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Functional interaction between E-cadherin and alphav-containing integrins in carcinoma cells
M von Schlippe1, J F Marshall, P Perry
1Richard Dimbleby Department of Cancer Research, Imperial Cancer Research Fund, Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Journal of Cell Science
|January 20, 2000
Summary
Cross-talk between E-cadherin and alphav integrins influences breast cancer cell behavior. Blocking alphav integrins alters cell growth, while disrupting E-cadherin increases migration via alphav integrin activation.
Area of Science:
- Cell Biology
- Molecular Biology
- Cancer Research
Background:
- E-cadherin mediates cell-cell adhesion, crucial for tissue integrity.
- Alphav integrins are cell surface receptors involved in cell adhesion and migration.
- Cross-talk between E-cadherin and integrins is implicated in cancer progression.
Purpose of the Study:
- To investigate the functional cross-talk between E-cadherin and alphav integrins in breast carcinoma cells.
- To determine how alphav integrin activity affects E-cadherin-mediated cell morphology.
- To explore the impact of modulating E-cadherin on alphav integrin activity and cell migration.
Main Methods:
- Utilized function-blocking anti-alphav monoclonal antibody (17E6) on breast cancer cell lines.
- Introduced a dominant-negative E-cadherin construct into ZR75-1 cells (ZR-E2R1).
- Assessed cell morphology, E-cadherin and beta-catenin levels, and cell migration towards specific substrates (vitronectin, collagen type I, fibronectin, laminin).
- Employed antibody blockade of alphavbeta5 and alphavbeta1 integrins.
Main Results:
- Blocking alphav integrins induced spheroid formation in cells with detergent-insoluble E-cadherin, dependent on alphav occupancy and aggregation.
- Dominant-negative E-cadherin in ZR-E2R1 cells led to reduced E-cadherin expression and increased beta-catenin levels.
- ZR-E2R1 cells exhibited significantly increased migration towards vitronectin, which was blocked by targeting alphavbeta5 and alphavbeta1 integrins.
- No change in total alphav integrin levels was observed.
Conclusions:
- Alphav integrin-dependent adhesion suppresses E-cadherin-mediated morphological changes in breast cancer cells.
- Disruption of E-cadherin function enhances cell migration towards vitronectin through increased alphav integrin activity.
- These findings reveal a significant cross-talk mechanism between E-cadherin and alphav integrins that influences breast cancer cell behavior and motility.
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