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Characterization of integrin and anchorage dependence in mammary epithelial cells following c-erbB2-induced epithelial-mesenchymal transition.

Journal article
Authors Lachmi E Jenndahl
Joyce Taylor-Papadimitriou
Dan Baeckström
Published in Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine
Volume 27
Issue 1
Pages 50-8
ISSN 1010-4283
Publication year 2006
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 50-8
Language en
Links dx.doi.org/10.1159/000090156
Keywords Breast Neoplasms, physiopathology, Cell Communication, Cell Proliferation, Epithelial Cells, physiology, Extracellular Matrix, Female, Fibroblasts, physiology, Humans, Integrins, Mammary Glands, Human, cytology, Mesoderm, Phenotype, Receptor, erbB-2, physiology, Receptors, Fibronectin, biosynthesis, physiology, Signal Transduction, Up-Regulation
Subject categories Medical and Health Sciences

Abstract

Signalling from the proto-oncogene c-erbB2 in mammary epithelial cells has earlier been shown to result in epithelial-mesenchymal transition (EMT) giving rise to fibroblast-like cells, and acquisition of anchorage-independent growth (AIG) usually determined by growth capacity in soft agar. In this study, we have analysed AIG associated with c-erbB2-induced EMT in a human mammary epithelial cell line. Intriguingly, cells capable of growth in soft agar were shown to be dependent on the function of beta(1) integrin extracellular matrix receptors for growth in collagen. We therefore tested the hypothesis that apparent AIG was due to deposition of extracellular matrix in the agar. Although the fibroblastic cells had strongly upregulated expression of the fibronectin receptor subunit integrin alpha(5) andabundant fibronectin fibrils, these properties did not have a positive correlation with AIG. Furthermore, antibody blocking of integrin alpha(5) and beta(1) failed to inhibit AIG. These results indicate that the anchorage-independent cells are not dependent on connection to extracellular matrix, but instead may be subject to a growth-inhibitory effect from the collagen in the absence of integrin signalling. This notion was supported by the finding that integrin blocking of the fibroblastic cells in fibrin was without effect on proliferation.

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