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Characterization of urokinase receptor expression by human placental
trophoblasts
JM Zini, SC Murray, CH Graham, PK Lala, K Kariko, ES Barnathan, A Mazar, J Henkin, DB Cines and KR McCrae
Department of Medicine, University of Pennsylvania School of Medicine,
Philadelphia.
The processes of implantation and placentation are both dependent on the
invasion and remodeling of the uterine endometrium and vasculature by
trophoblasts. Because the secretion and autocrine binding of urokinase
(uPA) appears to be a common mechanism used by cells to facilitate
plasmin-dependent tissue invasion, we measured the production of uPA and
expression of uPA receptors by trophoblasts. Prourokinase bound
specifically, reversibly, and with high affinity to cultured trophoblasts,
via the uPA epidermal growth factor-like domain. Trophoblasts derived from
two first-trimester placentae bound more prourokinase than cells isolated
from term placentae. Furthermore, in vitro differentiation of cultured
cytotrophoblasts into syncytiotrophoblasts was associated with diminished
expression of urokinase receptors and a parallel decrease in the cellular
content of uPA receptor mRNA. Trophoblasts also secreted prourokinase and
plasminogen activator inhibitors types 1 and 2 (PAI-1 and PAI-2). Although
prourokinase was secreted in amounts sufficient to endogenously saturate
trophoblast uPA receptors, trophoblasts secreted greater amounts of PAI-1
and PAI-2 than uPA, and no net plasminogen activator activity was detected
in trophoblast conditioned medium. In contrast, plasminogen added directly
to cultured trophoblasts was readily converted to plasmin. Although the
invasion and remodeling of uterine tissues by trophoblasts is a complex
process dependent on several proteases of varying specificity, our findings
suggest that the expression and modulation of urokinase receptors on the
trophoblast cell surface may play an important role in this process.
Volume 79,
Issue 11,
pp. 2917-2929,
06/01/1992
Copyright © 1992 by The American Society of Hematology
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