Role of p120ctn in Cadherin Mediated Suppression of Breast Cancer Invasiveness
Abstract
The goal of our research is to understand the way in which pl20--catenin regulates the function of the cell adhesion molecule E-cadherin. E-cadherin is necessary for inhibiting metastasis of human cancer cells. Previously, we uncoupled pl2O from E-cadherin through small juxtamembrane domain substitutions on E-cadherin. This resulted in a loss of strong adhesion and lack of tight colony formation in cells in which p120 and E-cadherin were uncoupled. In this reporting period, we have created a tool to investigate the role of p120 in cadherin clustering and cadherin-mediated signal transduction. We purified a dimerized form of the E-cadherin extracellular domain, and showed that this protein facilitates calcium-dependent homotypic interactions. In addition-, we have described a pl20-deficient cell line that requires" p120 transfection for normal cadherin function. Our data suggest a crucial role for p120 in E-cadherin function and stability, and give insight into possible ways to prevent or inhibit tumor metastasis.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2002
- Accession Number
- ADA406777
Entities
People
- Albert B. Reynolds
- Molly A. Thoreson
Organizations
- Vanderbilt University Medical Center