Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA

Abstract

E-cadherin is a cell surface glycoprotein responsible for Ca²⁺-dependent intercellular adhesion between epithelial cells¹; it is also called uvomorulin², L-CAM (ref. 3), cell-CAM 120/80 (ref. 4) or Arc-1 (ref. 5). Because blocking the action of E-cadherin by monoclonal antibodies causes dispersion of compact cell colonies¹, this molecule is thought to be an important factor for maintenance of multicellular systems. To demonstrate directly that E-cadherin is involved in cell–cell adhesion, we cloned full-length cDNA encoding E-cadherin from F9 cells and introduced it into L fibroblasts deficient in E-cadherin. These L cells acquire strong Ca²⁺-dependent aggregating activity by expressing the E-cadherin derived from the introduced cDNA, and were morphologically transformed so as to form colonies in which cells were tightly connected to each other.