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Protease nexin 1 is expressed in the human placenta
E A White1, J B Baker, M McGrogan
1Department of Biochemistry, University of Kansas, Lawerence 66045.
Thrombosis and Haemostasis
|February 1, 1993
Summary
Protease nexin 1 (PN1) is synthesized in human placentas, particularly in placental membranes. This study identifies the placenta as a key site for PN1 production in vivo.
Area of Science:
- Biochemistry
- Molecular Biology
- Reproductive Biology
Background:
- Protease nexin 1 (PN1) is a serine protease inhibitor.
- PN1 inactivates thrombin, urokinase, and plasmin.
- PN1 is abundant in fibroblast and glioma cell cultures, but its in vivo synthesis sites and functions are unknown.
Purpose of the Study:
- To investigate the in vivo synthesis sites of PN1.
- To determine the physiological role of PN1 in the human placenta.
Main Methods:
- Northern blot analysis using a full-length PN1 cDNA probe.
- In situ hybridization with a PN1 riboprobe.
- Immunohistochemical analysis with an anti-PN1 antibody.
Main Results:
- PN1 mRNA was detected in human term placentas.
- PN1 mRNA was found throughout the placenta and abundant in placental membranes.
- PN1 protein and mRNA co-localized within the placenta.
Conclusions:
- The human placenta is a significant site of PN1 synthesis in vivo.
- PN1 is present in both the placenta and placental membranes.
- Further research is needed to elucidate the physiological functions of PN1 in pregnancy.
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