Cellular fibronectin is induced by epidermal growth factor, but not by dexamethasone or cyclic AMP in rat liver epithelial cells

Seebacher, Thomas; Manske, Marianne; Kornblihtt, Alberto R.; Bade, Ernesto G.

doi:10.1016/0014-5793(88)80556-8

Cited by 19 publications

(8 citation statements)

References 18 publications

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“…For example, bFGF was found to stimulate the proliferation of melanoblasts, without activating their differentiation pattern, when cultured in presence of dibutyryl cyclic AMP [93]. Conversely, EGF induced rat liver epithelial cell migration, but this activity was down-modulated by cyclic AMP and cholera toxin [94,95]. In the same situation, EGF also induced fibronectin expression.…”

Section: Determination Of Transduction Pathway Specificitymentioning

confidence: 95%

Modulations of the epithelial phenotype during embryogenesis and cancer progression

Savagner¹,

Boyer²,

Vallés³

et al. 1994

Cancer Treatment and Research

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Section: Determination Of Transduction Pathway Specificitymentioning

confidence: 95%

Modulations of the epithelial phenotype during embryogenesis and cancer progression

Savagner¹,

Boyer²,

Vallés³

et al. 1994

Cancer Treatment and Research

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“…The plasma form of Fn (pFn) is predominantly synthesized by hepatocytes, circulates in blood and deposits rapidly upon tissue injury to initiate hemostasis, this deposition process is independent of other hemostasis factors, such as fibrinogen, von Willebrand factor, β3 integrin, and platelet 30 . Cellular Fn (cFn) is mainly produced by fibroblast, to a lesser extent by other cells, such as epithelial cell 25 , macrophage 2 , and endothelial cells 20 . cFn contributes to support the extracellular structure framework by actively binding with cells and other matrix proteins as mentioned above.…”

Section: Introductionmentioning

confidence: 99%

Human plasma fibronectin promotes proliferation and differentiation of odontoblast

Tang¹,

Saito²

2017

J. Appl. Oral Sci.

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Objective To assess the effect of fibronectin (Fn) and porcine type I collagen (PCOL) on odontoblast-like cells in vitro.Material and Methods Rat odontoblast-like cells (MDPC-23 cells) were inoculated and cultured on Fn-coated or type I collagen-coated substrates. Proliferation assay, alkaline phosphatase activity (ALP activity), mRNA expression of hard tissue-forming markers, and Alizarin red staining were investigated over a period of 10 days.Results Cells maintained a high proliferation activity on Fn and PCOL even at a low seeding concentration (0.5×104/mL) as demonstrated by CCK-8 assay. The proliferation activity of cells on Fn increases in a concentration-dependent manner while it reached a plateau after 10 µg/mL. Cells adopted long, thin and spindle shape on Fn(10-50) and PCOL. Parallel actin filaments were observed in MDPC-23 cells cultured on Fn and PCOL. ALP activity was markedly up-regulated on Fn and PCOL-coated surfaces. Importantly, gene expression of BSP (Fn10: 2.44±0.32; Fn20: 3.05±0.01; Fn30: 2.90±0.21; Fn40: 2.74±0.30; Fn50: 2.64±0.12; PCOL: 2.20±0.03) and OCN (Fn10: 2.52±0.23; Fn20: 2.28±0.24; Fn30: 2.34±0.21; Fn40: 2.34±0.25; Fn50: 2.20±0.22; PCOL: 1.56±0.16) was significantly enhanced on Fn and PCOL substrates as compared with control; moreover, expression of integrin beta 1 (ITGB1), an ubiquitous cell surface receptor was augmented in Fn(10-50) and PCOL groups simultaneously. In accordance with the ALP activity and gene expression data, calcific deposition in cells grown on Fn(10-50) and PCOL was observed as well.Conclusion Despite the limitation of this study, the findings indicate that a surface coating of Fn enhances the proliferation, differentiation and mineralization of odontoblast-like cells by activation of integrin beta 1 (ITG B1). The promoting effects of Fn on MDPC-23 cells were achieved at a comparatively lower coating concentration than type I collagen (300 µg/mL). Specifically, it is suggested that the optimum coating concentration of Fn to be 10 µg/mL.

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“…Interestingly, it is known that HGF works through the PI3K cascade to increase levels of EDA FN (Magnuson et al, 1991;Seebacher et al, 1988;Blaustein et al, 2004), further implicating this signaling pathway in regulating alternative splicing of FN. Recent evidence suggests that cell-ECM interactions will alter levels of EDA FN.…”

Section: Eda Fn Inductive Pathwaysmentioning

confidence: 96%

EDA Fibronectin in Keloids Create a Vicious Cycle of Fibrotic Tumor Formation

Kelsh

McKeown‐Longo

Clark

2015

Journal of Investigative Dermatology

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During the early phase of wound healing, first plasma fibronectin (FN) and then in situ FN are deposited at the site of injury. In situ FN--FN made by tissue cells at the injury site--often contains an extra domain A (EDA) insert. Multiple wound-related signal transduction pathways control the deposition of EDA FN, and the EDA insert can in turn trigger pathways that induce inflammation, increased extracellular matrix molecule deposition including FN and collagen, and activation of fibroblasts. Together these pathways can create a vicious cycle that leads to fibrosis or keloid formation.

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Cellular fibronectin is induced by epidermal growth factor, but not by dexamethasone or cyclic AMP in rat liver epithelial cells

Cited by 19 publications

References 18 publications

Modulations of the epithelial phenotype during embryogenesis and cancer progression

Modulations of the epithelial phenotype during embryogenesis and cancer progression

Human plasma fibronectin promotes proliferation and differentiation of odontoblast

EDA Fibronectin in Keloids Create a Vicious Cycle of Fibrotic Tumor Formation

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