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Vol. 12, Issue 9, 2699-2710, September 2001
v
3
and Cell Adhesion Molecule L1 in Transendothelial Migration of Melanoma
Cells
and
*Banting and Best Department of Medical Research and Department of
Biochemistry University of Toronto, Toronto, Ontario, Canada M5G 1L6;
and Tumor metastasis involves many stage-specific adhesive
interactions. The expression of several cell adhesion molecules,
notably the integrin Department of Pediatrics, University of California at
San Diego, La Jolla, California 92037
v
3, has been
associated with the metastatic potential of tumor cells. In this study,
we used a novel in vitro assay to examine the role of
v3 in the transmigration of melanoma cells through a monolayer of human lung microvascular endothelial cells. Confocal microscopy revealed the presence of the
integrin v3 on melanoma membrane
protrusions and pseudopods penetrating the endothelial junction.
v3 was also enriched in heterotypic contacts between endothelial cells and melanoma cells. Transendothelial migration of melanoma cells was inhibited by either a cyclic
Arg-Gly-Asp peptide or the anti-v3
monoclonal antibody LM609. Although both platelet endothelial
cell adhesion molecule-1 and L1 are known to bind integrin
v3, only L1 serves as a potential ligand
for v3 during melanoma transendothelial
migration. Also, polyclonal antibodies against L1 partially inhibited
the transendothelial migration of melanoma cells. However, addition of
both L1 and v3 antibodies did not show
additive effects, suggesting that they are components of the same
adhesion system. Together, the data suggest that interactions between
the integrin v3 on melanoma cells
and L1 on endothelial cells play an important role in the transendothelial migration of melanoma cells.
Corresponding author. E-mail
address: chi.hung.siu{at}utoronto.ca.
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