par Rocha, Ana Sofia;Moreira, Severina;Costa, Maria ;Soares, Paula;De Wever, Olivier;Mareel, Marcus;Vandekerckhove, Joël
Référence Thyroid, 14, 11, page (902-909)
Publication Publié, 2004-11
Référence Thyroid, 14, 11, page (902-909)
Publication Publié, 2004-11
Article révisé par les pairs
Résumé : | Members of a family of thyroid cell lines (KAT) were analyzed because they expressed a higher molecular weight (135 kd) form of E-cadherin at their surface. We found that this aberrant E-cadherin is the result of a point mutation in the exon 9 donor splice site causing a skipping of exon 9 with consequent deletion of the corresponding aminoacids on E-cadherin protein. As a spin-off, we report that the various members of the KAT family share this mutation as well as the genetic background. Furthermore we found that this mutated protein leads to disturbed cell-cell adhesion although E-cadherin is still able to mediate the formation of the cadherin/catenin complex. We also demonstrate the presence of another cell-cell adhesion complex, formed by P-cadherin and the catenins. The latter is also not able to mediate cell-cell adhesion. Although these cells lack cell-cell adhesion they are not invasive without exogenous stimulus. |