Fibronectin matrix polymerization regulates small airway epithelial cell migration

Hocking, Denise C.; Chang, Chien-Hsing

doi:10.1152/ajplung.00371.2002

Cited by 73 publications

(90 citation statements)

References 34 publications

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“…Hence, understanding how ECM molecules influence the deposition, stability, and organization of other ECM molecules and how these combinations of ECM molecules affect cell function is essential for understanding key aspects of cell behavior that underlie tissue morphogenesis, tissue repair, and maintenance of normal tissue function. We (32,78) and others (7,14,20,31,53) previously showed that fibronectin matrix can regulate adhesion-dependent cell growth, cell migration, and cell tension generation. In this report, we demonstrate that cells can organize and maintain a fibronectin matrix in the absence of fibrillar collagen I and that the interaction of fibronectin with collagen is critical for fibronectin-enhanced cell contractility.…”

Section: Discussionmentioning

confidence: 91%

“…Although these initial adhesive interactions are necessary for cell spreading and migration, ECM proteins elaborated by cells and organized into a fibrillar meshwork are also critical in regulating cell migration. For example, migration of FN null MF and airway epithelial cells is stimulated by cell-dependent fibronectin matrix polymerization (31). Similarly, SMC migration was shown to be regulated by cell-derived collagen (66).…”

Section: Discussionmentioning

confidence: 99%

“…Others have shown that addition of fibronectin to FN null MF or airway epithelial cells enhances cell migration (31). This increase in migration requires fibronectin deposition into the ECM (31).…”

Section: Characterization Of Collagen-binding Fibronectin Mutantmentioning

confidence: 98%

“…ECM fibronectin has been shown to stimulate cell growth and cell contractility and to enhance the migration of FN null MF and airway epithelial cells (31,32,77,78). Since collagen also has been shown to be an important modulator of cell phenotype (35,43,64,82,95), including cell migration (66,80), we asked whether fibronectin-dependent collagen deposition contributes to the migration-enhancing effects of fibronectin.…”

Section: Characterization Of Collagen-binding Fibronectin Mutantmentioning

confidence: 99%

“…Cells are known to respond in distinct ways to fibrillar ECM fibronectin compared with protomeric fibronectin. For example, matrix fibronectin promotes adhesion-dependent cell growth, modulates cell migration, and enhances cell contractility (16,31,32,53,77,78). Cells also respond in distinct ways to polymerized type I collagen gels and to thin coats of protomeric collagen (35,43,64).…”

mentioning

confidence: 99%

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Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Sottile

Shi²,

Rublyevska³

et al. 2007

American Journal of Physiology-Cell Physiology

150

178

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munication between cells and the extracellular matrix (ECM) is critical for regulation of cell growth, survival, migration, and differentiation. Remodeling of the ECM can occur under normal physiological conditions, as a result of tissue injury, and in certain pathological conditions. ECM remodeling leads to alterations in ECM composition and organization that can alter many aspects of cell behavior, including cell migration. The cell migratory response varies depending on the type, amount, and organization of ECM molecules present, as well as the integrin and proteoglycan repertoire of the cells. We and others have shown that the deposition of several ECM molecules, including collagen types I and III, depends on the presence and stability of ECM fibronectin. Hence, the effect of fibronectin and fibronectin matrix on cell function may partially depend on its ability to direct the deposition of collagen in the ECM. In this study, we used collagen-binding fibronectin mutants and recombinant peptides that interfere with fibronectin-collagen binding to show that fibronectindependent collagen I deposition regulates the cell migratory response to fibronectin. These data show that the ability of fibronectin to organize other proteins in the ECM is an important aspect of fibronectin function and highlight the importance of understanding how interactions between ECM proteins influence cell behavior. extracellular matrix; contractility CELL FATE DECISIONS involving cell growth, differentiation, and survival rely on the ability of cells to coordinate diverse input from cytokines, growth factors, and extracellular matrix (ECM) molecules (3,89,94). The effects of ECM molecules on cell behavior are particularly complicated, since they depend on the mixture of ECM molecules that are present, the way the ECM proteins are organized and presented to cells, and the presence of proteases, protease inhibitors, and endocytic mechanisms that can alter the levels of ECM proteins and ECM degradation products. Understanding how ECM proteins act in concert to elicit biological effects is key to understanding how cell-ECM interactions maintain normal tissue function and influence the cell response to tissue injury.There is much data showing that mixtures of different ECM molecules can have effects distinct from that of a single ECM molecule. For example, coating dishes with a combination of tenascin C and fibronectin results in altered expression of matrix metalloproteinases (MMPs) (86), whereas addition of tenascin C to dishes coated with fibrin and fibronectin results in altered cytoskeletal organization (90) compared with cells seeded in the absence of tenascin C. The ability of fibronectin null cells to produce a fibronectin matrix is also dependent on the combination of matrix proteins present on the substrate (4). Furthermore, mixed collagen and fibronectin substrates have been shown to alter the response of endothelial cells to shear stress compared with their response to fibronectin alone (59). Similarly, addition of soluble matric...

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Section: Discussionmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Section: Characterization Of Collagen-binding Fibronectin Mutantmentioning

confidence: 98%

Section: Characterization Of Collagen-binding Fibronectin Mutantmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Sottile

Shi²,

Rublyevska³

et al. 2007

American Journal of Physiology-Cell Physiology

150

178

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A comparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin

Zhang

Hekmatfer

Karuri

2013

J. Biomed. Mater. Res.

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The goal of our study was to compare the biological responses of cells cultured on polyethylene glycol (PEG) hydrogels functionalized with varying concentrations of the widely used adhesion peptide, RGD, and the cell-binding domain of fibronectin, III(9-10). We used Michael addition chemistry to covalently link cysteines in GRGDSPC and glutathione S-transferase (GST) tagged III(9-10) (GST-III(9-10)), to the acrylate groups in PEG diacrylate (PEGDA). Conjugation of GST-III(9-10) to PEGDA occurred through cysteine residues in GST. Ellman's reagent and immunoblotting studies demonstrated an efficiency of 90% or more for PEG conjugation of 1 μM GST-III(9-10) or GRDGSPC in 10% (wt/vol) PEGDA at 37°C for 1 h. Circular dichroism and limited proteolysis demonstrated that conjugating PEGDA to GST-III(9-10) did not significantly perturb its native secondary structure. Sodium dodecyl sulfate polyacrylamide gel electrophoresis characterization of the wash solution of PEG hydrogels after photopolymerization demonstrated that >95% of the 1 μM GST-III(9-10) was incorporated into the PEG hydrogels after cross-linking. PEG hydrogels derivatized with 1 μM GST-III(9-10) had significantly higher cell adhesion and spreading than PEG hydrogels with 1 μM GRGDSPC. A comparable adhesion response between GRGDSPC and GST-III(9-10) was obtained when the former was at millimolar and the latter at micromolar concentration. The amount and type of conjugate in the PEG hydrogel derivative was statistically more significant than hydrogel rigidity in stimulating the biological responses observed. This report presents new evidence of the robustness of III(9-10) in mediating cell adhesion and spreading on PEG hydrogels.

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Epithelial Repair and Regeneration

Brody

Atkinson

2008

Molecular Pathology Library

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Fibronectin matrix polymerization regulates small airway epithelial cell migration

Cited by 73 publications

References 34 publications

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

A comparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin

Epithelial Repair and Regeneration

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