The Influence of Fibrin Stabilizing Factor on the Growth of Fibroblats in vitro and Wound Healing

Beck, Eugene A.; Duckert, F; Ernst, Mary

doi:10.1055/s-0038-1654579

Cited by 120 publications

(40 citation statements)

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“…The abnormal scar formation in patients deficient in factor XIII 133,343, the effect of factor XIII on the growth of ~broblasts in celf culture [34] and the in vitro cross-linking of fibronectin to fibrin and collagen by factor XIII, indicate that e(y-glutamyl)lysyl amide bonds are of physiological importance not only between y-chains of fibrin but more generally in the matrix of connective tissue. The identification of a potential cross-linking site in plasma fibronectin should facilitate the isolation and characterization of cross-links formed in vivo to fibronectin.…”

Section: Resultsmentioning

confidence: 99%

Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin

et al. 1981

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Section: Resultsmentioning

confidence: 99%

Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin

et al. 1981

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“…Fibrin deposition is a common feature in wound healing and tissue repair and is typically associated to connective tissue fibroblast activation and proliferation [6]. On the other hand fibrinogen and fibrin constitute a substrate for fibroblast attachment and migration [7].…”

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confidence: 99%

Specific binding of human fibrinogen to cultured human fibroblasts

Dejana

Vergara-Dauden

Balconi

et al. 1984

European Journal of Biochemistry

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Highly purified human fibrinogen was labelled with radioactive iodine and its interaction with cultured human embryo lung fibroblasts (MRC5) was examined. The cell monolayer was incubated at 37" C with 1251-fibrinogen in phosphate/saline buffer containing 1 mM Ca2+ and 1 mM Mgzc. A direct interaction between 1251-fibrinogen and MRC5 was observed. The binding was time-dependent, reached saturation at 10 min and was regulated by the density of the cell monolayer. Non-labelled fibrinogen inhibited the interaction but unrelated proteins, including fibronectin, ovalbumin or myoglobin, did not. Monospecific Fab fragments, directed to fibrinogen, inhibited binding by 55.3 % at a 50/1 molar ratio while non-immune Fab produced a 1.5 % inhibition at similar concentration. Autoradiography of the display of fibroblast-bound 1251 on a 7.5 % polyacrylamide gel showed that the extract exhibited electrophoretic bands characteristic of the constitutive BP and y chains of the fibrinogen molecule. An apparent affinity constant, K, = 6.7 0.2 x lo6 M-', was estimated from binding isotherms. After a 30-min incubation time the interaction between '251-fibrinogen and the cells was completely reversible and displaceable by a large molar excess of non-labelled fibrinogen. When compared to fibroblasts (MRC5 or W138), cultures of human embryo epithelial cells (EUE) failed to interact with '251-fibrinogen, providing evidence for the specificity of binding for fibroblast monolayers. Plasmin-degradation fragments D and E, of 100000 and 50000 relative molecular mass respectively, were tested for their capacity to inhibit fibrinogen binding. At a 1/400 251-fibrinogen/fragment molar ratio, fragment E inhibited binding by 30 %while fragment D produced a 3 % inhibition only. Altogether, the results demonstrate that human fibroblasts possess specific binding sites for fibrinogen, which exhibit the characteristics of a receptor system regulated by the culture state ofithe cells. In addition the structural features, which are necessary for the interaction of fibrinogen with the cells, are probably located in the E domain of the molecule.Fibrinogen is a major plasma protein, involved in haemostatic and thrombotic disorders. It is a substrate for thrombin in the blood coagulation cascade and it is transformed into fibrin after a proteolytic activation by the enzyme. Fibrinogen is also essential in the initial haemostatic plug formation as it regulates platelet aggregation via its interaction with specific inducible receptors on the platelet membrane [l]. In addition several observations have implicated the molecule or its physiological derivatives in different cellular functions. This includes the immune response [2, 31, the acute-phase reaction [4] and cell proliferation [5]. A common mechanism for the participation of fibrinogen in these biological processes may involve a direct interaction of the molecule with surface-exposed or induced receptors.Fibroblasts are important in wound healing and play a role in the inflammatory response. Fibrin depositi...

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“…Secondary spontaneous pneumothorax in DPB is However, a large amount of coagulation factor XIII is needed to enhance wound healing 11,12 . Other reports have also recognized the beneficial effects of factor XIII replacement therapy in patients with acute therapy-resistant ulcerative colitis 13 and Crohn!s disease fistulas 14 .…”

Section: Discussionmentioning

confidence: 99%

The Treatment of Refractory Pneumothorax in Diffuse Panbronchiolitis by Intravenous Administration of Coagulation Factor XIII Concentrate

et al. 2006

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This case report presents a patient with advanced diffuse panbronchiolitis accompanied by chronic respiratory failure, marked cachexia, and refractory spontaneous pneumothorax.Because instillation of a pleurodesis agent and thoracoscopy were considered highly risky and invasive, we instead treated the patient with intravenous administration of a coagulation factor XIII concentrate, and the pneumothorax resolved. This case suggests refractory pneumothorax in a restrictive ventilatory disorder can be effectively treated with noninvasive intravenous administration of coagulation factor XIII concentrate.

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The Influence of Fibrin Stabilizing Factor on the Growth of Fibroblats in vitro and Wound Healing

Cited by 120 publications

References 0 publications

Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin

Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin

Specific binding of human fibrinogen to cultured human fibroblasts

The Treatment of Refractory Pneumothorax in Diffuse Panbronchiolitis by Intravenous Administration of Coagulation Factor XIII Concentrate

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The Influence of Fibrin Stabilizing Factor on the Growth of Fibroblats in vitro and Wound Healing

Cited by 120 publications

References 0 publications

Amino acid sequence of the factor XIIIa acceptor site in bovine plasma fibronectin

Amino acid sequence of the factor XIIIa acceptor site in bovine plasma fibronectin

Specific binding of human fibrinogen to cultured human fibroblasts

The Treatment of Refractory Pneumothorax in Diffuse Panbronchiolitis by Intravenous Administration of Coagulation Factor XIII Concentrate

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Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin

Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin