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Journal of Cell Science, Vol 114, Issue 6 1125-1136, Copyright © 2001 by Company of Biologists

JOURNAL ARTICLES

Overexpression of the integrin-linked kinase mesenchymally transforms mammary epithelial cells

A Somasiri, A Howarth, D Goswami, S Dedhar and CD Roskelley
Dept of Anatomy, University of British Columbia, Vancouver B.C., Canada, V6T 1Z3. roskelly@interchange.ubc.ca

Signals generated by the interaction of (&bgr;)1 integrins with laminin in the basement membrane contribute to mammary epithelial cell morphogenesis and differentiation. The integrin-linked kinase (ILK) is one of the signaling moieties that associates with the cytoplasmic domain of (&bgr;)1 integrin subunits with some specificity. Forced expression of a dominant negative, kinase-dead form of ILK subtly altered mouse mammary epithelial cell morphogenesis but it did not prevent differentiative milk protein expression. In contrast, forced overexpression of wild-type ILK strongly inhibited both morphogenesis and differentiation. Overexpression of wild-type ILK also caused the cells to lose the cell-cell adhesion molecule E-cadherin, become invasive, reorganize cortical actin into cytoplasmic stress fibers, and switch from an epithelial cytokeratin to a mesenchymal vimentin intermediate filament phenotype. Forced expression of E-cadherin in the latter mesenchymal cells rescued epithelial cytokeratin expression and it partially restored the ability of the cells to differentiate and undergo morphogenesis. These data demonstrate that ILK, which responds to interactions between cells and the extracellular matrix, induces a mesenchymal transformation in mammary epithelial cells, at least in part, by disrupting cell-cell junctions.


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