Summary
The alterations of the extracellular matrix play a critical role in the establishment, growth and invasiveness of tumors. We have reported an altered collagen metabolism in a human colon adenocarcinoma; the relative collagen content in the tumor was significantly lower than in normal tissue. This is due to a permanent phenotypic alteration in the tumor-associated fibroblast-like cells. The cell line BCS-TC2 established from this primary human colon adenocarcinoma maintains in culture several characteristics of the original tumor. We have studied the effects of extracellular matrix proteins on the behavior of BCS-TC2 cells. The modulation of the AMPase activity of 5′-nucleotidase by laminin and fibronectin suggest a possible function of the ectoenzyme as a cell receptor for matrix proteins. BCS-TC2 cell adhesion to laminin indicates the presence of different laminin receptors, among them, several integrins and the 67-kDa high-affinity laminin receptor. Integrins, talin and tyrosine phosphorylation activity, located into the focal adhesion sites could be implicated in the signal transduction by receptor from extracellular matrix. The expression of the 67-kDa laminin receptor, is modulated by laminin, and may contribute to BCS-TC2 cells interaction with the basement membranes, and it seems to be related to the invasive properties of these cells.
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Olmo, N., Lizarbe, M.A. (1994). Signal Transduction Through Laminin Receptors. Effects of Extracellular Matrix on BCS-TC2 Adenocarcinoma Cells. In: Municio, A.M., Miras-Portugal, M.T. (eds) Cell Signal Transduction, Second Messengers, and Protein Phosphorylation in Health and Disease. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1879-2_22
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DOI: https://doi.org/10.1007/978-1-4615-1879-2_22
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