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Vol. 11, Issue 7, 2485-2496, July 2000
5/
1 Mediates Fibronectin-dependent
Epithelial Cell Proliferation through Epidermal Growth Factor Receptor
Activation
Division of Gastroenterology, University of Utah and Salt Lake City
Veterans Affairs Medical Center, Salt Lake City, Utah 84132
Human integrin 
5 was transfected into the
integrin 5/
1-negative intestinal epithelial cell line
Caco-2 to study EGF receptor (EGFR) and integrin 5/1
signaling interactions involved in epithelial cell proliferation. On
uncoated or fibronectin-coated plastic, the integrin 5 and
control (vector only) transfectants grew at similar rates. In the
presence of the EGFR antagonistic mAb 225, the integrin 5
transfectants and controls were significantly growth inhibited on
plastic. However, when cultured on fibronectin, the integrin
5 transfectants were not growth inhibited by mAb 225. The reversal
of mAb 225-mediated growth inhibition on fibronectin for the integrin
5 transfectants correlated with activation of the EGFR, activation
of MAPK, and expression of proliferating cell nuclear antigen. EGFR
kinase activity was necessary for both MAPK activation and
integrin 5/1-mediated cell proliferation. Although EGFR
activation occurred when either the integrin 5-transfected or control cells were cultured on fibronectin, coprecipitation of the
EGFR with SHC could be demonstrated only in the integrin 5-transfected cells. These results suggest that integrin
5/1 mediates fibronectin-induced epithelial cell proliferation
through activation of the EGFR.
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