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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ohe, N. Maeda, T. Manabe, R. Sekiguchi, K. Fukuda, T. |
| Description | Author Affiliation: Manabe R ( Research Institute, Osaka Medical Center for Maternal and Child Health, Japan.) |
| Abstract | Fibronectin (FN) has a complex pattern of alternative splicing at the mRNA level. One of the alternatively spliced segments, EDA, is prominently expressed during biological processes involving substantial cell migration and proliferation, such as embryonic development, malignant transformation, and wound healing. To examine the function of the EDA segment, we overexpressed recombinant FN isoforms with or without EDA in CHO cells and compared their cell-adhesive activities using purified proteins. $EDA^{+}$ FN was significantly more potent than $EDA^{−}$ FN in promoting cell spreading and cell migration, irrespective of the presence or absence of a second alternatively spliced segment, EDB. The cell spreading activity of $EDA^{+}$ FN was not affected by antibodies recognizing the EDA segment but was abolished by antibodies against integrin α5 and β1 subunits and by Gly-Arg-Gly-Asp-Ser-Pro peptide, indicating that the EDA segment enhanced the cell-adhesive activity of FN by potentiating the interaction of FN with integrin α5β1. In support of this conclusion, purified integrin α5β1 bound more avidly to $EDA^{+}$ FN than to $EDA^{−}$ FN. Augmentation of integrin binding by the EDA segment was, however, observed only in the context of the intact FN molecule, since the difference in integrin-binding activity between $EDA^{+}$ FN and $EDA^{−}$ FN was abolished after limited proteolysis with thermolysin. Consistent with this observation, binding of integrin α5β1 to a recombinant FN fragment, consisting of the central cell-binding domain and the adjacent heparin-binding domain Hep2, was not affected by insertion of the EDA segment. Since the insertion of an extra type III module such as EDA into an array of repeated type III modules is expected to rotate the polypeptide up to 180° at the position of the insertion, the conformation of the FN molecule may be globally altered upon insertion of the EDA segment, resulting in an increased exposure of the RGD motif in $III_{10}$ module and/or local unfolding of the module. Our results suggest that alternative splicing at the EDA exon is a novel mechanism for up-regulating integrin-binding affinity of FN operating when enhanced migration and proliferation of cells are required. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 139 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1997-10-06 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Alternative Splicing Fibronectins Genetics Physiology Animals Binding Sites CHO Cells Cell Adhesion Cell Membrane Cell Movement Drug Effects Cricetinae Fibroblasts Biosynthesis Fibrosarcoma Genetic Vectors Heparitin Sulfate Mice Molecular Sequence Data Peptide Fragments Recombinant Fusion Proteins Isolation & Purification Tumor Cells, Cultured Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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