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(Received for publication, November 25, 1996, and in revised form, February 28, 1997)
From the Department of Medical Biophysics, University of Toronto
and Cancer Biology Research, Sunnybrook Health Science Centre, Toronto,
Ontario M4N 3M5, Canada
Cell adhesion to substratum has been shown to
regulate cyclin A expression as well as cyclin D- and
E-dependent kinases, the latter via the up-regulation of
cyclin D1 and the down-regulation of cyclin-Cdk inhibitors p21 and p27,
respectively. This adhesion-dependent regulation of cell
cycle is thought to be mediated by integrins. Here we demonstrate that
stable transfection and overexpression of the
integrin-linked kinase (ILK), which
interacts with the
Volume 272, Number 21,
Issue of May 23, 1997
pp. 13937-13944
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
1 and 3 integrin cytoplasmic domains, induces
anchorage-independent cell cycle progression but not serum-independent
growth of rat intestinal epithelial cells (IEC18). ILK overexpression
results in increased expression of cyclin D1, activation of Cdk4 and
cyclin E-associated kinases, and hyperphosphorylation of the
retinoblastoma protein. In addition, ILK overexpression results in the
expression of p21 and p27 Cdk inhibitors with altered electrophoretic
mobilities, with the p27 from ILK-overexpressing cells having reduced
inhibitory activity. The transfer of serum-exposed IEC18 cells from
adherent cultures to suspension cultures results in a rapid
down-regulation of expression of cyclin D1 and cyclin A proteins as
well as in retinoblastoma protein dephosphorylation. In marked
contrast, transfer of ILK-overexpressing cells from adherent to
suspension cultures results in continued high levels of expression of
cyclin D1 and cyclin A proteins, and a substantial proportion of the retinoblastoma protein remains in a hyperphosphorylated state. These
results indicate that, when overexpressed, ILK induces signaling pathways resulting in the stimulation of G1/S
cyclin-Cdk activities, which are normally regulated by cell adhesion
and integrin engagement.
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