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Fig. 7. Ectopic E-cadherin cell surface expression and association with catenins. The amount of surface E-cadherin was analyzed biochemically. (A) E-cadherin was detected by immunoblot analysis after trypsin/Ca2+ (TC) or trypsin/EGTA (TE) treatment. E-cadherin expressed on the cell surface was resistant to TC treatment, but sensitive to TE treatment. Only intracellular E-cadherin was detected following TE treatment. (B) E-cadherin was detected by immunoblot analysis after cell surface proteins were biotinylated and collected using avidin beads. After surface biotinylation, cells were lysed. After collection of biotinylated proteins (collected 1), the remaining lysate was re-collected (collected 2). The E-cadherin protein contained in either the collected (1) or remainder (2) portions were subjected to immunoblot analysis using an anti-E-cadherin antibody. To facilitate estimation, dilutions of the materials in each fraction were applied to the gels. (C) Formation of E-cadherin and catenin complexes in MDCK-Sna-Ecad cells. Cells were lysed and subjected to immunoprecipitation with an anti-myc antibody to precipitate ectopically expressed E-cadherin. Immunoprecipitates were subjected to immunoblot analysis using the indicated antibodies.





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