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Am J Physiol Gastrointest Liver Physiol 284: G75-G84, 2003; doi:10.1152/ajpgi.00300.2002
0193-1857/03 $5.00
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Vol. 284, Issue 1, G75-G84, January 2003

Stimulation of gastrin-CCKB receptor promotes migration of gastric AGS cells via multiple paracrine pathways

Peter J. M. Noble1, Geraint Wilde2, Michael R. H. White2, Steven R. Pennington3, Graham J. Dockray1, and Andrea Varro1

1 Physiological Laboratory, 2 School of Biological Sciences, and 3 Department of Human Anatomy and Cell Biology, University of Liverpool, Liverpool L69 3BX, United Kingdom

Responses to G protein-coupled receptor stimulation may be mediated by paracrine factors. We have developed a coculture system to study paracrine regulation of migration of gastric epithelial (AGS) cells after stimulation of gastrin-CCKB receptors. In cells expressing this receptor, G-17 stimulated migration by activation of protein kinase C. However, G-17 also stimulated the migration of cells expressing green fluorescent protein, but not the receptor, when they were cocultured with receptor-expressing cells consistent with activation of paracrine signals. The use of various pharmacological inhibitors indicated that gastrin stimulated migration via activation of the EGF receptor (EGR-R), the erbB-2 receptor tyrosine kinase, and the MAP kinase pathway. However, gastrin also released fibroblast growth factor (FGF)-1, and migration was inhibited by the FGF receptor tyrosine kinase inhibitor SU-5402. Flow cytometry indicated that in both cell types, gastrin increased MAP kinase via activation of EGF-R but not FGF-R1 or erbB-2. We conclude that gastrin-CCKB receptors stimulate epithelial cell migration partly via paracrine mechanisms; transactivation of EGF-R is only one component of the paracrine pathway.

epidermal growth factor; epithelial cell migration; G protein-coupled receptor; fibroblast growth factor


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