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(Received for publication, September 1, 1994)
Platelet integrin 
(GPIIb-IIIa) plays important roles in platelet-mediated clot
retraction. However, little is known about the mechanisms of clot
retraction mediated by nucleated cells. In this report, we demonstrate
that another member of the integrin family,
, is involved in clot retraction
mediated by nucleated cells. Retraction of fibrin clots was observed
using a human melanoma cell line, C32TG, which contains no
complex. This retraction was
inhibited by RGD-containing peptide, monoclonal anti-,
and anti- antibodies. Immunoelectron
microscopic studies revealed a direct interaction between integrin and fibrin fibers at an early stage of clot retraction.
We found that another human embryonal cell line, 293, which is known to
express 
, but no
, lacks fibrin gel retractile
activity. Upon transfection of DNA into 293 cells,
the subunit formed a complex with an endogenous
subunit. The -bearing transfectants
were found to retract fibrin gels, which was specifically inhibited by
anti- antibody. In addition, a point mutation at
Asp in the
ligand binding domain
abolished the clot retractile activity of 293 transfectants, indicating
the requirement of ligand-binding
activity. Our findings suggest that is involved in mediating the interaction between the
three-dimensional fibrin network and nucleated cells and in promoting
``post-receptor occupancy'' events.
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