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J. Biol. Chem., Vol. 276, Issue 44, 40402-40410, November 2, 2001
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From the The various molecular forms of gastrin can act as
promoters of proliferation and differentiation in different regions of
the gastrointestinal tract. We report a novel stimulatory effect of glycine-extended gastrin17 only on cell/cell
dissociation and cell migration in a non-tumorigenic mouse gastric
epithelial cell line (IMGE-5). In contrast, both amidated and
glycine-extended gastrin17 stimulated proliferation of
IMGE-5 cells via distinct receptors. Glycine-extended
gastrin17-induced dissociation preceded migration and was
blocked by selective inhibitors of phosphatidylinositol 3-kinase
(PI3-kinase) but did not require mitogen-activated protein (MAP) kinase
activation. Furthermore, glycine-extended gastrin17 induced
a PI3-kinase-mediated tyrosine phosphorylation of the adherens junction
protein
Involvement of Phosphatidylinositol 3-Kinase and
Mitogen-activated Protein Kinases in Glycine-extended Gastrin-induced
Dissociation and Migration of Gastric Epithelial Cells*
§,§,¶,
,, and**
Laboratoire de Signalisation Cellulaire
Normale et Tumorale, EA MNRT 2995, Faculté de Pharmacie,
Montpellier 34060, France, and University of Melbourne,
Department of Surgery, Austin Hospital,
Melbourne, Victoria 3084, Australia
-catenin, partial dissociation of the complex between
-catenin and the transmembrane protein E-cadherin, and
delocalization of -catenin into the cytoplasm. Long lasting activation of MAP kinases by glycine-extended gastrin17 was
specifically required for the migratory response, in contrast to the
involvement of a rapid and transient MAP kinase activation in the
proliferative response to both amidated and glycine-extended
gastrin17. Therefore, the time course of MAP kinase
activation appears to be a critical determinant of the biological
effects mediated by this pathway. Together with the involvement of
PI3-kinase in the dissociation of adherens junctions, long term
activation of MAP kinases seems responsible for the selectivity of this
novel effect of G17-Gly on the adhesion and migration of
gastric epithelial cells.
*
This work was supported in part by Grants 940924 and 980625 from the National Health and Medical Research Council of Australia (to
G. B), IREX Grant X00001703 from the Australian Research Council, and
by the French Ministry for Education and Research and the Association
pour la Recherche contre le Cancer.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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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