E-cadherin and β-catenin interactions plays a significant role in several essential biological processes, with disruptions in this interaction contributing to cancer progression. Naveni® technology enables scientists to visualize and quantify these interactions in patient samples, offering insights into cancer development and aiding targeted therapy development.
E-cadherin and β-catenin interactions and their impact on cell adhesion and cancer
E-cadherin and β-catenin interactions plays a significant role in several essential biological processes, with disruptions in this interaction contributing to cancer progression. Naveni® technology enables scientists to visualize and quantify these interactions in patient samples, offering insights into cancer development and aiding targeted therapy development.
E-cadherin/β-catenin interaction visualized in healthy colon tissue with NaveniFlex™ Tissue. Interaction in yellow, co-stain with cytokeratin in red, and cell nuclei in blue (DAPI)
Disruption of E-cadherin/β-catenin interaction and the initiation of cancer progression
Among other biological processes, E-cadherin/β-catenin interactions are notably involved in cell adhesion. The extracellular domain of E-cadherin, a transmembrane glycoprotein, forms calcium-dependent homophilic bonds with E-cadherin molecules on neighboring cells, resulting in adherens junctions. β-catenin, an intracellular protein, binds to the cytoplasmic domain of E-cadherin, linking it to the actin cytoskeleton. This interaction contributes to the maintenance of tissue integrity and tight cell-cell adhesion [1].
However, disruption of this E-cadherin/β-catenin interaction is implicated in the initiation of epithelial to mesenchymal transition (EMT) and cancer progression [2]. During EMT, differentiated epithelial cells lose their epithelial characteristics, gain a more invasive, mesenchymal phenotype and start producing interstitial matrix components [3]. Loss or downregulation of E-cadherin is a common feature in many cancer types and is associated with increased invasiveness and metastasis, as reduced E-cadherin expression disrupts cell-cell adhesion, allowing cancer cells to detach from the primary tumor and invade surrounding tissues [4].
Furthermore, dysregulation of the Wnt signaling pathway can lead to the accumulation of cytoplasmic β-catenin, which can then translocate to the nucleus and activate oncogenic targets. This process is frequently observed in colorectal cancer and various other malignancies [5].
E-cadherin/β-catenin interaction visualized in healthy colon tissue with NaveniFlex™ Tissue. Interaction in yellow, co-stain with cytokeratin in red, and cell nuclei in blue (DAPI)
Disruption of E-cadherin/β-catenin interaction and the initiation of cancer progression
Among other biological processes, E-cadherin/β-catenin interactions are notably involved in cell adhesion. The extracellular domain of E-cadherin, a transmembrane glycoprotein, forms calcium-dependent homophilic bonds with E-cadherin molecules on neighboring cells, resulting in adherens junctions. β-catenin, an intracellular protein, binds to the cytoplasmic domain of E-cadherin, linking it to the actin cytoskeleton. This interaction contributes to the maintenance of tissue integrity and tight cell-cell adhesion [1].
However, disruption of this E-cadherin/β-catenin interaction is implicated in the initiation of epithelial to mesenchymal transition (EMT) and cancer progression [2]. During EMT, differentiated epithelial cells lose their epithelial characteristics, gain a more invasive, mesenchymal phenotype and start producing interstitial matrix components [3]. Loss or downregulation of E-cadherin is a common feature in many cancer types and is associated with increased invasiveness and metastasis, as reduced E-cadherin expression disrupts cell-cell adhesion, allowing cancer cells to detach from the primary tumor and invade surrounding tissues [4].
Furthermore, dysregulation of the Wnt signaling pathway can lead to the accumulation of cytoplasmic β-catenin, which can then translocate to the nucleus and activate oncogenic targets. This process is frequently observed in colorectal cancer and various other malignancies [5].
Figure 1. Model of Navinci’s in situ proximity ligation assay for E-cadherin and β-catenin interactions. Only if the Navenibodies are in close proximity will they generate a rolling circle amplification reaction, leading to a strong and distinct signal
Figure 1. Model of Navinci’s in situ proximity ligation assay for E-cadherin and β-catenin interactions. Only if the Navenibodies are in close proximity will they generate a rolling circle amplification reaction, leading to a strong and distinct signal
Naveni® technology enables the visualization of E-cadherin and β-catenin interactions
We have demonstrated the use of the classic Naveni® in situ proximity ligation assay for the visualization of the interaction between E-cadherin and β-catenin both in cell lines and FFPE tissues. Furthermore, with Naveni® TriFlex Cell we simultaneously showed both the individual E-cadherin and β-catenin molecules and their interaction and quantified the data. The information of the presence or disruption of the interaction in patient samples, and the possibility to observe the levels and localization of the individual proteins can have significant implications for cancer research and the development of targeted therapies.
Naveni® technology enables the visualization of E-cadherin and β-catenin interactions
We have demonstrated the use of the classic Naveni® in situ proximity ligation assay for the visualization of the interaction between E-cadherin and β-catenin both in cell lines and FFPE tissues. Furthermore, with Naveni® TriFlex Cell we simultaneously showed both the individual E-cadherin and β-catenin molecules and their interaction and quantified the data. The information of the presence or disruption of the interaction in patient samples, and the possibility to observe the levels and localization of the individual proteins can have significant implications for cancer research and the development of targeted therapies.
Application example – E-cadherin/β-catenin interaction in skin brightfield readout
Application example – E-cadherin/β-catenin interaction in skin brightfield readout
E-cadherin and β-catenin interactions in tissue slides from skin, detection using NaveniBright HRP
E-cadherin and β-catenin interactions in tissue slides from skin, detection using NaveniBright HRP
E-cadherin and β-catenin interactions in tissue slides from skin, detection using NaveniBright HRP
Application example – E-cadherin/β-catenin interaction fluorescence readout
Application example – E-cadherin/β-catenin interaction fluorescence readout
E-cadherin/β-catenin interaction visualized in skin tissue (scalp), detection with NaveniFlex Tissue
E-cadherin/β-catenin interaction visualized in colon cancer, detection with NaveniFlex Tissue
E-cadherin/β-catenin interaction visualized in MCF-7 cells, detection with NaveniFlex
E-cadherin/β-catenin interaction visualized in skin tissue, colon cancer, and MCF-7 cells, detection with NaveniFlex Tissue and NaveniFlex
Application example – E-cadherin/β-catenin interaction as well as total E-cadherin and β-catenin
Application example – E-cadherin/β-catenin interaction as well as total E-cadherin and β-catenin
Total protein signal of Beta-catenin in MCF7 cells, signals visualized in FITC filter set (yellow)
Total protein signal of E-Cadherin in the same MCF7 cells, signals visualized in Cy3 filter set (magenta)
Beta-catenin/E-Cadherin interaction in the same MCF7 cells, signals visualized in Cy5 filter set (cyan)
Merge of the three filter sets, Beta-catenin signals in yellow and E-Cadherin signals in magenta. Beta-catenin/E-Cadherin interaction in cyan. Overlapping signal is white.
Beta-catenin signals in yellow, and E-Cadherin signals in magenta. Beta-catenin/E-Cadherin interaction in cyan. Overlapping signal is white.
How to detect E-cadherin and β-catenin interactions
Use our products NaveniBright AP, NaveniFlex Tissue MR Atto647N, NaveniFlex Cell MR Atto647N, and Naveni TriFlex Cell; these products were used in the above examples. For further information about E-cadherin/β-catenin monoclonal antibodies and protocols, contact us using the form below.
How to detect E-cadherin and β-catenin interactions
Use our products NaveniBright AP, NaveniFlex Tissue MR Atto647N, NaveniFlex Cell MR Atto647N, and Naveni TriFlex Cell; these products were used in the above examples. For further information about E-cadherin/β-catenin monoclonal antibodies and protocols, contact us using the form below.
NaveniBright AP
The assay is designed to be used with a mouse and a rabbit primary pair. Chromogenic readout with AP substrate.
NaveniFlex Tissue
The assay is designed to be used with a mouse and rabbit primary antibody pair. Detection with Atto647N fluorophore is included.
Naveni Triflex Cell
The assay is designed to be used with a mouse and rabbit primary antibody pair.
NaveniFlex Cell
The assay is designed to be used with a mouse and rabbit primary antibody pair. Detection with Atto647N fluorophore is included.
NaveniBright AP
The assay is designed to be used with a mouse and a rabbit primary pair. Chromogenic readout with AP substrate.
NaveniFlex Tissue
The assay is designed to be used with a mouse and rabbit primary antibody pair. Detection with Atto647N fluorophore is included.
Naveni Triflex Cell
The assay is designed to be used with a mouse and rabbit primary antibody pair.
NaveniFlex Cell
The assay is designed to be used with a mouse and rabbit primary antibody pair. Detection with Atto647N fluorophore is included.
References
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- Gumbiner, B.M. (2005). Regulation of cadherin-mediated adhesion in morphogenesis. Nature Reviews Molecular Cell Biology, 6(8), 622–634. DOI: 10.1038/nrm1699
- Thiery, J.P., Acloque, H., Huang, R.Y., & Nieto, M.A. (2009). Epithelial-mesenchymal transitions in development and disease. Cell, 139(5), 871-890. DOI: 10.1016/j.cell.2009.11.007
- Tian, X., Liu, Z., Niu, B., Zhang, J., Tan, T.K., Lee, S.R., Zhao, Y., Harris, D.C., & Zheng G. (2011). E-cadherin/β-catenin complex and the epithelial barrier. J Biomed Biotechnol. 2011:567305. DOI: 10.1155/2011/567305
- Jeanes, A., Gottardi, C.J., & Yap, A.S. (2008). Cadherins and cancer: How does cadherin dysfunction promote tumor progression? Oncogene, 27(55), 6920-6929. DOI: 10.1038/onc.2008.343
- Clevers, H., & Nusse, R. (2012). Wnt/β-catenin signaling and disease. Cell, 149(6), 1192-1205. DOI: 10.1016/j.cell.2012.05.012