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Regular Article |
From the Departments of Laboratory Medicine and
Pathology,*
Medicine,
and
Orthopaedic Surgery,
University of Minnesota,
Minneapolis, Minnesota
Ovarian carcinoma multicellular spheroids are an in
vitro model of micrometastasis whose adhesive abilities have
not been elucidated. In this study, we identified adhesion
molecules that mediate the formation of ovarian carcinoma spheroids and
their subsequent adhesion to extracellular matrix proteins. The
NIH:OVCAR5, but not the SKOV3, ovarian carcinoma cell
line formed spheroids similar to multicellular aggregates isolated from
patient ascitic fluid. NIH:OVCAR5 spheroid formation was augmented by a
ß1-integrin-stimulating monoclonal antibody or exogenous
fibronectin, but was inhibited by blocking monoclonal
antibodies against the 
5- or ß1-integrin subunits. By
immunohistochemical staining, 2-, 3-,
5-, 6-, and ß1-integrin subunits,
CD44, and fibronectin were detected in NIH:OVCAR5 spheroids.
NIH:OVCAR5 spheroids adhered to fibronectin, laminin,
and type IV collagen, and this adhesion was partially inhibited
by blocking antibodies against the 5-, 6-, and
2-integrin subunits, respectively. A blocking monoclonal
antibody against the ß1-integrin subunit completely inhibited
adhesion of the spheroids to all three proteins. These results suggest
that interactions between the 5ß1-integrin and fibronectin mediate
the formation of ovarian carcinoma spheroids and that their adhesion to
extracellular matrix proteins at sites of secondary tumor growth may be
mediated by a complex interaction between multiple integrins and their
ligands.
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