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PubMed1990

Enhancement of fibrinolysis by bispecific monoclonal antibodies reactive to fibrin and plasminogen activators.

Murine hybrid hybridomas secreting bispecific monoclonal antibodies (bs mAbs) were constructed by fusing hybridomas secreting an anti-tissue plasminogen activator (tPA) or anti-urokinase (UK) mAb with hybridomas secreting a mAb which binds to human fibrin but not to fibrinogen. The bs mAbs reactive to both fibrin and PA (tPA or UK) were purified by affinity chromatography employing the respective antigen-coupled columns and characterized by fibrin-binding, amidolytic and fibrinolytic assays. Immunochemical conjugation of PAs and the bs mAbs did not impair the catalytic activity of PAs at all and made it possible to concentrate PAs on fibrin clot. Pretreatment of fibrin with the bs mAbs enhanced the fibrin-binding of PAs and the subsequent fibrinolysis.

Animals↗
PubMed1993

Shear dependence of the fibrin coagulation kinetics in vitro.

Fibrin thrombus formation, in vivo and in vitro, preferentially occurs in regions of retarded, recirculating flow which promote local variations of the distribution of blood components, e.g. thrombin, and shear rates. To better understand the effects of shear forces on the thrombin induced fibrin coagulation process the time course of fibrin formation in a fibrinogen/thrombin solution was studied for different shear rates gamma (0 s-1 < or = gamma < or = 500 s-1) and thrombin concentrations cthr (0.1 units/ml < or = cthr < or = 1.0 units/ml). The clotting curves at zero shear and the shear induced alterations of these curves could essentially be described in terms of a reaction kinetics defined by two rate coefficients k1, k2 which can be attributed to fibrinogen cleavage by thrombin and fibrin polymerisation, respectively. For cthr > approximately 0.5 units/ml and gamma > approximately 15 s-1 an additional mechanism, presumably fibrin breakage, had to be assumed. The rate coefficient k2 was markedly more affected by cthr and shear forces then was k1. The results fit well to the growth kinetics of fibrin thrombi formed in glass models of an arterial branching.

Animals↗
PubMed1994

Flow and antibody binding properties of hydrated fibrins prepared from plasma, platelet rich plasma and whole blood.

Previous studies, using cross-linked fibrin prepared from purified fibrinogen, showed low binding of a fibrin-specific monoclonal antibody designated T2G1 (Procyk et al., Blood 77:1469-75, 1991). In this study we investigated the binding of T2G1 and one other antibody to clots prepared from platelet poor plasma (PPP), platelet rich plasma (PRP) and whole blood. In contrast to our previous study, we used unlabelled antibodies and quantitated the level bound by ELISA, measuring antibody concentration in the non-adsorbed fraction. Antibody T2G1 bound 1.35 +/- 0.10 pmol/pmol fibrin (n = 11) to whole blood columns, 1.64 +/- 0.18 (n = 10) to PRP columns and 1.58 +/- 0.13 (n = 8) to PPP columns. The binding of T2G1 to columns made from purified fibrinogen was 0.78 +/- 0.05 pmol/pmol fibrin (n = 15). An antibody to a conformation-dependent epitope on Fragment D (Fd4-7B3) bound in comparable amounts to the different fibrins. Flow data show that whole blood columns, and also, but to a lesser extent those made with plasma, had a higher flow rate, permeability and fiber mass-length ratio than columns prepared from fibrinogen indicating a more coarse fibrin network. These data show that the presence of other proteins and blood cells, similar to what might occur in vivo, not only lead to an increase in the permeability of gels but also allow for better exposure of some epitopes.

Antibodies, Monoclonal↗
PubMed1994

Flow mediated fibrin thrombus formation in an endothelium-lined model of arterial branching.

In vivo arterial thrombosis occurs preferentially at curvatures and branchings, i.e. regions of flow separation and recirculation where blood is retained orders of magnitude longer than within straight vessel sections. To examine the effect of such disturbed flow on endothelial thromboresistance glass T-branchings lined with endothelial cells from human umbilical cord veins (HUVEC) were perfused with buffered fibrinogen solution (3mg/ml). The flow was adjusted to form a large recirculation zone and flow conditions were determined beforehand by means of flow visualization via dye injection as well as by laser ultramicroscope anemometry. Thrombus formation, which was registered on-line by video and evaluated planimetrically, was induced by injection of thrombin at concentrations ranging from 0.3 to 2.0 units/ml. Fibrin thrombus growth always began within the flow niche at the point of flow separation and extended downstream along the wall and into the vessel lumen finally occluding up to 80% of the lumen. Light and electron microscopy revealed that overall thrombus form as well as the orientation of single fibrin fibers were correlated strictly to the prevailing streamlines. Despite the integrity of the endothelial lining fibrin thrombus formation occurred. The fibrin fibers closely contacted the endothelial surface. These results indicate that recirculation zones promote fibrin thrombus formation sufficient to obstruct the vessel lumen and that intact endothelium alone is insufficient in preventing adhesion of fibrin to its surface.

Arteries↗
PubMed1980

Fibroblast adhesion to fibrinogen and fibrin substrata: requirement for cold-insoluble globulin (plasma fibronectin).

We carried out experiments to determine conditions for fibroblast adhesion to fibrinogen and fibrin substrata. Baby hamster kidney (BHK) cells did not attach to substrata composed of purified fibrinogen or fibrin. When cold-insoluble globulin (CIG) (plasma fibronectin) was bound to fibrinogen or fibrin substrata, adhesion of BHK sells was observed and the extent of adhesion was dependent upon the CIG conecntration. Binding of CIG to fibrinogen or fibrin substrata in the presence of Factor XIII (factor) under covalent crosslinking conditions resulted in a marked increased in the ability of the substrata to support cell adhesion. Control experiments indicated that CIG formed the sites on the fibrinogen and fibrin substrata to which the cells were attaching. In addition, the effect of factor XIII was shown to require covalent crossliking of CIG to the fibrinogen or fibrin, which involved a glutamine residue on the CIG molecule and could be prevented by prior crosslinking of CIG with putrescine or with itself. The enhanced ability of Factor XIII-crosslinked CIG substrata to support cell adhesion could not be accounted for by the absolute amount of CIG bound to the substrata. We present in this paper the possibility that the orientation of CIG on the substrata is the critical factor.

Animals↗
PubMed1995

The morphologic change of endothelial cells by ancrod-generated fibrin is triggered by alpha v beta 3 integrin binding and the subsequent activation of a G-protein coupled phospholipase C.

The mechanism of morphologic change of human cultured umbilical vein endothelial cells (HUVECs) caused by fibrin was investigated. Ancrod, a thrombin-like enzyme, did not cause morphologic alteration of HUVEC by itself at concentrations ranging from 0.01 to 10 U/ml. However, when 0.02 U/ml of ancrod was added to cultured HUVEC monolayers in the presence of citrated plasma, it caused pronounced morphologic change of HUVEC after 6-10 h incubation period. Gly-Pro-Arg-Pro (4 mg/ml), an inhibitor of fibrin polymerization, prevented the morphologic alteration, indicating that the morphologic alteration was caused by the polymerized fibrin. The morphologic change of HUVEC caused by ancrod-generated fibrin was not observed in the presence of an intracellular calcium mobilization inhibitor TMB-8 (50 microM), and the morphologic alteration was also less pronounced with BAPTA(15 microM)-loaded HUVECs and HUVECs pretreated with EGTA (1.2 mM). Ancrod (in Medium 199) itself did not stimulate phosphoinositide breakdown of HUVEC. However, when ancrod was present in plasma, it caused an increase of [3H]IP1 of HUVECs preloaded with [3H]myoinositol. This IP1 increment was inhibited by Gly-Pro-Arg-Pro. The increase of IP1 was significantly inhibited by the pretreatment of monoclonal antibodies 23C6 and 7E3 directed against alpha v beta 3 integrin. Neomycin (1 mM) and pertussis toxin (100 ng/ml), but not aspirin or mepacrine, blocked this enhanced phosphoinositide breakdown. The morphologic change was also prevented by the monoclonal antibodies, 23C6 and 7E3. These results suggest that both intra- and extra-cellular calcium participate in the event of morphologic change of HUVEC caused by ancrod-generated fibrin, and the morphologic change is mediated, at least in part, by fibrin binding to integrin alpha v beta 3 on HUVECs, causing the subsequent activation of the endogenous G-protein coupled phospholipase C.

Ancrod↗
PubMed1998

Endoscopic sclerotherapy with fibrin glue as compared with polidocanol to prevent early esophageal variceal rebleeding.

BACKGROUND/AIMS: Endoscopic sclerotherapy is of proven benefit for patients after esophageal variceal bleeding, but is associated with substantial local and systemic complications. Since fibrin glue is a promising agent for endoscopic sclerotherapy of esophageal varices, we compared its safety and efficacy in patients after esophageal variceal bleeding. PATIENTS AND METHODS: In a randomized, controlled trial, 36 patients with an acute episode of variceal bleeding were endoscopically treated with either polidocanol (18 patients) or fibrin glue (18 patients) by intravariceal injections within 12 h of admission. Tissue compatibility, incidence of various complications, episodes of rebleeding and overall survival rates were investigated. RESULTS: Rebleeding, especially from enrollment to day 28, was less common in the fibrin group (p=0.046), and all patients treated with fibrin glue survived for more than 28 days, whereas five patients treated with polidocanol died within this period. The incidence of sclerotherapy-induced ulcers was significantly lower in the fibrin group than in the polidocanol group (p=0.001), and major complications such as perforation or ulcer bleeding were observed only in the polidocanol group. There were no complications in any group due to activation of systemic coagulation, fibrinolysis or clinically relevant pulmonary embolization. CONCLUSIONS: We conclude that fibrin glue is an efficient and safe agent for endoscopic sclerotherapy of bleeding esophageal varices, especially in the immediate posthemorrhagic period.

Aged↗
PubMed1984

Fibrinogen and fibrin in strong magnetic fields. Complementary results and discussion.

When fibrin polymerizes in a strong magnetic field, it can be highly oriented. The structural diffraction study of the oriented polymer becomes thus possible. The magnetic birefringence can also be used to study the development of the polymer Fibrinogen in solution is weakly oriented in high magnetic fields. In this work we present complementary results and discussion. The validity of the comparison of the orientation parameters of fibrinogen and fibrin with those of other orientable known biological structures is discussed. The orientation of fibrin formed from fibrin monomer solution is compared to that of fibrin formed by the action of thrombin on fibrinogen. The conditions to obtain highly oriented fibrin gels suitable for three dimensional structure studies are also briefly discussed.

Animals↗
PubMed1985

Effects of semi-dilute actin solutions on the mobility of fibrin protofibrils during clot formation.

Low concentrations of actin filaments (F-actin) inhibit the rate and extent of turbidity developed during polymerization of purified fibrinogen by thrombin. Actin incorporates into the fibrin clot in a concentration-dependent manner that does not reach saturation, indicating nonspecific trapping of actin filaments in the fibrin network. Actin does not retard activation of fibrinogen by thrombin, but rather the alignment of fibrin protofibrils into bundles which constitute the coarse clot. In contrast, equivalent F-actin concentrations have little or no effect on the turbidity of plasma clots. The difference is attributed to the presence of a plasma protein, gelsolin, that severs actin filaments. Purified gelsolin greatly reduces the effect of F-actin on the turbidity of a pure fibrin clot and decreases the fraction of actin incorporated by the clot. A calculation of the extent to which the gelsolin concentrations used in these experiments reduce the fraction of actin filaments which are long enough to impede each other's rotational diffusion indicates that it is the overlapping actin filaments which retard the association of fibrin protofibrils. The findings suggest that one role for the F-actin depolymerizing and particularly actin severing activities in blood is to prevent actin filaments released by tissue injury from interfering with the formation of coarse fibrin clots.

Actins↗
PubMed1992

Plasminogen binding by alpha 2-antiplasmin and histidine-rich glycoprotein does not inhibit plasminogen activation at the surface of fibrin.

alpha 2-antiplasmin (alpha 2-AP) exerts its inhibitory effect on fibrinolysis by rapidly inhibiting the plasmin evolved; in addition, it has been suggested that interference with the binding of plasminogen to fibrin, a function shared with histidine-rich glycoprotein (HRGP), may also be significant in inhibition of fibrinolysis. To elucidate if plasminogen binding by these two alpha 2-globulins may decrease the generation of plasmin by tissue-type plasminogen activator (t-PA) at the surface of fibrin, a system mimicking the fibrin/plasma interface was used. Attempts were made to differentiate the plasminogen binding from the plasmin inhibitory function of alpha 2-AP. The activation of human Glu-plasminogen (native plasminogen with NH2-terminal glutamic acid) by fibrin-bound t-PA was performed in a plasma environment using either normal plasma, alpha 2-AP- or HRGP-depleted plasmas supplemented with increasing amounts of the lacking protein, or in a reconstituted system with purified plasminogen and various concentrations of alpha 2-AP and HRGP. The activation of Glu-plasminogen in alpha 2-AP-depleted plasma containing a normal concentration of HRGP produced a time-dependent increase in the generation of plasmin. The addition of 1 microM-alpha 2-AP to this plasma prevented the formation of Lys-derivatives and produced a marked decrease (42%) in the number of plasminogen-binding sites. In contrast, the addition of 1.5 microM-HRGP to HRGP-depleted plasma containing a normal amount of alpha 2-AP produced only a modest (17%) decrease in the amount of plasmin(ogen) bound. Moreover, in a purified system the amount of plasminogen-binding sites and thereby of plasmin generated at the surface of fibrin in the presence of both alpha-2 globulins was similar to the amount generated in the presence of alpha 2-AP alone. These results indicate clearly that the formation of reversible complexes between plasminogen and alpha 2-AP does not interfere with the binding and activation of plasminogen at the fibrin surface. In contrast, the inhibition of plasmin by alpha 2-AP decreases importantly the number of plasminogen-binding sites (carboxyl-terminal lysines) and inhibits thereby the accelerated phase of fibrinolysis. It can be concluded that interference of the binding of plasminogen to fibrin by alpha 2-AP during plasminogen activation, does not play a significant role in inhibition of fibrinolysis, and that the plasminogen-binding effect of HRGP, if any, is obscured by the important inhibitory effect of alpha 2-AP.

Biotransformation↗
PubMed1994

Polymeric stenting in the porcine coronary artery model: differential outcome of exogenous fibrin sleeves versus polyurethane-coated stents.

OBJECTIVES: In a porcine coronary model, fibrin film soaked for 3 h in heparin was used as a circumferential coating on a tantalum stent to assess the effect of this naturally occurring biopolymer on arterial healing. The results were compared with those obtained with medical grade polyurethane-coated stainless steel stents. BACKGROUND: Thrombus plays an important role in healing after arterial injury and may affect the development of neointimal hyperplasia. Manipulation of the initial thrombus may alter the healing response. To study this, we placed a template of fibrin in a porcine coronary artery restenosis model. METHODS: Thirty-four fibrin film stents were delivered in 20 swine. Oversizing was avoided, to prevent deep arterial injury, by placement of optimally sized stents. Initial patency of the stented vessel was confirmed by angiography. RESULTS: Three fibrin-stented swine died within 48 h; in each, the stent was occluded with a fibrin/red blood cell mass. In two of these three, a portion of the exogenous fibrin had become detached from the stent and partially occluded the lumen. Of the remaining 31 stents, all were patent at elective sacrifice at 28 days. Eighty-four percent had a diameter stenosis < 50%, and the mean (+/- SD) diameter stenosis was 32.3 +/- 13%. There was no evidence of significant foreign-body giant-cell reaction. These results contrasted with the medical grade polyurethane-coated stents placed according to the same protocol without oversizing. Twelve of these stents were placed; six swine died of thrombotic occlusion within the 1st 48 h. At elective sacrifice at 28 days, the remaining polyurethane-coated stents were occluded by marked neointimal hyperplasia. CONCLUSIONS: Fibrin film-coated stents seem promising as a template for modifying the local response to arterial injury and for potentially decreasing restenosis rates.

Animals↗
PubMed1992

Autologous fibrin glue--preparation and clinical use in thoracic surgery.

Autologous fibrin glue was used in 20 patients undergoing lung resection to reduce pulmonary air leaks and improve hemostasis. The fibrinogen in the glue was prepared by ethanol precipitation of plasma separated from 88 ml of the patient's blood. The mean volume of fibrinogen concentrate +/- SD was 4.9 +/- 0.5 ml with a fibrinogen concentration of 28 +/- 5 mg/ml. The yield obtained by the separation was 81% +/- 9%. One part of fibrinogen concentrate was converted to solid fibrin by means of 0.3 parts of thrombin solution. The outcome was 6.4 ml of two-component fibrin glue. The preparation was performed in a closed system to ensure sterility, and was completed within 90 min. Pulmonary air leak decreased following sealing of the resection lines with autologous fibrin glue and the hemostasis was effective. No adverse effects were observed, and all cultures from the glue were negative. Autologous fibrin glue has the obvious advantages of safety from transmission of viral diseases and from immunological reactions. In summary, we report a new technique for preparing autologous fibrin glue with a high concentration of fibrinogen making it a safe and effective sealant of pulmonary air leak and hemostatic agent in thoracic surgery.

Blood Transfusion, Autologous↗
PubMedDate not supplied

Effects of gliclazide on fibrin network.

Fibrin network structure is altered by diabetes, peripheral vascular disease, and by some drugs. The antidiabetic drug, gliclazide, increases fibrin fiber thickness but reduces whole network permeability. The networks are, however, more lysable. These effects are further examined in this study using electron microscopy. Changes were observed in protein concentrations in fibrin fibers, in fibrin fiber alignment and in fiber porosity. These results show that gliclazide modifies fibrin monomer polymerization so that the fibrin network is rendered more susceptible to fibrinolysis. This pharmacological action of gliclazide may be useful in the treatment of thromboembolism.

Fibrin↗
PubMed2006

Long-term stable fibrin gels for cartilage engineering.

It is essential that hydrogel scaffold systems maintain long-term shape stability and mechanical integrity for applications in cartilage tissue engineering. Within this study, we aimed at the improvement of a commercially available fibrin gel in order to develop a long-term stable fibrin gel and, subsequently, investigated the suitability of the optimized gel for in vitro cartilage engineering. Only fibrin gels with a final fibrinogen concentration of 25mg/ml or higher, a Ca(2+) concentration of 20mm and a pH between 6.8 and 9 were transparent and stable for three weeks, the duration of the experiment. In contrast, when preparing fibrin gels with concentrations out of these ranges, turbid gels were obtained that shrank and completely dissolved within a few weeks. In rheological characterization experiments, the optimized gels showed a broad linear viscoelastic region and withstood mechanical loadings of up to 10,000 Pa. Bovine chondrocytes suspended in the optimized fibrin gels proliferated well and produced the extracellular matrix (ECM) components glycosaminoglycans and collagen type II. When initially seeding 3 million cells or more per construct (5mm diameter, 2mm thick), after 5 weeks of culture, a coherent cartilaginous ECM was obtained that was homogenously distributed throughout the whole construct. The developed fibrin gels are suggested also for other tissue engineering applications in which long-term stable hydrogels appear desirable.

Animals↗
PubMed2007

Thrombin generation and fibrin clot structure.

Generation of a hemostatic clot requires thrombin-mediated conversion of fibrinogen to fibrin. Previous in vitro studies have demonstrated that the thrombin concentration present at the time of gelation profoundly influences fibrin clot structure. Clots formed in the presence of low thrombin concentrations are composed of thick fibrin fibers and are highly susceptible to fibrinolysis; while, clots formed in the presence of high thrombin concentrations are composed of thin fibers and are relatively resistant to fibrinolysis. While most studies of clot formation have been performed by adding a fixed amount of purified thrombin to fibrinogen, clot formation in vivo occurs in a context of continuous, dynamic changes in thrombin concentration. These changes depend on the local concentrations of pro- and anti-coagulants and cellular activities. Recent studies suggest that patterns of abnormal thrombin generation produce clots with altered fibrin structure and that these changes are associated with an increased risk of bleeding or thrombosis. Furthermore, it is likely that clot structure also contributes to cellular events during wound healing. These findings suggest that studies explicitly evaluating fibrin formation during in situ thrombin generation are warranted to explain and fully appreciate mechanisms of normal and abnormal fibrin clot formation in vivo.

Blood Coagulation↗
PubMed2004

Modes and consequences of thrombin's interaction with fibrin.

Thrombin mediates the balance between coagulant and fibrinolytic forces and has numerous cellular effects. This intricate balance is maintained by biochemical mechanisms that regulate thrombin activity. Disruption of this balance could lead to bleeding or thrombosis. Once thrombin is generated, two major mechanisms regulate its activity. By binding fibrin, thrombin's activity is localized to the thrombus, a process that limits its systemic procoagulant effects. Thrombin that escapes into the circulation is efficiently inactivated by plasma inhibitors, such as antithrombin, or is sequestered by thrombomodulin on the endothelium. Although thrombin's interaction with fibrin limits its systemic effects, fibrin-bound thrombin resists inactivation and can produce a local procoagulant stimulus that triggers thrombus growth. Direct thrombin inhibitors were developed, at least in part, to target fibrin-bound thrombin. These agents are finding their niche for the prevention and treatment of venous and arterial thrombosis. The mechanisms by which thrombin binds fibrin are reviewed in this paper. As well, the potential pathological consequences of thrombin's interaction with fibrin are discussed.

Fibrin↗
PubMed2005

Endothelial cell proliferation and progenitor maturation by fibrin-bound VEGF variants with differential susceptibilities to local cellular activity.

A number of vascular therapies could benefit from advanced methods for presentation of angiogenic growth factors, including growth of endothelium on small caliber vascular grafts and revascularization of ischemic tissue through induction of collateral vessels and microvessels. To explore methods to optimize the presentation and release of angiogenic factors in such applications in device integration and tissue repair, we studied three variant forms of vascular endothelial growth factor 121 (VEGF121), each with differential susceptibility to local cellular proteolytic activity, formulated within fibrin matrices. (1) The prototypic variant alpha2PI(1-8)-VEGF121 remains immobilized in fibrin matrices until its liberation by cell-associated enzymes, such as plasmin, that degrade the fibrin network [slow, cell-demanded release; J. Control. Release 72 (2001) 101-113]; the alpha2PI(1-8) domain serves as a site for covalent attachment to fibrin during coagulation. (2) We created a new VEGF variant, alpha2PI(1-8)-Pla-VEGF121 that couples to fibrin via a plasmin-sensitive sequence (Pla). Cleavage of this target site by plasmin enables direct release of alpha2PI(1-8)-Pla-VEGF121 from bulk matrix degradation (accelerated, cell-demanded release). (3) Native VEGF121 (burst, passive release) was considered as a reference. VEGF release profiles were determined experimentally as well as mathematically, alpha2PI(1-8)-Pla-VEGF121 being released ca. fourfold more quickly than alpha2PI(1-8)-VEGF121, both being retained compared to native VEGF121; the differences in release could be accounted for based on knowledge of the plasmin sensitivity of the bound growth factor and the structure of the fibrin network. The bound factors were competent in inducing endothelial cell proliferation, the matrix-bound forms being more effective than native VEGF121; as well as competent in inducing endothelial progenitor cell maturation into endothelial cells. These matrix-bound variants of VEGF121 may be particularly useful where retention in locally applied surgical sites is desired, such as prevention of washout from vascular graft coatings and slowing loss from tissue ingrowth matrices used in local tissue revascularization and repair.

Cell Proliferation↗
PubMed2004

Therapeutic application of tissue plasminogen activator for fibrin reaction after cataract surgery.

PURPOSE: To evaluate the efficacy and safety of therapeutic application of recombinant tissue plasminogen activator (rtPA) for fibrin reaction after uneventful cataract surgery. SETTING: Department of Ophthalmology, SSK Istanbul Hospital, Istanbul, Turkey. METHOD: In a prospective study between January and June 2000, 26 eyes of 26 patients with fibrin reaction after uneventful cataract surgery received 3 microg of intracameral rtPA. Patients were evaluated for recurrences of fibrin reaction or complications by slitlamp biomicroscopy 2, 12, and 24 hours, 1 week, and 1 and 6 months after rtPA application. Intraocular pressure (IOP) was measured by Goldmann applanation tonometry. Visual acuity was tested using a standard Snellen chart 1 week after rtPA application. RESULTS: All 26 eyes had complete fibrinolysis. Three eyes (11.5%) had corneal edema that lasted fewer than 24 hours. Visual acuity improved by 0 to 7 lines in 19 patients (73.1%). No patient had an increase in IOP. At 6 months, no patient had hyphema or recurrence of fibrin reaction. CONCLUSIONS: Complete lysis of fibrin after cataract surgery with conventional topical medications can take a long time and is not successful in some patients. Intracameral application of 3 microg rtPA was an efficient, safe method for the treatment of fibrin reaction after cataract surgery.

Female↗