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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 ,
Christian W. Heegard ,
Jeffrey White ,
Federica Cheli  and
Ioannis Politis
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
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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
Information
Journal of Dairy Research , Volume 63 , Issue 3 , August 1996 , pp. 451 - 458
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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