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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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Double immunofluorescence microscopy showing  the colocalization of δ-catenin  with β-catenin in neocortical  neuroepithelia of postnatal day 2  mouse brain. (A) Low magnification view in which the rectangle shows the location of the immunofluorescent images in B  and C. CC, cerebral cortex. VZ,  ventricular zone. S, striatum.  Bar, 0.3 mm. (B) Frozen sagittal  section stained by rAb62. (C)  Same section immunostained by  mouse monoclonal anti–β-catenin. Bar, 20 μm.
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Figure 3: Double immunofluorescence microscopy showing the colocalization of δ-catenin with β-catenin in neocortical neuroepithelia of postnatal day 2 mouse brain. (A) Low magnification view in which the rectangle shows the location of the immunofluorescent images in B and C. CC, cerebral cortex. VZ, ventricular zone. S, striatum. Bar, 0.3 mm. (B) Frozen sagittal section stained by rAb62. (C) Same section immunostained by mouse monoclonal anti–β-catenin. Bar, 20 μm.

Mentions: δ-catenin is preferentially expressed in brain, with the highest expression levels during brain development. We first sought to determine whether δ-catenin was localized to cell boundaries in the developing brain. Postnatal day 2 mouse brain sections were double labeled with rAb62 and mouse monoclonal anti–β-catenin (Fig. 3). We concentrated on the neuroepithelial precursor cell population in the cortical ventricular zone where δ-catenin staining was most intense and where junctional complexes are prominent. The staining was most intense at the apical end of these cells along the ventricular boundary. Consistent with the staining pattern, adherens junctions are known to be prominent along the lateral surface at the apical end of neuroepithelial cells (Hinds and Ruffett, 1971; Shoukimas and Hinds, 1978). Deeper in the ventricular zone, δ-catenin staining was less intense and outlined the cell periphery in a honeycomb pattern. Double labeled samples showed that δ-catenin colocalized with β-catenin at points of cell–cell contact (Fig. 3, B and C). Double labeling with anti–N-cadherin showed similar colocalization; anti–E-cadherin failed to demonstrate a neuroepithelial localization (data not shown). Although weaker than in the ventricular zone, neuronal staining was present throughout the nervous system as described in Paffenholz and Franke and Zhou et al. (1997).


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)

Double immunofluorescence microscopy showing  the colocalization of δ-catenin  with β-catenin in neocortical  neuroepithelia of postnatal day 2  mouse brain. (A) Low magnification view in which the rectangle shows the location of the immunofluorescent images in B  and C. CC, cerebral cortex. VZ,  ventricular zone. S, striatum.  Bar, 0.3 mm. (B) Frozen sagittal  section stained by rAb62. (C)  Same section immunostained by  mouse monoclonal anti–β-catenin. Bar, 20 μm.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2132907&req=5

Figure 3: Double immunofluorescence microscopy showing the colocalization of δ-catenin with β-catenin in neocortical neuroepithelia of postnatal day 2 mouse brain. (A) Low magnification view in which the rectangle shows the location of the immunofluorescent images in B and C. CC, cerebral cortex. VZ, ventricular zone. S, striatum. Bar, 0.3 mm. (B) Frozen sagittal section stained by rAb62. (C) Same section immunostained by mouse monoclonal anti–β-catenin. Bar, 20 μm.
Mentions: δ-catenin is preferentially expressed in brain, with the highest expression levels during brain development. We first sought to determine whether δ-catenin was localized to cell boundaries in the developing brain. Postnatal day 2 mouse brain sections were double labeled with rAb62 and mouse monoclonal anti–β-catenin (Fig. 3). We concentrated on the neuroepithelial precursor cell population in the cortical ventricular zone where δ-catenin staining was most intense and where junctional complexes are prominent. The staining was most intense at the apical end of these cells along the ventricular boundary. Consistent with the staining pattern, adherens junctions are known to be prominent along the lateral surface at the apical end of neuroepithelial cells (Hinds and Ruffett, 1971; Shoukimas and Hinds, 1978). Deeper in the ventricular zone, δ-catenin staining was less intense and outlined the cell periphery in a honeycomb pattern. Double labeled samples showed that δ-catenin colocalized with β-catenin at points of cell–cell contact (Fig. 3, B and C). Double labeling with anti–N-cadherin showed similar colocalization; anti–E-cadherin failed to demonstrate a neuroepithelial localization (data not shown). Although weaker than in the ventricular zone, neuronal staining was present throughout the nervous system as described in Paffenholz and Franke and Zhou et al. (1997).

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