TGF‐β1 stimulates cultured human fibroblasts to proliferate and produce tissue‐like fibroplasia: A fibronectin matrix‐dependent event

Clark, Richard A.F.; McCoy, Georgia A.; Folkvord, Joy M.; McPherson, John M.

doi:10.1002/(sici)1097-4652(199701)170:1<69::aid-jcp8>3.3.co;2-2

Cited by 23 publications

(27 citation statements)

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Section: Introductionmentioning

confidence: 99%

“…Our data indicate that fibronectin deposition into the extracellular matrix increases adhesiondependent cell growth and cell contractility . Others have shown that inhibiting fibronectin deposition or disrupting a preexisting fibronectin matrix can inhibit adhesion-dependent (Clark et al, 1997;Bourdoulous et al, 1998;Mercurius and Morla, 1998) and -independent cell growth (Wu et al, 1998).Remodeling of the extracellular matrix by proteases promotes cell migration, a critical event in the formation of new vessels. Remodeling of the extracellular matrix could alter the cell response to extracellular matrix by production of fragments of matrix proteins with distinct properties from the native proteins.…”

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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

536

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: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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

Sottile

Hocking

2002

MBoC

536

510

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“…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).…”

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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

149

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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“…A number of in vitro studies based on fibroblast proliferation have been produced that elucidate the effects of different agents as wound healing promoters (19,20). Measurement of cell viability and proliferation forms the basis for numerous in vitro assays of a cell population's response to external factors.…”

Section: Discussionmentioning

confidence: 99%

The effect of Malaysian honey and its major components on the proliferation of cultured fibroblasts

Aljadi¹,

Enchang²,

Yusoff³

2014

Turk J Med Sci

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Background/aim: To examine, for the first time, the effect of a selected Malaysian honey and its major components on the proliferation of cultured fibroblasts. Materials and methods:Honey and some of its components, which include the sugars, the proteins, the hydrogen peroxide produced, and the phenolics, were exposed to cultured fibroblasts. The MTT colorimetric assay was used to assess cell viability and proliferation. Results:The stimulatory effect of honey on fibroblast proliferation was observed to be time-and dose-dependent. The continuous production of hydrogen peroxide by the honey-glucose oxidase system also acts to stimulate cell proliferation in a time-and dosedependent manner. The presence of phenolics with antioxidant properties, on the other hand, renders protection to the cells against the toxic effect of hydrogen peroxide. However, the presence of a growth factor-like substance in honey could not be ascertained. Conclusion:For the first time, honey and its major components were shown to exert stimulatory effects on cultured fibroblasts. Honey is therefore potentially useful in medicinal practices.

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TGF‐β1 stimulates cultured human fibroblasts to proliferate and produce tissue‐like fibroplasia: A fibronectin matrix‐dependent event

Cited by 23 publications

References 0 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

The effect of Malaysian honey and its major components on the proliferation of cultured fibroblasts

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