Thromb Haemost 1993; 69(02): 119-123
DOI: 10.1055/s-0038-1651566
Original Article
Coagulation
Schattauer GmbH Stuttgart

Protease Nexin 1 Is Expressed in the Human Placenta

Elizabeth A White
The Department of Biochemistry, The University of Kansas, Lawrence, Kansas, USA
,
Joffre B Baker
,
Michael McGrogan
,
Paul A Kitos
The Department of Biochemistry, The University of Kansas, Lawrence, Kansas, USA
› Institutsangaben
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Publikationsverlauf

Received 08. Januar 1992

Accepted after revision 25. September 1992

Publikationsdatum:
03. Juli 2018 (online)

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Summary

Protease nexin 1 (PN1), a serine protease inhibitor that inactivates thrombin, urokinase, and plasmin, is produced abundantly in cultures of human fibroblasts and rat and human glioma cells. The major sites of PN1 synthesis in vivo and the specific physiological function(s) of this serpin are unknown. Using Northern blot analysis and a full-length PN1 cDNA probe we demonstrated the presence of PN1 mRNA in human term placentas. In situ hybridization of placental tissue with a PN1 riboprobe showed that PN1 mRNA is present throughout the placenta and is also abundant in the placental membranes. Immunohistochemical analysis with an anti-PN1 antibody showed co-localization of PN1 and its mRNA within the placenta.