Growth regulation of fibroblasts by thrombin, factor XIII and fibronectin

Bruhn, H. D.; Pohl, J.

doi:10.1007/bf01477357

Cited by 59 publications

(23 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…23 In FXIII-deficient mice, collagen synthesis was found to be downregulated. These data correspond to previous reports on control of fibroblast proliferation by FXIII 26 and its ability to regulate collagen synthesis in vitro. 8 In addition, FXIII provides cross-linking of fibrin and collagen fibers.…”

Section: Discussionsupporting

confidence: 92%

Factor XIII Deficiency Causes Cardiac Rupture, Impairs Wound Healing, and Aggravates Cardiac Remodeling in Mice With Myocardial Infarction

et al. 2006

View full text Add to dashboard Cite

Background-Identification of key molecular players in myocardial healing could lead to improved therapies, reduction of scar formation, and heart failure after myocardial infarction (MI). We hypothesized that clotting factor XIII (FXIII), a transglutaminase involved in wound healing, may play an important role in MI given prior clinical and mouse model data. Methods and Results-To determine whether a truly causative relationship existed between FXIII activity and myocardial healing, we prospectively studied myocardial repair in FXIII-deficient mice. All FXIII Ϫ/Ϫ and FXIII Ϫ/ϩ (FXIII activity Ͻ5% and 70%) mice died within 5 days after MI from left ventricular rupture. In contradistinction, FXIII Ϫ/Ϫ mice that received 5 days of intravenous FXIII replacement therapy had normal survival rates; however, cardiac MRI demonstrated worse left ventricular remodeling in these reconstituted FXIII Ϫ/Ϫ mice. Using a FXIII-sensitive molecular imaging agent, we found significantly greater FXIII activity in wild-type mice and FXIII Ϫ/Ϫ mice receiving supplemental FXIII than in FXIII Ϫ/Ϫ mice (PϽ0.05). In FXIII Ϫ/Ϫ but not in reconstituted FXIII Ϫ/Ϫ mice, histology revealed diminished neutrophil migration into the MI. Reverse transcriptase-polymerase chain reaction studies suggested that the impaired inflammatory response in FXIII Ϫ/Ϫ mice was independent of intercellular adhesion molecule and lipopolysaccharideinduced CXC chemokine, both important for cell migration. After MI, expression of matrix metalloproteinase-9 was 650% higher and collagen-1 was 53% lower in FXIII Ϫ/Ϫ mice, establishing an imbalance in extracellular matrix turnover and providing a possible mechanism for the observed cardiac rupture in the FXIII Ϫ/Ϫ mice. Conclusions-These data suggest that FXIII has an important role in murine myocardial healing after infarction.

show abstract

Section: Discussionsupporting

confidence: 92%

Factor XIII Deficiency Causes Cardiac Rupture, Impairs Wound Healing, and Aggravates Cardiac Remodeling in Mice With Myocardial Infarction

et al. 2006

View full text Add to dashboard Cite

show abstract

“…Fibronectin may de crease both the solubility and the breaking strength of fi brin gels as observed in nerve anastomoses [52]; it may inhibit fibrin polymerization and increase the thrombin clotting time in a concentration-dependent manner [53]. In addition, fibroblast proliferation may be inhibited by fibro nectin [3]. Finally, fibronectin was shown not to play a role in the angiogenic property of fibrin gels [7], Excess of albumin, by increasing fibrin solubility and favoring fine gel fibers [54], may interfere with fibrin gelation.…”

Section: Discussionmentioning

confidence: 99%

“…Thrombin-induced activation of fibrinogen results in the formation of a fibrin clot, such as occurs in the last step of the clotting cascade; the fibrin clot consolidates and adheres to the site of application. Factor XIII participates in the cross-linking and stabiliza tion of fibrin [1] and stimulates fibroblast growth [2,3]. Fibronectin may help to enhance fibroblast adhesion [4] and favor reepithelialization [5], but such a role is debated [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and Physical Properties of a Solvent-Detergent-Treated Fibrin Glue

Burnouf-Radosevich¹,

Burnouf²,

Huart³

1990

Vox Sanguinis

View full text Add to dashboard Cite

A fibrin glue preparation has been obtained from pooled human plasma using a procedure which includes a solvent-detergent (SD) treatment to inactivate lipid-enveloped viruses. The SD treatment inactivated ≥5.5 log(10) of HIV in less than 45 min, and ≥5 log(10) and ≥6.5 log(10) of VSV and Sindbis virus, respectively, in less than 2 h. The product was found to contain high quantities of fibrinogen (116±2.49 g/l; n = 12), factor XIII (35±2.88 U/ml) and von Willebrand factor (23±1.9 U/ml ristocetin cofactor activity), and relatively low levels of fibronectin (5.9±0.51 g/l). Plasminogen, the precursor of plasmin, which may play a negative role by decreasing the resistance of the fibrin clot, was at only 0.03 g/l. Cellulose acetate electrophoresis showed 95% gamma-proteins and 5% alpha-2-beta proteins. Sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions detected three main protein bands with apparent molecular weights of 65, 56 and 47 kilodaltons, probably corresponding to the alpha, beta, and gamma fibrinogen subunits. Other characteristics of the product included (1) high clottability of fibrinogen (over 85%); (2) absence of low molecular weight fibrin degradation products; (3) rapid solubilization at room temperature (less than 10 min); (4) high tensile strength (202±27 g/cm^2 after 2 h of application), and (5) high elasticity of the fibrin clot. In addition, scanning electron microscopy revealed a highly organized structure showing tridimensional arrangement of the fibrin fibers. SD treated fibrin glue should efficiently replace autologous fibrinogen or cryoprecipitate preparations for surgical application.

show abstract

“…Therefore, the question arises of whether the differential expression of FXIII would allow discrimination of RA from OA synovitis. FXIII is known to have important functions in crosslinking of coagulation proteins [5,10], in stimulation of fibroblast proliferation [26] and in inflammatory tissue matrix organization (Table 4).…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical detection of factor XIIIa and factor XIIIs in synovial membranes of patients with rheumatoid arthritis or osteoarthritis

Plenz

Fritz²,

König³

et al. 1996

Rheumatol Int

View full text Add to dashboard Cite

In spite of differences in etiology, RA and OA lead to astonishingly similar synovitic alterations. Fibroblastic transformation of the synovial membrane and an increase in monocytes constitute a rare but highly characteristic feature of RA. Monocytes synthesize factor (F) XIII, implying that FXIII (a and s) in synovial tissue might help to differentiate between RA and OA. Biopsies were obtained at open surgery from 98 unselected patients with the clinical diagnosis of RA (n = 54) or OA (n = 44). In a three-stage (ABC) immunoperoxidase technique, polyclonal antisera against factor XIIIa and factor XIIIs were investigated. Compared to OA sections. RA synovium showed more FXIIIa-positive cells-monocytes, fibrocytes, fibroblasts and synovial lining cells. In the subsynovial layer, band-like structure of FXIIIa-stained cells was observed in 27.8% of the RA patients, but in only one OA specimen. Higher proportions of FXIIIa-positive monocytes, macrophages, histiocytes and fibroblasts, as well as positive Langhans giant cells and vascular wall regions (except endothelial cells), were observed in RA. OA specimens revealed more intense FXIIIa labeling of these cells with a lower percentage of stained cells. Overall, labeling with FXIIIs antibody resulted in less intense staining. In conclusion, distinction between synovitis caused by RA and synovitis due to OA is possible, as the former show higher numbers of FXIIIa-positive cells, including monocytes, fibroblasts, fibrocytes and synovial lining cells. Further more, RA tissue is stained less intensely than OA tissue. There is evidence for continuous excretion of FXIII in the synovial membrane by the above-mentioned cell systems.

show abstract

Growth regulation of fibroblasts by thrombin, factor XIII and fibronectin

Cited by 59 publications

References 4 publications

Factor XIII Deficiency Causes Cardiac Rupture, Impairs Wound Healing, and Aggravates Cardiac Remodeling in Mice With Myocardial Infarction

Factor XIII Deficiency Causes Cardiac Rupture, Impairs Wound Healing, and Aggravates Cardiac Remodeling in Mice With Myocardial Infarction

Biochemical and Physical Properties of a Solvent-Detergent-Treated Fibrin Glue

Immunohistochemical detection of factor XIIIa and factor XIIIs in synovial membranes of patients with rheumatoid arthritis or osteoarthritis

Contact Info

Product

Resources

About