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Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin.

dc.contributor.author Xu, J
dc.contributor.author Bae, E
dc.contributor.author Zhang, Q
dc.contributor.author Annis, DS
dc.contributor.author Erickson, HP
dc.contributor.author Mosher, DF
dc.coverage.spatial United States
dc.date.accessioned 2011-06-21T17:31:26Z
dc.date.issued 2009
dc.identifier https://www.ncbi.nlm.nih.gov/pubmed/19119318
dc.identifier.uri https://hdl.handle.net/10161/4509
dc.description.abstract BACKGROUND: Fibronectin-null cells assemble soluble fibronectin shortly after adherence to a substrate coated with intact fibronectin but not when adherent to the cell-binding domain of fibronectin (modules (7)F3-(10)F3). Interactions of adherent cells with regions of adsorbed fibronectin other than modules (7)F3-(10)F3, therefore, are required for early display of the cell surface sites that initiate and direct fibronectin assembly. METHODOLOGY/PRINCIPAL FINDINGS: To identify these regions, coatings of proteolytically derived or recombinant pieces of fibronectin containing modules in addition to (7)F3-(10)F3 were tested for effects on fibronectin assembly by adherent fibronectin-null fibroblasts. Pieces as large as one comprising modules (2)F3-(14)F3, which include the heparin-binding and cell adhesion domains, were not effective in supporting fibronectin assembly. Addition of module (1)F3 or the C-terminal modules to modules (2)F3-(14)F3 resulted in some activity, and addition of both (1)F3 and the C-terminal modules resulted in a construct, (1)F3-C, that best mimicked the activity of a coating of intact fibronectin. Constructs (1)F3-C V0, (1)F3-C V64, and (1)F3-C Delta(V(15)F3(10)F1) were all able to support fibronectin assembly, suggesting that (1)F3 through (11)F1 and/or (12)F1 were important for activity. Coatings in which the active parts of (1)F3-C were present in different proteins were much less active than intact (1)F3-C. CONCLUSIONS: These results suggest that (1)F3 acts together with C-terminal modules to induce display of fibronectin assembly sites on adherent cells.
dc.language eng
dc.language.iso en_US
dc.publisher Public Library of Science (PLoS)
dc.relation.ispartof PLoS One
dc.relation.isversionof 10.1371/journal.pone.0004113
dc.subject Animals
dc.subject Cell Adhesion
dc.subject Cells, Cultured
dc.subject Fibronectins
dc.subject Focal Adhesions
dc.subject Humans
dc.subject Mice
dc.subject Mice, Knockout
dc.subject Peptide Fragments
dc.subject Recombinant Proteins
dc.subject Vinculin
dc.title Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin.
dc.title.alternative
dc.type Journal article
duke.contributor.id Erickson, HP|0114747
dc.description.version Version of Record
duke.date.pubdate 2009-1-1
duke.description.issue 1
duke.description.volume 4
dc.relation.journal Plos One
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/19119318
pubs.begin-page e4113
pubs.issue 1
pubs.organisational-group Basic Science Departments
pubs.organisational-group Biochemistry
pubs.organisational-group Cell Biology
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group School of Medicine
pubs.publication-status Published
pubs.volume 4
dc.identifier.eissn 1932-6203


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