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delta-catenin, an adhesive junction-associated protein which promotes cell scattering.

Lu Q, Paredes M, Medina M, Zhou J, Cavallo R, Peifer M, Orecchio L, Kosik KS - J. Cell Biol. (1999)

Bottom Line: We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain.In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone.The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin.

View Article: PubMed Central - PubMed

Affiliation: Center for Neurologic Diseases, Department of Neurology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.

ABSTRACT
The classical adherens junction that holds epithelial cells together consists of a protein complex in which members of the cadherin family linked to various catenins are the principal components. delta-catenin is a mammalian brain protein in the Armadillo repeat superfamily with sequence similarity to the adherens junction protein p120(ctn). We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain. The interaction with cadherin involves direct contact within the highly conserved juxtamembrane region of the COOH terminus, where p120(ctn) also binds. In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone. When transfected into Madin-Darby canine kidney (MDCK) epithelial cells delta-catenin colocalized with cadherin, p120(ctn), and beta-catenin. The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin. The ectopic expression of delta-catenin in MDCK cells altered their morphology, induced the elaboration of lamellipodia, interfered with monolayer formation, and increased scattering in response to hepatocyte growth factor treatment. We propose that delta-catenin can regulate adhesion molecules to implement the organization of large cellular arrays necessary for tissue morphogenesis.

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Ectopic expression of δ-catenin promotes HGF-stimulated cell spreading and scattering. (A) Two-chamber system showing the enhanced migration of δ-catenin–expressing cells.  CellL/CellU is the ratio of cells which migrated  from the upper chamber to the lower chamber.  C, control MDCK cells. C/H, control cells  treated with HGF. MF, δ-catenin–transfected  MDCK cells. MF/H, δ-catenin–transfected  MDCK cells treated with HGF. (B and C)  Monoclonal anti–E-cadherin immunofluorescence after overnight treatment with HGF. (B)  Mock-transfected MDCK cells. (C) MDCK cells  stably expressing δ-catenin. In B, cell–cell contact is still largely intact while in C cell–cell contact points appear disrupted (see arrows). (D and  E) Anti–δ-catenin immunofluorescent microscopy showing the effect of HGF on δ-catenin distribution. (D) δ-catenin–expressing cells before  HGF treatment. (E) δ-catenin–expressing cells  after HGF treatment sometimes remain in clusters but show disruptions at points of cell–cell  contact (see arrow) and show a redistribution of  δ-catenin to the intracellular compartment.  Bar, 5 μm.
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Figure 10: Ectopic expression of δ-catenin promotes HGF-stimulated cell spreading and scattering. (A) Two-chamber system showing the enhanced migration of δ-catenin–expressing cells. CellL/CellU is the ratio of cells which migrated from the upper chamber to the lower chamber. C, control MDCK cells. C/H, control cells treated with HGF. MF, δ-catenin–transfected MDCK cells. MF/H, δ-catenin–transfected MDCK cells treated with HGF. (B and C) Monoclonal anti–E-cadherin immunofluorescence after overnight treatment with HGF. (B) Mock-transfected MDCK cells. (C) MDCK cells stably expressing δ-catenin. In B, cell–cell contact is still largely intact while in C cell–cell contact points appear disrupted (see arrows). (D and E) Anti–δ-catenin immunofluorescent microscopy showing the effect of HGF on δ-catenin distribution. (D) δ-catenin–expressing cells before HGF treatment. (E) δ-catenin–expressing cells after HGF treatment sometimes remain in clusters but show disruptions at points of cell–cell contact (see arrow) and show a redistribution of δ-catenin to the intracellular compartment. Bar, 5 μm.

Mentions: Another explanation for the altered cell–cell relationships in transfected cells was that δ-catenin conferred enhanced motility on the cells, perhaps by altering the composition of the wild-type junctions. To explore this possibility the transfected cells were treated with hepatocyte growth factor/scatter factor (HGF/SF) (Rosen et al., 1994; Balkovetz et al., 1997) in two cell dispersion assays. In one assay, 5,000 control or transfected MDCK cells were plated in the upper chambers of a two-chamber system overnight. The upper chambers were then transferred to another chamber in the presence or absence of HGF for an additional 2 d. HGF treatment induced the migration of control MDCK cells to the lower chamber. When those cells expressed δ-catenin, a significantly greater number of cells migrated to the lower chamber compared to controls (Fig. 10 A). In a second assay, the effect of HGF on the scattering of islands of MDCK cells was measured. In this dispersion assay, islands of δ-catenin–expressing cells and control cells were treated overnight with HGF and immunostained with rAb62. δ-catenin–expressing cells showed a greater degree of dispersion than control cells. Indeed, after HGF stimulation >78% of the δ-catenin–expressing cells completely detached from each other, while only 17% of the untransfected cells reached the same stage of dissociation. Thus, δ-catenin further stimulated HGF-induced cell scattering.


delta-catenin, an adhesive junction-associated protein which promotes cell scattering.

Lu Q, Paredes M, Medina M, Zhou J, Cavallo R, Peifer M, Orecchio L, Kosik KS - J. Cell Biol. (1999)

Ectopic expression of δ-catenin promotes HGF-stimulated cell spreading and scattering. (A) Two-chamber system showing the enhanced migration of δ-catenin–expressing cells.  CellL/CellU is the ratio of cells which migrated  from the upper chamber to the lower chamber.  C, control MDCK cells. C/H, control cells  treated with HGF. MF, δ-catenin–transfected  MDCK cells. MF/H, δ-catenin–transfected  MDCK cells treated with HGF. (B and C)  Monoclonal anti–E-cadherin immunofluorescence after overnight treatment with HGF. (B)  Mock-transfected MDCK cells. (C) MDCK cells  stably expressing δ-catenin. In B, cell–cell contact is still largely intact while in C cell–cell contact points appear disrupted (see arrows). (D and  E) Anti–δ-catenin immunofluorescent microscopy showing the effect of HGF on δ-catenin distribution. (D) δ-catenin–expressing cells before  HGF treatment. (E) δ-catenin–expressing cells  after HGF treatment sometimes remain in clusters but show disruptions at points of cell–cell  contact (see arrow) and show a redistribution of  δ-catenin to the intracellular compartment.  Bar, 5 μm.
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Related In: Results  -  Collection

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Figure 10: Ectopic expression of δ-catenin promotes HGF-stimulated cell spreading and scattering. (A) Two-chamber system showing the enhanced migration of δ-catenin–expressing cells. CellL/CellU is the ratio of cells which migrated from the upper chamber to the lower chamber. C, control MDCK cells. C/H, control cells treated with HGF. MF, δ-catenin–transfected MDCK cells. MF/H, δ-catenin–transfected MDCK cells treated with HGF. (B and C) Monoclonal anti–E-cadherin immunofluorescence after overnight treatment with HGF. (B) Mock-transfected MDCK cells. (C) MDCK cells stably expressing δ-catenin. In B, cell–cell contact is still largely intact while in C cell–cell contact points appear disrupted (see arrows). (D and E) Anti–δ-catenin immunofluorescent microscopy showing the effect of HGF on δ-catenin distribution. (D) δ-catenin–expressing cells before HGF treatment. (E) δ-catenin–expressing cells after HGF treatment sometimes remain in clusters but show disruptions at points of cell–cell contact (see arrow) and show a redistribution of δ-catenin to the intracellular compartment. Bar, 5 μm.
Mentions: Another explanation for the altered cell–cell relationships in transfected cells was that δ-catenin conferred enhanced motility on the cells, perhaps by altering the composition of the wild-type junctions. To explore this possibility the transfected cells were treated with hepatocyte growth factor/scatter factor (HGF/SF) (Rosen et al., 1994; Balkovetz et al., 1997) in two cell dispersion assays. In one assay, 5,000 control or transfected MDCK cells were plated in the upper chambers of a two-chamber system overnight. The upper chambers were then transferred to another chamber in the presence or absence of HGF for an additional 2 d. HGF treatment induced the migration of control MDCK cells to the lower chamber. When those cells expressed δ-catenin, a significantly greater number of cells migrated to the lower chamber compared to controls (Fig. 10 A). In a second assay, the effect of HGF on the scattering of islands of MDCK cells was measured. In this dispersion assay, islands of δ-catenin–expressing cells and control cells were treated overnight with HGF and immunostained with rAb62. δ-catenin–expressing cells showed a greater degree of dispersion than control cells. Indeed, after HGF stimulation >78% of the δ-catenin–expressing cells completely detached from each other, while only 17% of the untransfected cells reached the same stage of dissociation. Thus, δ-catenin further stimulated HGF-induced cell scattering.

Bottom Line: We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain.In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone.The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin.

View Article: PubMed Central - PubMed

Affiliation: Center for Neurologic Diseases, Department of Neurology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.

ABSTRACT
The classical adherens junction that holds epithelial cells together consists of a protein complex in which members of the cadherin family linked to various catenins are the principal components. delta-catenin is a mammalian brain protein in the Armadillo repeat superfamily with sequence similarity to the adherens junction protein p120(ctn). We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain. The interaction with cadherin involves direct contact within the highly conserved juxtamembrane region of the COOH terminus, where p120(ctn) also binds. In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone. When transfected into Madin-Darby canine kidney (MDCK) epithelial cells delta-catenin colocalized with cadherin, p120(ctn), and beta-catenin. The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin. The ectopic expression of delta-catenin in MDCK cells altered their morphology, induced the elaboration of lamellipodia, interfered with monolayer formation, and increased scattering in response to hepatocyte growth factor treatment. We propose that delta-catenin can regulate adhesion molecules to implement the organization of large cellular arrays necessary for tissue morphogenesis.

Show MeSH
Related in: MedlinePlus