myoepithelial cells contained PAI-1 mRNA. Bovine PAI-1 was encoded by a single mRNA species ∼ 3·0 kb long. BME-UV cells contained 2·0-fold (P < 0·01) the PAI-1 mRNA of MAC-T or BMM-UV cells. Reverse zymography indicated that both epithelial and myoepithelial cells synthesized PAI-1 protein with a molecular mass of ∼ 50 kDa.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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References

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