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J. Biol. Chem., Vol. 276, Issue 24, 21885-21894, June 15, 2001
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From the CIHR 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 intracellular signaling pathways responsible
for cell cycle arrest and differentiation along the crypt-villus axis
of the human small intestine remain largely unknown. p38
mitogen-activated protein kinases (MAPKs) have recently emerged as key
modulators of various vertebrate cell differentiation processes. In
order to elucidate further the mechanism(s) responsible for the loss of
proliferative potential once committed intestinal cells begin to
differentiate, the role and regulation of p38 MAPK with regard to
differentiation were analyzed in both intact epithelium as well as in
well established intestinal cell models recapitulating the crypt-villus
axis in vitro. Results show that phosphorylated and active
forms of p38 were detected primarily in the nuclei of differentiated
villus cells. Inhibition of p38 MAPK signaling by 2-20
µM SB203580 did not affect E2F-dependent
transcriptional activity in subconfluent Caco-2/15 or HIEC cells. p38
MAPK activity dramatically increased as soon as Caco-2/15 cells reached
confluence, whereas addition of SB203580 during differentiation of
Caco-2/15 cells strongly attenuated sucrase-isomaltase gene and protein expression as well as protein expression of villin and alkaline phosphatase. The binding of CDX2 to the sucrase-isomaltase promoter and
its transcriptional activity were significantly reduced by SB203580.
Pull-down glutathione S-transferase and immunoprecipitation experiments demonstrated a direct interaction of CDX3 with p38. Finally, p38-dependent phosphorylation of CDX3 was observed
in differentiating Caco-2/15 cells. Taken together, our results
indicate that p38 MAPK may be involved in the regulation of CDX2/3
function and intestinal cell differentiation.
Intestinal Epithelial Cell Differentiation Involves Activation of
p38 Mitogen-activated Protein Kinase That Regulates the Homeobox
Transcription Factor CDX2*
*
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.
Chercheur-boursier du Fonds de la Recherche en Santé du
Québec. To whom correspondence should be addressed: Dépt.
d'Anatomie et de Biologie Cellulaire, Faculté de Médecine,
Université de Sherbrooke, Sherbrooke, Québec J1H5N4,
Canada. Tel.: 819-564-5271; Fax: 819-564-5320; E-mail:
nrivard@courrier.usherb.ca.
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