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Institute for Cancer Research and Treatment, University of Torino Medical School, 10060 Candiolo-Torino, Italy
1Correspondence: Division of Molecular Oncology, Institute for Cancer Research, Str. Provinciale 142, 10060 Candiolo (Torino), Italy. E-mail: cboccaccio{at}ircc.unito.it
Hepatocyte growth factor/scatter factor (HGF/SF) controls a genetic program known as ‘invasive growth’, which involves as critical steps cell adhesion, migration, and trespassing of basement membranes. We show here that in MDA-MB-231 carcinoma cells, these steps are elicited by HGF/SF but not by epidermal growth factor (EGF). Neither factor substantially alters the production or activity of extracellular matrix proteases. HGF/SF, but not EGF, selectively promotes cell adhesion on laminins 1 and 5, fibronectin, and vitronectin through a PI3-K-dependent mechanism. Increased adhesion is followed by enhanced invasiveness through isolated matrix proteins as well as through reconstituted basement membranes. Inhibition assays using function-blocking antibodies show that this phenomenon is mediated by multiple integrins including ß1, ß3, ß4, and ß5. HGF/SF triggers clustering of all these integrins at actin-rich adhesive sites and lamellipodia but does not quantitatively modify their membrane expression. These data suggest that HGF/SF promotes cell adhesion and invasiveness by increasing the avidity of integrins for their specific ligands.—Trusolino, L., Cavassa, S., Angelini, P., Andò, M., Bertotti, A., Comoglio, P. M., Boccaccio, C. HGF/scatter factor selectively promotes cell invasion by increasing integrin avidity.
Key Words: growth factors • tyrosine kinase receptors • MET • adhesion • integrin activation
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