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Vol. 11, Issue 1, 51-64, January 2000
*The Beatson Institute for Cancer Research, CRC Beatson
Laboratories, Glasgow G61 1BD, United Kingdom; and
Despite the importance of epithelial cell contacts in determining
cell behavior, we still lack a detailed understanding of the assembly
and disassembly of intercellular contacts. Here we examined the role of
the catalytic activity of the Src family kinases at epithelial cell
contacts in vitro. Like E- and P-cadherin, Ca2+ treatment
of normal and tumor-derived human keratinocytes resulted in c-Yes (and
c-Src and Fyn), as well as their putative substrate p120CTN, being recruited to cell-cell contacts. A tyrosine
kinase inhibitor with selectivity against the Src family kinases,
PD162531, and a dominant-inhibitory c-Src protein that interferes with
the catalytic function of the endogenous Src kinases induced cell-cell
contact and E-cadherin redistribution, even in low Ca2+,
which does not normally support stable cell-cell adhesion. Time-lapse microscopy demonstrated that Src kinase inhibition induced
stabilization of transiently formed intercellular contacts in low
Ca2+. Furthermore, a combination of E- and
P-cadherin-specific antibodies suppressed cell-cell contact,
indicating cadherin involvement. As a consequence of contact
stabilization, normal cells were unable to dissociate from an
epithelial sheet formed at high density and repair a wound in vitro,
although individual cells were still motile. Thus, cadherin-dependent
contacts can be stabilized both by high Ca2+ and by
inhibiting Src activity in low (0.03 mM) Ca2+ in vitro.
Department of Pathology and Microbiology, University of
Bristol, School of Medical Sciences, Bristol BS8 1TD, United Kingdom
These authors contributed equally to this work.
§
Corresponding author. E-mail address:
m.frame{at}beatson.gla.ac.uk.
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