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(Received for publication, April 27, 1996, and in revised form, August 30, 1996)
From The urokinase plasminogen activator (uPA)
interacts with its cell surface receptor (uPAR), providing an
inducible, localized cell surface proteolytic activity, thereby
promoting cellular invasion. Evidence is provided for a novel function
of cell surface-associated uPA·uPAR. Specifically, induction of cell
surface expression of uPA·uPAR by growth factors or phorbol ester was
necessary for vitronectin-dependent carcinoma cell
migration, an event mediated by integrin
Volume 271, Number 46,
Issue of November 15, 1996
pp. 29393-29399
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
v
5-directed Cell Migration
,
,
The Scripps Research Institute, Departments of
Immunology and Vascular Biology, IMM24, La Jolla, California 92037 and
¶ Chiron Corporation, Emeryville, California 94608
v
5. Cell migration on
vitronectin was blocked with either a soluble form of uPAR, an antibody
that disrupts uPA binding to uPAR, or a monoclonal antibody to
v5. Moreover, plasminogen activator inhibitor type 2 blocked this
migration event but did not affect adhesion, suggesting a direct role
for uPA enzyme activity in this process and that migration but not
adhesion of these cells is regulated by uPA·uPAR. Growth
factor-mediated induction of uPA·uPAR on the carcinoma cell surface
promotes a specific motility event mediated by integrin v5, since
cells transfected with the 3 integrin subunit expressed v3 and
migrated on vitronectin independently of growth factors or uPA·uPAR
expression. This relationship between v5 and the uPA·uPAR
system has significant implications for regulation of motility events
associated with development, angiogenesis, and tumor
metastasis.
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