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Overexpression of c-Src Enhances Cell-Matrix Adhesion and Cell Migration in PDGF-Stimulated NIH3T3 Fibroblasts
c-Src is normally associated with the plasma membrane, but upon activation by tyrosine kinase receptors it translocates to the cytoskeleton. Activation of c-Src alters its conformation and induces the association of c-Src with cytoskeletal proteins. c-Src is implicated in tyrosine phosphorylation of...
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Published in: | Experimental cell research 1999-05, Vol.248 (2), p.531-537 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | c-Src is normally associated with the plasma membrane, but upon activation by tyrosine kinase receptors it translocates to the cytoskeleton. Activation of c-Src alters its conformation and induces the association of c-Src with cytoskeletal proteins. c-Src is implicated in tyrosine phosphorylation of cytoskeletal proteins, which might affect the cytoskeletal architecture. Rearrangements of the cytoskeleton affect cell-matrix adhesion and cell migration. In this study NIH3T3 fibroblasts, that overexpress c-Src, were used to analyze the effect of c-Src on both cell-matrix adhesion and cell migration. Upon PDGF stimulation translocation of c-Src to the cytoskeleton was detected. PDGF treatment also increased cell-matrix adhesion and cell migration. The cell line with the highest c-Src expression showed the largest increases in both phenomena. These findings suggest that translocation of c-Src to the cytoskeleton results in enhanced cell-matrix adhesion and cell migration. |
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ISSN: | 0014-4827 1090-2422 |
DOI: | 10.1006/excr.1999.4416 |