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J. Biol. Chem., Vol. 277, Issue 10, 8226-8234, March 8, 2002
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From the Canadian Institutes of Health Research Group on Functional
Development and Physiopathology of the Digestive Tract,
Département d'Anatomie et Biologie Cellulaire, Faculté de
Médecine, Université de Sherbrooke, Sherbrooke,
Québec J1H 5N4, Canada
The signaling pathways mediating human intestinal
epithelial cell differentiation remain largely undefined.
Phosphatidylinositol 3-kinase (PI3K) is an important modulator of
extracellular signals, including those elicited by E-cadherin-mediated
cell-cell adhesion, which plays an important role in maintenance of the
structural and functional integrity of epithelia. In this study, we
analyzed the involvement of PI3K in the differentiation of human
intestinal epithelial cells. We showed that inhibition of PI3K
signaling in Caco-2/15 cells repressed sucrase-isomaltase and villin
protein expression. Morphological differentiation of enterocyte-like
features in Caco-2/15 cells such as epithelial cell polarity and
brush-border formation were strongly attenuated by PI3K inhibition.
Immunofluorescence and immunoprecipitation experiments revealed that
PI3K was recruited to and activated by E-cadherin-mediated cell-cell
contacts in confluent Caco-2/15 cells, and this activation appears to
be essential for the integrity of adherens junctions and association
with the cytoskeleton. We provide evidence that the assembly of
calcium-dependent adherens junctions led to a rapid and
remarkable increase in the state of activation of Akt and p38 MAPK
pathways and that this increase was blocked in the presence of
anti-E-cadherin antibodies and PI3K inhibitor. Therefore, our results
indicate that PI3K promotes assembly of adherens junctions, which, in
turn, control p38 MAPK activation and enterocyte differentiation.
Phosphatidylinositol 3-Kinase Controls Human Intestinal
Epithelial Cell Differentiation by Promoting Adherens Junction Assembly
and p38 MAPK Activation*
,
*
This work was supported by Canadian Institutes of Health
Research Grants MT-14405 and GR-15186.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Student Scholar from the Fonds de la Recherche en Santé du
Québec.
§
Scholar from the Fonds de la Recherche en Santé du
Québec. To whom correspondence should be addressed. Tel.:
819-564-5271; Fax: 819-564-5320; E-mail:
nrivard@courrier.usherb.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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