Calcium and fibrin gel structure

Okada, Masahisa; Blombäck, Birger

doi:10.1016/0049-3848(83)90039-7

Cited by 77 publications

(64 citation statements)

References 20 publications

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“…As one might expect, changes in ionic strength decrease the clot pore size. 149,380,381 As one would also expect from Debye-Hückel theory, it binds divalent cations such as Ca 2+ 380,392,398,399 and Zn 2+ 404 ; the trivalent iron ion is especially effective. 389,406 It has also been suggested that added ferric iron can carry out Fenton chemistry by reacting with peroxide that may be formed in a variety of ways.…”

Section: Electrostatic Considerationsmentioning

confidence: 99%

“…378 On simple kinetic grounds alone, changes in the fibrinogen concentration might be expected to have significant effects on the nature of the clot, and this is indeed observed, 34,113,126,238,292,379 with, for instance, higher fibrinogen concentrations leading to faster clotting times and hence 148 smaller clot pores. 149,380,381 In addition to changes in fibrinogen levels, one might suppose that changes in the fibrinogen molecule itself would have substantial effects, and this too is found. In one very nice study, a common variant BbArg448Lys in the C-terminal region of the fibrinogen betachain had major effects on the nature of the clot, 192 and the fact that this was also true for recombinant protein implied that the changes were due to interactions with substances in the blood itself.…”

Section: Effects Of Fibrinogen Concentration On the Nature Of The Clotmentioning

confidence: 99%

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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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Section: Electrostatic Considerationsmentioning

confidence: 99%

Section: Effects Of Fibrinogen Concentration On the Nature Of The Clotmentioning

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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“…Fibronectin can inhibit fibrin cross-linking and lead to the formation of soluble fibrin. [74][75][76] Cross-linking of fibronectin to fibrin can alter the mechanical properties [76][77][78] of the clot and promote cellular adherence as well as migration of cells into the clot. 79 This may be important to facilitate the wound healing process.…”

Section: Fibronectinmentioning

confidence: 99%

Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms

Ariëns

Lai

Weisel

et al. 2002

Blood

327

272

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Factor XIII and fibrinogen are unusual among clotting factors in that neither is a serine protease. Fibrin is the main protein constituent of the blood clot, which is stabilized by factor XIIIa through an amide or isopeptide bond that ligates adjacent fibrin monomers. Many of the structural and functional features of factor XIII and fibrin(ogen) have been elucidated by protein and gene analysis, site-directed mutagenesis, and x-ray crystallography. However, some of the molecular aspects involved in the complex processes of insoluble fibrin formation in vivo and in vitro remain unresolved. The findings of a relationship between fibrinogen, factor XIII, and cardiovascular or other thrombotic disorders have focused much attention on these 2 proteins. Of particular interest are associations between common variations in the genes of factor XIII and altered risk profiles for thrombosis. Although there is much debate regarding these observations, the implications for our understanding of clot formation and therapeutic intervention may be of major importance. In this review, we have summarized recent findings on the structure and function of factor XIII. This is followed by a review of the effects of genetic polymorphisms on protein structure/function and their relationship to disease. (Blood. 2002;100:743-754)

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“…In the course of an extensive study on calcium ions binding to fibrin during clot formation, Mihalyi showed that there is an uptake of Ca 2+ that runs parallel to FPB release, while FPA is released largely during its lag period (46). Overall, calcium ions are known to accelerate the fibrinogen-fibrin transition promoted by thrombin, decreasing the clotting time (2,45).…”

mentioning

confidence: 99%

Kinetics of Fibrinopeptide Release by Thrombin as a Function of CaCl₂ Concentration: Different Susceptibility of FPA and FPB and Evidence for a Fibrinogen Isoform-Specific Effect at Physiological Ca²⁺ Concentration

et al. 2003

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The kinetics of release of fibrinopeptide A (FPA) and B (FPB) by thrombin were investigated on unfractionated fibrinogen samples as a function of CaCl 2 concentration. A 50 mM Tris, 104 mM NaCl, pH 7.4 (TBS) buffer, to which 1 mM EDTA-Na 2 (TBE) or 2.5 (TBC2.5), 14 (TBC14), and 30 mM CaCl 2 (TBC30) was alternatively added, was employed. The % FPA versus time curves were fitted with single stretched-exponential growth functions, where the stretch parameter likely reflects substrate polydispersity ( ) 1, monodisperse). For TBE, TBS, TBC14, and TBC30, we found ≈ 1, with corresponding normalized rate constants (K a ) of 3.8, 4.2, 2.7, and 1.9 × 10 -5 [(NIHu/L)s] -1 . Surprisingly, in TBC2.5 we found ) 0.69, with an "average" K a of 3.} with an increase in the ionic strength I to that of TBC30 with 186 mM NaCl (TBCaNa buffer). FPB releases were instead consistent with a nonstretched consecutive exponential growth function, except in TBC30 where some FPB appeared to be cleaved independently. Log-log plots of K a versus Ca 2+ concentration, Cl -concentration, or I showed a strong linear correlation with only the latter two except in TBCaNa, again suggesting specific effects of the physiological Ca 2+ concentration and I on FPA release. The corresponding K b plots showed instead that both total depletion and high Ca 2+ hampered FPB release. To further investigate the TBC2.5 ) 0.69 effect, FG polydispersity was assessed by Western blot analyses. The thrombin-binding γ′-chain isoform was ∼4%, resulting in a bound:free thrombin ratio of ∼25:75. With regard to the C-terminal ends of the AR-chains, ∼45% were either intact or lightly degraded, while the remaining ∼55% were more degraded. Fitting the % FPA release data in TBC2.5 with a sum of two exponentials resulted in a faster component and a slower component (K a1 /K a2 ≈ 6), with a ratio of ∼48:52. While a role for the γ′-chain isoform cannot be excluded, this good correlation with the C-terminal degradation of the AR-chains suggests their calcium-dependent involvement in FPA release.

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Calcium and fibrin gel structure

Cited by 77 publications

References 20 publications

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

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

Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms

Kinetics of Fibrinopeptide Release by Thrombin as a Function of CaCl₂ Concentration: Different Susceptibility of FPA and FPB and Evidence for a Fibrinogen Isoform-Specific Effect at Physiological Ca²⁺ Concentration

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Calcium and fibrin gel structure

Cited by 77 publications

References 20 publications

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

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

Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms

Kinetics of Fibrinopeptide Release by Thrombin as a Function of CaCl2 Concentration: Different Susceptibility of FPA and FPB and Evidence for a Fibrinogen Isoform-Specific Effect at Physiological Ca2+ Concentration

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Kinetics of Fibrinopeptide Release by Thrombin as a Function of CaCl₂ Concentration: Different Susceptibility of FPA and FPB and Evidence for a Fibrinogen Isoform-Specific Effect at Physiological Ca²⁺ Concentration