Modulation of haptotactic migration of metastatic melanoma cells by the interaction between heparin and heparin-binding domain of fibronectin
Autor: | Takashi Makabe, Yuki Taguchi, F Kimizuka, Yasutoshi Kawase, I. Kato, Ikuo Saiki, Jun Murata, Ichiro Azuma, Yoichi Ohdate, Tomoko Shimojo |
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Rok vydání: | 1990 |
Předmět: |
Cell
Melanoma Experimental Biochemistry Cell Line Mice Cell Movement medicine Cell Adhesion Tumor Cells Cultured Animals Neoplasm Invasiveness Binding site Cell adhesion Molecular Biology Binding Sites biology Chemistry Heparin Cell Biology Adhesion Peptide Fragments Recombinant Proteins Cell biology Fibronectins Fibronectin Kinetics medicine.anatomical_structure Liver Cell culture biology.protein Binding domain medicine.drug |
Zdroj: | The Journal of biological chemistry. 265(24) |
ISSN: | 0021-9258 |
Popis: | We utilized recombinant fibronectin polypeptides with cell-binding domain and heparin-binding domains (referred to as C-274 and H-271, respectively) and their fusion polypeptide (CH-271) to examine the role of sulfated polysaccharide heparin and/or the functional domains of fibronectin in modulating tumor cell behavior. Both C-274 and CH-271 polypeptides with cell-binding domains promoted the adhesion and migration of B16-BL6 melanoma cells, whereas H-271 did not. Heparin bound to the immobilized polypeptides with heparin-binding domain (H-271, CH-271, and a mixture of C-274 and H-271 or fibronectin) but did not affect the tumor cell adhesion to the substrates. At the same time, heparin or two monoclonal antibodies against the heparin-binding domain were able to inhibit the haptotactic migration to CH-271 or fibronectin, though not to C-274 or a mixture of C-274 and H-271. This suggests that although heparin did not affect tumor cell adhesion to the cell-binding domain near the heparin-binding domain in CH-271 or fibronectin, it did lead to a modulation of cell motility. It seems likely that the regulatory mechanism may depend on interaction between heparin-like molecules on the cell surface and the heparin-binding domain in fibronectin, rather than on simple steric hindrance or on the masking of the cell-binding domain caused by the binding of heparin to heparin-binding domain. |
Databáze: | OpenAIRE |
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