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Vol. 10, Issue 2, 259-270, February 1999
3
1 Integrin, and Mitogen-activated Protein
Kinase Can Regulate Epithelial Cell Proliferation
and
Departments of
*Cell and Molecular Biology and
Laminin-5 (LN5) is a matrix component of epithelial tissue
basement membranes and plays an important role in the initiation and
maintenance of epithelial cell anchorage to the underlying connective
tissue. Here we show that two distinct LN5 function-inhibitory antibodies, both of which bind the globular domain of the Medicine, Northwestern University Medical School,
Chicago, Illinois 60611; and
Desmos Inc., San Diego, CA
92121
3 subunit, inhibit proliferation of epithelial cells. These same antibodies also
induce a decrease in mitogen-activated protein kinase activity. Inhibition of proliferation by the function-perturbing LN5 antibodies is reversed upon removal of the antibodies and can be overcome by
providing the antibody-treated cells with exogenous LN5 and rat tail
collagen. Because epithelial cells use the integrin receptor 3
1 to interact with both LN5 and rat tail collagen, we next investigated the possibility that integrin 31 is involved
in mediating the proliferative impact of LN5. Proliferation of human epithelial cells is significantly inhibited by a function-perturbing 3 integrin antibody. In addition, antibody activation of
1 integrin restores the proliferation of epithelial cells
treated with LN5 function-perturbing antibodies. These data indicate
that a complex comprising LN5 and 31 integrin is
multifunctional and contributes not only to epithelial cell adhesion
but also to the regulation of cell growth via a signaling pathway
involving mitogen-activated protein kinase. We discuss our study
in light of recent evidence that LN5 expression is up-regulated at the
leading tips of tumors, where it may play a role in tumor cell proliferation.
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