Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts.

Allen-Hoffmann, B. Lynn; Crankshaw, C L; Mosher, Deane F.

doi:10.1128/mcb.8.10.4234

Cited by 53 publications

(32 citation statements)

References 28 publications

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“…The ability of cells to up-and downregulate fibronectin polymerization (Ignotz and Massague, 1986;Allen-Hoffmann et al, 1988;Sommers and Mosher, 1993;Zhang et al, 1994Zhang et al, , 1999Zhong, 1998) thus provides cells with a novel mechanism for selectively altering cell-matrix adhesion structures and cell matrix signaling events.…”

Section: Discussionmentioning

confidence: 99%

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Fibronectin Polymerization Regulates the Composition and Stability of Extracellular Matrix Fibrils and Cell-Matrix Adhesions

Sottile

Hocking

2002

MBoC

546

510

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Remodeling of extracellular matrices occurs during development, wound healing, and in a variety of pathological processes including atherosclerosis, ischemic injury, and angiogenesis. Thus, identifying factors that control the balance between matrix deposition and degradation during tissue remodeling is essential for understanding mechanisms that regulate a variety of normal and pathological processes. Using fibronectin-null cells, we found that fibronectin polymerization into the extracellular matrix is required for the deposition of collagen-I and thrombospondin-1 and that the maintenance of extracellular matrix fibronectin fibrils requires the continual polymerization of a fibronectin matrix. Further, integrin ligation alone is not sufficient to maintain extracellular matrix fibronectin in the absence of fibronectin deposition. Our data also demonstrate that the retention of thrombospondin-1 and collagen I into fibrillar structures within the extracellular matrix depends on an intact fibronectin matrix. An intact fibronectin matrix is also critical for maintaining the composition of cell-matrix adhesion sites; in the absence of fibronectin and fibronectin polymerization, neither ␣5␤1 integrin nor tensin localize to fibrillar cell-matrix adhesion sites. These data indicate that fibronectin polymerization is a critical regulator of extracellular matrix organization and stability. The ability of fibronectin polymerization to act as a switch that controls the organization and composition of the extracellular matrix and cell-matrix adhesion sites provides cells with a means of precisely controlling cell-extracellular matrix signaling events that regulate many aspects of cell behavior including cell proliferation, migration, and differentiation. INTRODUCTIONExtracellular matrix remodeling plays an important role during development, wound healing, atherosclerosis, ischemic injury, and angiogenesis. Perturbing matrix remodeling by preventing the turnover of collagen I or by altering the levels of matrix-degrading proteases or protease inhibitors has been shown to result in fibrosis, arthritis, reduced angiogenesis, and developmental abnormalities (Liu et al., 1995;Vu et al., 1998;Holmbeck et al., 1999;Ducharme et al., 2000). In normal adult tissue, some extracellular matrix components such as elastin and fibrillar collagen have half lives of months to years (Krane, 1985;Debelle and Tamburro, 1999). Other extracellular matrix components, such as proteoglycans, thrombospondin-1 and -2, and vitronectin, can be endocytosed and degraded in the lysosomes (McKeownLongo et al., 1984;Yanagishita and Hascall, 1984; MurphyUllrich and Mosher, 1987;Hausser et al., 1992;Godyna et al., 1995a;Pijuan-Thompson and Gladson, 1997;Memmo and McKeown-Longo, 1998). Extracellular matrix molecules can also be degraded extracellularly by proteases such as matrix metalloproteinases (MMPs), plasminogen activators, and plasmin (Hynes, 1990;Marchina and Barlati, 1996;Shapiro, 1998).Recent data indicate that polymerized forms of extracellular matri...

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Section: Discussionmentioning

confidence: 99%

“…The ability of cells to up-and downregulate fibronectin polymerization (Ignotz and Massague, 1986;Allen-Hoffmann et al…”

Section: Discussionmentioning

confidence: 99%

Fibronectin Polymerization Regulates the Composition and Stability of Extracellular Matrix Fibrils and Cell-Matrix Adhesions

Sottile

Hocking

2002

MBoC

546

510

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“…It is also possible that binding of type I collagen to integrins or other collagen receptors initiates signaling independent of the ability of collagen to form fibrils. A variety of extracellular signals are known to regulate fibronectin matrix deposition (1,4,11,36,58,62,75). Hence, collagen-dependent cell signaling may influence the ability of cells to make matrix fibronectin fibrils; such collagen-dependent signaling would be lost in the cells lacking type I collagen but present in cells in which fibronectin-collagen interactions are blocked.…”

Section: Discussionmentioning

confidence: 99%

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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“…Matrix stiffness could be an underlying mediator of TGF-β-driven processes, such as the epithelial-to-mesenchymal transition in development and cancer cell metastasis. Fibronectin dynamics might be influenced by the mechanosensitive release of TGF-β given that stretch can expose fibronectin self-assembly sites (28,29) and that TGF-β affects both fibronectin synthesis and assembly (30,31). An intriguing possibility is that EDA-fibronectin, which is required in addition to TGF-β and matrix tension for myofibroblast differentiation, might be particularly sensitive to changes in stiffness.…”

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confidence: 99%

Matrix Elasticity, Cytoskeletal Tension, and TGF-β: The Insoluble and Soluble Meet

2008

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Soluble growth factors are potent regulators of normal and pathological processes. Mechanical factors are emerging as similarly important, but there has been no obvious mechanism linking the different factors. A recent report now demonstrates that cell-generated mechanical tension results in release of active transforming growth factor-β from stiff extracellular matrix, providing a mechanism for differentiation and maintenance of myofibroblasts in processes like fibrosis. More broadly, the work suggests that matrix stiffness could regulate the equilibrium between storage and release of a host of matrix-bound growth factors.The link between the tension generated by a cell and its physical and soluble microenvironments has long been a conundrum. Referring to muscle and its secreted soluble products, it was hypothesized by Starr more than a century ago that "...the active shortening of the fibre is due to an increase in the surface tension of the substance of the cell, caused by an increase in the proportional amount of the products of decomposition. Equilibrium is restored-after the stimulus which hastened the chemical changes has ceased-by a part of the products of decomposition finding their way into the blood-current...." (1) The problem has only broadened over the past 50 years with the discovery that most nonmuscle cells express muscle-like assemblies of actin and myosin-appropriately called stress fibers -and thereby also generate contractile tension (2). Understanding the interplay between cell contractility and cellular microenvironment became additionally complex with the recognition that the extracellular matrix serves not only as a scaffold for cells, but also as a local depot for growth factors that are potent regulators of cell tension (3). Hinz and co-workers now integrate these observations by demonstrating that cell-generated tension-depending on matrix elasticity-physically shifts the equilibrium between matrix binding and release of transforming growth factor-β (TGF-β), resulting in maintenance of the contractile phenotype (4).Cells sense their surroundings not through sight or sound but through the "smell" or "taste" of various soluble factors and the "touch" or "feel" of insoluble mechanical cues. Matrix elasticity is one of those cues, with an abundance of research over the last decade demonstrating that

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Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts.

Cited by 53 publications

References 28 publications

Fibronectin Polymerization Regulates the Composition and Stability of Extracellular Matrix Fibrils and Cell-Matrix Adhesions

Fibronectin Polymerization Regulates the Composition and Stability of Extracellular Matrix Fibrils and Cell-Matrix Adhesions

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

Matrix Elasticity, Cytoskeletal Tension, and TGF-β: The Insoluble and Soluble Meet

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