Fibrin gel structure and clotting time

Blombäck, Birger; Okada, Masahisa

doi:10.1016/0049-3848(82)90214-6

Cited by 168 publications

(106 citation statements)

References 27 publications

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“…2b, no plateau can be distinguished, giving the impression that translucent gels did not reach equilibrium. Fibrin gel opacity and structure are known to be affected by calcium and chloride contents, but have also been linked to ionic strength of the gelling solution [11,24]. In the present study, the effects of calcium and chloride cannot be discriminated from those of ionic strength, and no conclusion can be drawn on the direct effects of calcium or chloride on fibrin structure.…”

Section: Discussioncontrasting

confidence: 46%

Influencing biophysical properties of fibrin with buffer solutions

et al. 2010

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Fibrin has been proposed as cell scaffold for numerous tissue engineering applications. While most of the studies have focused on fibrinogen and thrombin, other components of fibrin can also affect its properties. The present study aimed to evaluate the effects of buffer solution composition on fibrin biophysical properties. Fibrin scaffolds were synthesized with different calcium, chloride, and factor XIII (FXIII) final concentrations. Light transmission was determined as a relative, semi-quantitative estimator of fiber structure differences, and two compositions, resulting in translucent and opaque gels, were tested for mechanical and biological properties. Gels were seeded with mouse mesenchymal cells, C3H10T1/2, or bovine bone marrow-derived mesenchymal stromal cells and cultured up to 10 or 24 days, before cell number, morphology and distribution were evaluated. Calcium increased gel opacity (i.e., fiber thickness), while chloride and FXIII decreased it. Opaque gels displayed a fluid-like viscous behavior while translucent gels showed improved elastic properties. Both compositions supported survival of both cell types with opaque gels leading to better proliferation, but significant scaffold shrinkage after 17 days of culture. These results demonstrated that calcium, chloride, and FXIII modulate the biophysical properties of fibrin, and can be used to adjust mechanical and biological properties for tissue engineering applications.

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Section: Discussioncontrasting

confidence: 46%

Influencing biophysical properties of fibrin with buffer solutions

et al. 2010

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“…ref. [148][149][150][151][152][153], and a number of more specialist coagulometric instruments based on optical (e.g. ref.…”

Section: The Clot Lifespan Modelmentioning

confidence: 99%

The simultaneous occurrence of both hypercoagulability and hypofibrinolysis in blood and serum during systemic inflammation, and the roles of iron and fibrin(ogen)

Kell

Pretorius

2014

Integrative Biology

127

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Although the two phenomena are usually studied separately, we summarise a considerable body of literature to the effect that a great many diseases involve (or are accompanied by) both an increased tendency for blood to clot (hypercoagulability) and the resistance of the clots so formed (hypofibrinolysis) to the typical, 'healthy' or physiological lysis. We concentrate here on the terminal stages of fibrin formation from fibrinogen, as catalysed by thrombin. Hypercoagulability goes hand in hand with inflammation, and is strongly influenced by the fibrinogen concentration (and vice versa); this can be mediated via interleukin-6. Poorly liganded iron is a significant feature of inflammatory diseases, and hypofibrinolysis may change as a result of changes in the structure and morphology of the clot, which may be mimicked in vitro, and may be caused in vivo, by the presence of unliganded iron interacting with fibrin(ogen) during clot formation. Many of these phenomena are probably caused by electrostatic changes in the iron-fibrinogen system, though hydroxyl radical (OH ) formation can also contribute under both acute and (more especially) chronic conditions. Many substances are known to affect the nature of fibrin polymerised from fibrinogen, such that this might be seen as a kind of bellwether for human or plasma health. Overall, our analysis demonstrates the commonalities underpinning a variety of pathologies as seen in both hypercoagulability and hypofibrinolysis, and offers opportunities for both diagnostics and therapies.

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“…The self-assembly of fibrin fibers is influenced by the concentration of fibrinogen, calcium and thrombin as well as other proteins [15]. While ionic strength and hydrogen ion concentration are important, clotting time is a dominant parameter in the determination of structure [16][17]. Increases in thrombin concentration are associated with faster gelation times [18][19], as well as characteristics of the gel microstructure such as fiber size and porosity.…”

Section: Introductionmentioning

confidence: 99%

Influence of thrombin concentration on the mechanical and morphological properties of cell-seeded fibrin hydrogels

2007

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Fibrin is a biopolymer that has been used in a variety of biomaterial, cell delivery and tissue engineering applications. The enzyme thrombin catalyzes the formation of fibrin microfibrils, which form a three-dimensional mesh in which cells can be directly embedded at the time of gel formation. In this study, fibrin hydrogels containing vascular smooth muscle cells were created using varying concentrations of thrombin. Over 7 days in culture, all gels decreased in volume as the fibrin matrix compacted, and the degree of gel compaction increased as thrombin concentration decreased. The material modulus and ultimate tensile stress of the gels also increased with decreasing thrombin concentration. Addition of thrombin to similar constructs made using collagen Type I did not show an effect on gel compaction or mechanical properties, suggesting that these effects were a result of thrombin's action on fibrin polymerization, and not cellular functions. Cell proliferation in fibrin hydrogels was not significantly affected by thrombin addition. Matrix examination using scanning electron microscopy showed increasing fibrin fiber diameters as thrombin concentration decreased. Confocal microscopic imaging of the actin cytoskeleton showed that cell morphology on twodimensional substrates of fibrin showed marked changes, with higher thrombin concentrations producing cells with longer cellular projections. However, these morphological changes were not as apparent in cells embedded in three-dimensional (3-D) matrices, in which cells exhibited a similar morphology independent of thrombin concentration. These results relate features of the matrix and cellular components of 3-D fibrin constructs to mechanical properties, and contribute to the understanding of structure-function relationships in cell-seeded, 3-D protein hydrogels.

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Fibrin gel structure and clotting time

Cited by 168 publications

References 27 publications

Influencing biophysical properties of fibrin with buffer solutions

Influencing biophysical properties of fibrin with buffer solutions

The simultaneous occurrence of both hypercoagulability and hypofibrinolysis in blood and serum during systemic inflammation, and the roles of iron and fibrin(ogen)

Influence of thrombin concentration on the mechanical and morphological properties of cell-seeded fibrin hydrogels

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