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The receptor for urokinase-type plasminogen activator and urokinase is
translocated from two distinct intracellular compartments to the plasma
membrane on stimulation of human neutrophils
T Plesner, M Ploug, V Ellis, E Ronne, G Hoyer-Hansen, M Wittrup, TL Pedersen, T Tscherning, K Dano and NE Hansen
Department of Medicine and Hematology L, Herlev Hospital, Herlev, Denmark.
The cellular receptor for urokinase-type plasminogen activator (uPAR) binds
pro-urokinase (pro-uPA) and facilitates its conversion to enzymatically
active urokinase (uPA). uPA in turn activates surface- bound plasminogen to
plasmin, a process of presumed importance for a number of biologic
processes including cell migration and resolution of thrombi. We have
previously shown that uPAR is expressed on the plasma membrane of
circulating neutrophils, and we now report that stimulation with phorbol
myristate acetate (PMA), FMLP, or tumor necrosis factor- alpha results in a
rapid increase in the expression of uPAR. This process is accompanied by an
increased cell-associated plasminogen activation after preincubation of
neutrophils with pro-uPA in vitro. By subcellular fractionation of
unstimulated neutrophils, 50% of uPAR is recovered in fractions containing
latent alkaline phosphatase, corresponding to an intracellular compartment
of easily mobilizable secretory vesicles distinct from both primary and
specific granules, whereas the remaining 50% of uPAR is associated with a
compartment eluting close to the specific granules. In contrast, the ligand
pro-uPA is primarily (approximately 80%) found in the specific granules,
but small amounts of pro-uPA/uPA (approximately 20%) coelute with latent
alkaline phosphatase. Stimulation of neutrophils with FMLP results in
translocation of uPAR as well as of pro-uPA from the secretory vesicles,
whereas stimulation with PMA is required to translocate material from
specific granules. Flow cytometry of neutrophils saturated with exogenous
diisopropyl fluorophosphate-uPA shows a large excess (approximately 90%) of
unoccupied uPAR on resting as well as FMLP- and PMA-stimulated neutrophils,
suggesting a possible role for exogenous pro-uPA in providing neutrophils
with a potential for plasminogen activation. These processes may be
important for neutrophil extravasation and migration through extracellular
matrix and for the contribution of neutrophils to resolution of thrombi.
Volume 83,
Issue 3,
pp. 808-815,
02/01/1994
Copyright © 1994 by The American Society of Hematology
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