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Expression of podocalyxin enhance the adherence, migration, and intercellular communication of cells

AutorLarrucea, Susana ; Butta, Nora ; García Arias-Salgado, Elena ; Alonso-Martín, Sonia; Sánchez Ayuso, Matilde ; Parrilla, Roberto L.
Palabras clavePodocalyxin
shRNA
Cell adhesion
Cell–cell contact
Migration
Actin cytoskeleton
β1 integrins
Glycomutant CHO cells
Fecha de publicaciónjun-2008
EditorElsevier
CitaciónExperimental Cell Research 314(10):2004-2015(2008)
ResumenPodocalyxin (PODXL) is an anti-adhesive glycoprotein expressed abundantly in the epithelial cells of kidney glomeruli. In contrast, we report herein that expression of podocalyxinGFP (PODXLGFP) in CHO cells increased the adherence to immobilized fibronectin, spreading, and migration. The transient knockdown of PODXL or the expression of PODXL lacking the cytosolic carboxyterminal domain (PODXL-Δ451) inhibited cell adherence. Moreover, the effect of PODXL was prevented by the ectodomain of podocalyxin (PODXL-Δ429), by RGD peptides, or by inhibitors of the vitronectin receptor (αvβ3). CHO-PODXLGFP also showed adherence to human vascular endothelial cells (HUVEC), exhibiting polarization of granular PODXL and emission of long and thin, spike-like, protrusions with PODXL granules progressing along. We found PODXL colocalized with β1 integrins at membrane ruffle regions on the leading edge of the cell and a blocking β1 mAb prevented the spreading of cells. PODXL was also associated with submembrane actin in lamellipodia ruffles, or with vinculin at cell protrusions. The proadhesive effects of PODXL were absent in sialic acid deficient O-glycomutant CHO cells. To conclude, we present evidence indicating that human PODXL enhances the adherence of cells to immobilized ligands and to vascular endothelial cells through a mechanism(s) dependent on the activity of integrins
Descripción12 páginas, 9 páginas -- PAGS nros. 2004-2015
Versión del editorhttp://dx.doi. org/10.1016/j.yexcr.2008.03.009
URIhttp://hdl.handle.net/10261/57321
DOI10.1016/j.yexcr.2008.03.009
ISSN0014-4827
E-ISSN1090-2422
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